메뉴 건너뛰기




Volumn 1572, Issue 2-3, 2002, Pages 341-363

Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors

Author keywords

Asialoglycoprotein receptor; Coated pit; Hyaluronan receptor; Multiple endocytosis pathway; State 1 pathway; State 2 pathway

Indexed keywords

ASIALOGLYCOPROTEIN; CARBOHYDRATE; CHONDROITIN SULFATE; CLATHRIN; GALACTOSE; GLYCAN; GLYCOCONJUGATE; GLYCOPROTEIN; GLYCOSAMINOGLYCAN; HYALURONIC ACID; LECTIN; LIGAND; MEMBRANE ENZYME; N ACETYLGALACTOSAMINE; RECEPTOR; SUGAR;

EID: 0037136420     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(02)00318-5     Document Type: Review
Times cited : (201)

References (232)
  • 1
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: An historical introduction and overview
    • Kilpatrick D.C. Animal lectins: an historical introduction and overview. Biochim. Biophys. Acta. 1572:2002;187-197.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 187-197
    • Kilpatrick, D.C.1
  • 4
    • 0016322758 scopus 로고
    • The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins
    • Ashwell G., Morell A.G. The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins. Adv. Enzymol. 41:1974;99-128.
    • (1974) Adv. Enzymol. , vol.41 , pp. 99-128
    • Ashwell, G.1    Morell, A.G.2
  • 5
    • 0020021127 scopus 로고
    • Carbohydrate-specific receptors of the liver
    • Ashwell G., Harford J. Carbohydrate-specific receptors of the liver. Ann. Rev. Biochem. 51:1982;531-554.
    • (1982) Ann. Rev. Biochem. , vol.51 , pp. 531-554
    • Ashwell, G.1    Harford, J.2
  • 6
    • 0021073678 scopus 로고
    • Sorting and recycling of cell surface receptors and endocytosed ligands: The asialoglycoprotein and transferrin receptors
    • Ciechanover A., Schwartz A.L., Lodish H.F. Sorting and recycling of cell surface receptors and endocytosed ligands: the asialoglycoprotein and transferrin receptors. J. Cell. Biochem. 23:1983;107-130.
    • (1983) J. Cell. Biochem. , vol.23 , pp. 107-130
    • Ciechanover, A.1    Schwartz, A.L.2    Lodish, H.F.3
  • 7
    • 0021192483 scopus 로고
    • The hepatic asialoglycoprotein receptor
    • Schwartz A.L. The hepatic asialoglycoprotein receptor. CRC Crit. Rev. Biochem. 16:1984;207-233.
    • (1984) CRC Crit. Rev. Biochem. , vol.16 , pp. 207-233
    • Schwartz, A.L.1
  • 9
    • 0025043480 scopus 로고
    • The asialoglycoprotein receptor: A model for endocytic transport receptors
    • Spiess M. The asialoglycoprotein receptor: a model for endocytic transport receptors. Biochemistry. 29:1990;10009-10018.
    • (1990) Biochemistry , vol.29 , pp. 10009-10018
    • Spiess, M.1
  • 10
    • 0026967509 scopus 로고
    • Asialoglycoprotein receptor
    • Geffen I., Spiess M. Asialoglycoprotein receptor. Int. Rev. Cyt. 137B:1992;181-219.
    • (1992) Int. Rev. Cyt. , vol.137 B , pp. 181-219
    • Geffen, I.1    Spiess, M.2
  • 11
    • 0002517079 scopus 로고
    • Glycoconjugates composition, structure and function
    • H.J. Allen, & E.C. Kisailus. New York: Marcel Dekker
    • Weigel P.H. Glycoconjugates composition, structure and function. Allen H.J., Kisailus E.C. Mechanisms and Control of Glycoconjugate Turnover. 1992;421-497 Marcel Dekker, New York.
    • (1992) Mechanisms and Control of Glycoconjugate Turnover , pp. 421-497
    • Weigel, P.H.1
  • 12
    • 0027358217 scopus 로고
    • Endocytosis and function of the hepatic asialoglycoprotein receptor
    • Weigel P.H. Endocytosis and function of the hepatic asialoglycoprotein receptor. Subcell. Biochem. 19:1993;125-161.
    • (1993) Subcell. Biochem. , vol.19 , pp. 125-161
    • Weigel, P.H.1
  • 13
    • 0028998769 scopus 로고
    • The asialoglycoprotein receptor: Relationships between structure, function, and expression
    • Stockert R.J. The asialoglycoprotein receptor: relationships between structure, function, and expression. Physiol. Rev. 75:1995;591-609.
    • (1995) Physiol. Rev. , vol.75 , pp. 591-609
    • Stockert, R.J.1
  • 14
    • 0020685762 scopus 로고
    • Intracellular site of asialoglycoprotein receptor-ligand uncoupling: Double-label immunoelectron microscopy during receptor-mediated endocytosis
    • Geuze H.J., Slot J.W., Strous G.J.A.M., Lodish H.F., Schwartz A.L. Intracellular site of asialoglycoprotein receptor-ligand uncoupling: double-label immunoelectron microscopy during receptor-mediated endocytosis. Cell. 32:1983;277-287.
    • (1983) Cell , vol.32 , pp. 277-287
    • Geuze, H.J.1    Slot, J.W.2    Strous, G.J.A.M.3    Lodish, H.F.4    Schwartz, A.L.5
  • 15
    • 0021040348 scopus 로고
    • The pathway of the asialoglycoprotein-ligand during receptor-mediated endocytosis: A morphological study with colloidal gold/ligand in the human hepatoma cell line, Hep G2
    • Geuze H.J., Slot J.W., Strous G.J.A.M., Schwartz A.L. The pathway of the asialoglycoprotein-ligand during receptor-mediated endocytosis: a morphological study with colloidal gold/ligand in the human hepatoma cell line, Hep G2. Eur. J. Cell Biol. 32:1983;38-44.
    • (1983) Eur. J. Cell Biol. , vol.32 , pp. 38-44
    • Geuze, H.J.1    Slot, J.W.2    Strous, G.J.A.M.3    Schwartz, A.L.4
  • 16
    • 0021233676 scopus 로고
    • Intracellular receptor sorting during endocytosis: Comparative immunoelectron microscopy of multiple receptors in rat liver
    • Geuze H.J., Slot J.W., Strous G.J.A.M., Peppard J., von Figura K., Hasilik A., Schwartz A.L. Intracellular receptor sorting during endocytosis: comparative immunoelectron microscopy of multiple receptors in rat liver. Cell. 37:1984;195-204.
    • (1984) Cell , vol.37 , pp. 195-204
    • Geuze, H.J.1    Slot, J.W.2    Strous, G.J.A.M.3    Peppard, J.4    Von Figura, K.5    Hasilik, A.6    Schwartz, A.L.7
  • 17
    • 0027344590 scopus 로고
    • Oligosaccharide valency and conformation in determining binding to the asialoglycoprotein receptor of rat hepatocytes
    • Rice K.G., Lee Y.C. Oligosaccharide valency and conformation in determining binding to the asialoglycoprotein receptor of rat hepatocytes. Advan. Enzymol. Relat. Areas Mol. Biol. 66:1993;41-83.
    • (1993) Advan. Enzymol. Relat. Areas Mol. Biol. , vol.66 , pp. 41-83
    • Rice, K.G.1    Lee, Y.C.2
  • 18
    • 0018634472 scopus 로고
    • An electron microscope autoradiographic study of the carbohydrate recognition systems in rat liver: I. Distribution of 125I-ligands among the liver cell types
    • Hubbard A.L., Wilson G., Ashwell G., Stukenbrok H. An electron microscope autoradiographic study of the carbohydrate recognition systems in rat liver: I. Distribution of 125I-ligands among the liver cell types. J. Cell Biol. 83:1979;47-64.
    • (1979) J. Cell Biol. , vol.83 , pp. 47-64
    • Hubbard, A.L.1    Wilson, G.2    Ashwell, G.3    Stukenbrok, H.4
  • 19
    • 0020536404 scopus 로고
    • The large intracellular pool of asialoglycoprotein receptors functions during the endocytosis of asialoglycoproteins by isolated rat hepatocytes
    • Weigel P.H., Oka J.A. The large intracellular pool of asialoglycoprotein receptors functions during the endocytosis of asialoglycoproteins by isolated rat hepatocytes. J. Biol. Chem. 258:1983;5095-5102.
    • (1983) J. Biol. Chem. , vol.258 , pp. 5095-5102
    • Weigel, P.H.1    Oka, J.A.2
  • 21
    • 0019815676 scopus 로고
    • Galactose-specific recognition system of mammalian liver: Receptor distribution on the hepatocyte cell surface
    • Wall D.A., Hubbard A.L. Galactose-specific recognition system of mammalian liver: receptor distribution on the hepatocyte cell surface. J. Cell Biol. 90:1981;687-696.
    • (1981) J. Cell Biol. , vol.90 , pp. 687-696
    • Wall, D.A.1    Hubbard, A.L.2
  • 22
    • 0020162411 scopus 로고
    • Electron microscopic evidence for an asialoglycoprotein receptor on Kupffer cells: Localization of lectin-mediated endocytosis
    • Kolb-Bachofen V., Schlepper-Schafer J., Vogell W., Kolb H. Electron microscopic evidence for an asialoglycoprotein receptor on Kupffer cells: localization of lectin-mediated endocytosis. Cell. 29:1982;859-866.
    • (1982) Cell , vol.29 , pp. 859-866
    • Kolb-Bachofen, V.1    Schlepper-Schafer, J.2    Vogell, W.3    Kolb, H.4
  • 23
    • 0025365551 scopus 로고
    • Molecular cloning and sequence analysis of cDNA encoding the macrophage lectin specific for galactose and N-acetylgalactosamine
    • Ii M., Kurata H., Itoh N., Yamashina I., Kawasaki T. Molecular cloning and sequence analysis of cDNA encoding the macrophage lectin specific for galactose and N-acetylgalactosamine. J. Biol. Chem. 265:1990;11295-11298.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11295-11298
    • Ii, M.1    Kurata, H.2    Itoh, N.3    Yamashina, I.4    Kawasaki, T.5
  • 24
    • 0028069170 scopus 로고
    • Expression of an endogenous asialoglycoprotein receptor in a human intestinal epithelial cell line, Caco-2
    • Mu J.Z., Fallon R.J., Swanson P.E., Carroll S.B., Danaher M., Alpers D.H. Expression of an endogenous asialoglycoprotein receptor in a human intestinal epithelial cell line, Caco-2. Biochim. Biophys. Acta. 1222:1994;483-491.
    • (1994) Biochim. Biophys. Acta , vol.1222 , pp. 483-491
    • Mu, J.Z.1    Fallon, R.J.2    Swanson, P.E.3    Carroll, S.B.4    Danaher, M.5    Alpers, D.H.6
  • 25
    • 0025727545 scopus 로고
    • A mammalian sperm lectin related to rat hepatocyte lectin-2/3. Purification from rabbit testis and identification as a zona binding protein
    • Abdullah M., Widgren E.E., O'Rand M.G. A mammalian sperm lectin related to rat hepatocyte lectin-2/3. Purification from rabbit testis and identification as a zona binding protein. Mol. Cell. Biochem. 103:1991;155-161.
    • (1991) Mol. Cell. Biochem. , vol.103 , pp. 155-161
    • Abdullah, M.1    Widgren, E.E.2    O'Rand, M.G.3
  • 26
    • 0027081524 scopus 로고
    • Late-stage spermatids are characterized by expression of the "liver-specific" asialoglycoprotein receptor, RHL-1
    • Huber B.E. Late-stage spermatids are characterized by expression of the "liver-specific" asialoglycoprotein receptor, RHL-1. Mol. Pharmacol. 41:1992;639-644.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 639-644
    • Huber, B.E.1
  • 27
    • 0027944498 scopus 로고
    • The major form of the murine asialoglycoprotein receptor: CDNA sequence and expression in liver, testis and epididymis
    • Monroe R.S., Huber B.E. The major form of the murine asialoglycoprotein receptor: cDNA sequence and expression in liver, testis and epididymis. Gene. 148:1994;237-244.
    • (1994) Gene , vol.148 , pp. 237-244
    • Monroe, R.S.1    Huber, B.E.2
  • 28
    • 0028919091 scopus 로고
    • Galactosyl receptor in human testis and sperm is antigenically related to the minor C-type (Ca(2+)-dependent) lectin variant of human and rat liver
    • Goluboff E.T., Mertz J.R., Tres L.L., Kierszenbaum A.L. Galactosyl receptor in human testis and sperm is antigenically related to the minor C-type (Ca(2+)-dependent) lectin variant of human and rat liver. Mol. Reprod. Dev. 40:1995;460-466.
    • (1995) Mol. Reprod. Dev. , vol.40 , pp. 460-466
    • Goluboff, E.T.1    Mertz, J.R.2    Tres, L.L.3    Kierszenbaum, A.L.4
  • 29
    • 0032729762 scopus 로고    scopus 로고
    • Thyroglobulin binding and TSH regulation of the RHL-1 subunit of the asialoglycoprotein receptor in rat thyroid
    • Pacifico F., Liguoro D., Acquaviva R., Formisano S., Consiglio E. Thyroglobulin binding and TSH regulation of the RHL-1 subunit of the asialoglycoprotein receptor in rat thyroid. Biochimie. 81:1999;493-496.
    • (1999) Biochimie , vol.81 , pp. 493-496
    • Pacifico, F.1    Liguoro, D.2    Acquaviva, R.3    Formisano, S.4    Consiglio, E.5
  • 30
    • 0037136413 scopus 로고    scopus 로고
    • Mannan-binding lectin: Clinical significance and applications
    • Kilpatrick D.C. Mannan-binding lectin: clinical significance and applications. Biochim. Biophys. Acta. 1572:2002;401-413.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 401-413
    • Kilpatrick, D.C.1
  • 31
    • 0037136421 scopus 로고    scopus 로고
    • Collectins and ficolins: Sugar pattern recognition molecules of the mammalian innate immune system
    • Lu J., Teh C., Kishore U., Reid K.B.M. Collectins and ficolins: sugar pattern recognition molecules of the mammalian innate immune system. Biochim. Biophys. Acta. 1572:2002;387-400.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 387-400
    • Lu, J.1    Teh, C.2    Kishore, U.3    Reid, K.B.M.4
  • 32
    • 0017137316 scopus 로고
    • Carbohydrate structure of glycopeptides isolated from an hepatic membrane-binding protein specific for asialoglycoproteins
    • Kawasaki T., Ashwell G. Carbohydrate structure of glycopeptides isolated from an hepatic membrane-binding protein specific for asialoglycoproteins. J. Biol. Chem. 251:1976;5292-5299.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5292-5299
    • Kawasaki, T.1    Ashwell, G.2
  • 33
    • 0025044295 scopus 로고
    • Mouse asialoglycoprotein receptor cDNA sequence: Conservation of receptor genes during mammalian evolution
    • Sanford J.P., Doyle D. Mouse asialoglycoprotein receptor cDNA sequence: conservation of receptor genes during mammalian evolution. Biochim. Biophys. Acta. 1087:1990;259-261.
    • (1990) Biochim. Biophys. Acta , vol.1087 , pp. 259-261
    • Sanford, J.P.1    Doyle, D.2
  • 34
    • 0027511367 scopus 로고
    • Determination of mouse major asialoglycoprotein receptor cDNA sequence
    • Takezawa R., Shinzawa K., Watanabe Y., Akaike T. Determination of mouse major asialoglycoprotein receptor cDNA sequence. Biochim. Biophys. Acta. 1172:1993;220-222.
    • (1993) Biochim. Biophys. Acta , vol.1172 , pp. 220-222
    • Takezawa, R.1    Shinzawa, K.2    Watanabe, Y.3    Akaike, T.4
  • 35
    • 3042905513 scopus 로고
    • Sequence of a second human asialoglycoprotein receptor: Conservation of two receptor genes during evolution
    • Spiess M., Lodish H.F. Sequence of a second human asialoglycoprotein receptor: conservation of two receptor genes during evolution. Proc. Natl. Acad. Sci. 82:1985;6465-6569.
    • (1985) Proc. Natl. Acad. Sci. , vol.82 , pp. 6465-6569
    • Spiess, M.1    Lodish, H.F.2
  • 36
    • 0023179606 scopus 로고
    • Two asialoglycoprotein receptor polypeptides in human hepatoma cells
    • Bischoff J., Lodish H.F. Two asialoglycoprotein receptor polypeptides in human hepatoma cells. J. Biol. Chem. 262:1987;11825-11832.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11825-11832
    • Bischoff, J.1    Lodish, H.F.2
  • 37
    • 0021922288 scopus 로고
    • Sequence of human asialoglycoprotein receptor cDNA, an internal signal sequence for membrane insertion
    • Spiess M., Schwartz A.L., Lodish H.F. Sequence of human asialoglycoprotein receptor cDNA, an internal signal sequence for membrane insertion. J. Biol. Chem. 260:1985;1979-1982.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1979-1982
    • Spiess, M.1    Schwartz, A.L.2    Lodish, H.F.3
  • 38
    • 0021343204 scopus 로고
    • Primary structure of the rat liver asialoglycoprotein receptor. Structural evidence for multiple polypeptide species
    • Drickamer K., Mamon J.F., Binns G., Leung J.O. Primary structure of the rat liver asialoglycoprotein receptor. Structural evidence for multiple polypeptide species. J. Biol. Chem. 259:1984;770-778.
    • (1984) J. Biol. Chem. , vol.259 , pp. 770-778
    • Drickamer, K.1    Mamon, J.F.2    Binns, G.3    Leung, J.O.4
  • 39
    • 0025346331 scopus 로고
    • Surface and internal galactosyl receptors are heterooligomers and retain this structure after ligand internalization or receptor modulation
    • Herzig M.C.S., Weigel P.H. Surface and internal galactosyl receptors are heterooligomers and retain this structure after ligand internalization or receptor modulation. Biochemistry. 10:1990;6437-6447.
    • (1990) Biochemistry , vol.10 , pp. 6437-6447
    • Herzig, M.C.S.1    Weigel, P.H.2
  • 40
    • 0021721888 scopus 로고
    • Direct evidence for the transmembrane orientation of the hepatic glycoprotein receptors
    • Chiacchia K.B., Drickamer K. Direct evidence for the transmembrane orientation of the hepatic glycoprotein receptors. J. Biol. Chem. 259:1984;15440-15446.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15440-15446
    • Chiacchia, K.B.1    Drickamer, K.2
  • 41
    • 0026559111 scopus 로고
    • Differences in the abundance of variably spliced transcripts for the second asialoglycoprotein receptor polypeptide, H2, in normal and transformed human liver
    • Paietta E., Stockert R.J., Racevskis J. Differences in the abundance of variably spliced transcripts for the second asialoglycoprotein receptor polypeptide, H2, in normal and transformed human liver. Hepatology. 15:1992;395-402.
    • (1992) Hepatology , vol.15 , pp. 395-402
    • Paietta, E.1    Stockert, R.J.2    Racevskis, J.3
  • 42
    • 0030001518 scopus 로고    scopus 로고
    • Membrane-bound versus secreted forms of human asialoglycoprotein receptor subunits. Role of a juxtamembrane pentapeptide
    • Tolchinsky S., Yuk M.H., Ayalon M., Lodish H.F., Lederkremer G.Z. Membrane-bound versus secreted forms of human asialoglycoprotein receptor subunits. Role of a juxtamembrane pentapeptide. J. Biol. Chem. 271:1996;14496-14503.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14496-14503
    • Tolchinsky, S.1    Yuk, M.H.2    Ayalon, M.3    Lodish, H.F.4    Lederkremer, G.Z.5
  • 43
    • 0028930061 scopus 로고
    • Detection and quantification of soluble asialoglycoprotein receptor in human serum
    • Yago H., Kohgo Y., Kato J., Watanabe N., Sakamaki S., Niitsu Y. Detection and quantification of soluble asialoglycoprotein receptor in human serum. Hepatology. 21:1995;383-388.
    • (1995) Hepatology , vol.21 , pp. 383-388
    • Yago, H.1    Kohgo, Y.2    Kato, J.3    Watanabe, N.4    Sakamaki, S.5    Niitsu, Y.6
  • 44
    • 0037151117 scopus 로고    scopus 로고
    • The minor subunit splice variants, H2b and H2c, of the human asialoglycoprotein receptor are present with the major subunit H1 in different hetero-oligomeric receptor complexes
    • Yik J.H.N., Saxena A., Weigel P.H. The minor subunit splice variants, H2b and H2c, of the human asialoglycoprotein receptor are present with the major subunit H1 in different hetero-oligomeric receptor complexes. J. Biol. Chem. 277:2002;23076-23082.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23076-23082
    • Yik, J.H.N.1    Saxena, A.2    Weigel, P.H.3
  • 45
    • 0021264739 scopus 로고
    • Influence of the N-linked oligosaccharides on the biosynthesis, intracellular routing, and function of the human asialoglycoprotein receptor
    • Breitfeld P.P., Rup D., Schwartz A.L. Influence of the N-linked oligosaccharides on the biosynthesis, intracellular routing, and function of the human asialoglycoprotein receptor. J. Biol. Chem. 259:1984;10414-10421.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10414-10421
    • Breitfeld, P.P.1    Rup, D.2    Schwartz, A.L.3
  • 46
    • 0022998706 scopus 로고
    • The rat liver asialoglycoprotein receptor polypeptide must be inserted into a microsome to achieve its active conformation
    • Hsueh E.C., Holland E.C., Carrera G.M. Jr., Drickamer K. The rat liver asialoglycoprotein receptor polypeptide must be inserted into a microsome to achieve its active conformation. J. Biol. Chem. 261:1986;4940-4947.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4940-4947
    • Hsueh, E.C.1    Holland, E.C.2    Carrera G.M., Jr.3    Drickamer, K.4
  • 47
    • 0017757107 scopus 로고
    • Reactivation of asialo-rabbit liver binding protein by resialylation with beta-D-galactoside α2→6 sialyltransferase
    • Paulson J.C., Hill R.L., Tanabe T., Ashwell G. Reactivation of asialo-rabbit liver binding protein by resialylation with beta-D-galactoside α2→6 sialyltransferase. J. Biol. Chem. 252:1977;8624-8628.
    • (1977) J. Biol. Chem. , vol.252 , pp. 8624-8628
    • Paulson, J.C.1    Hill, R.L.2    Tanabe, T.3    Ashwell, G.4
  • 48
    • 0017773087 scopus 로고
    • Hepatic binding protein: The protective role of its sialic acid residues
    • Stockert R.J., Morell A.G., Scheinberg I.H. Hepatic binding protein: the protective role of its sialic acid residues. Science. 197:1977;667-668.
    • (1977) Science , vol.197 , pp. 667-668
    • Stockert, R.J.1    Morell, A.G.2    Scheinberg, I.H.3
  • 49
    • 0025217276 scopus 로고
    • Tyrosine phosphorylation of the asialoglycoprotein receptor
    • Fallon R.J. Tyrosine phosphorylation of the asialoglycoprotein receptor. J. Biol. Chem. 265:1990;3401-3406.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3401-3406
    • Fallon, R.J.1
  • 50
    • 0028577264 scopus 로고
    • The rat hepatic lectin 1 subunit of the rat asialoglycoprotein receptor is a phosphoprotein and contains phosphotyrosine
    • Haynes P.A., Oka J.A., Weigel P.H. The rat hepatic lectin 1 subunit of the rat asialoglycoprotein receptor is a phosphoprotein and contains phosphotyrosine. J. Biol. Chem. 269:1994;33146-33151.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33146-33151
    • Haynes, P.A.1    Oka, J.A.2    Weigel, P.H.3
  • 51
    • 0026058910 scopus 로고
    • In vitro binding of the asialoglycoprotein receptor to the beta adaptin of plasma membrane coated vesicles
    • Beltzer J.P., Spiess M. In vitro binding of the asialoglycoprotein receptor to the beta adaptin of plasma membrane coated vesicles. EMBO J. 10:1991;3735-3742.
    • (1991) EMBO J. , vol.10 , pp. 3735-3742
    • Beltzer, J.P.1    Spiess, M.2
  • 52
    • 0025738178 scopus 로고
    • Endocytosis of the ASGP receptor H1 is reduced by mutation of tyrosine-5 but still occurs via coated pits
    • Fuhrer C., Geffen I., Spiess M. Endocytosis of the ASGP receptor H1 is reduced by mutation of tyrosine-5 but still occurs via coated pits. J. Cell Biol. 114:1991;423-431.
    • (1991) J. Cell Biol. , vol.114 , pp. 423-431
    • Fuhrer, C.1    Geffen, I.2    Spiess, M.3
  • 53
    • 0028029794 scopus 로고
    • The asialoglycoprotein receptor is associated with a tyrosine kinase in HepG2 cells
    • Fallon R.J., Danaher M., Saxena A. The asialoglycoprotein receptor is associated with a tyrosine kinase in HepG2 cells. J. Biol. Chem. 269:1994;26626-26629.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26626-26629
    • Fallon, R.J.1    Danaher, M.2    Saxena, A.3
  • 54
    • 0035193121 scopus 로고    scopus 로고
    • C-src tyrosine kinase is associated with the asialoglycoprotein receptor in human hepatoma cells
    • Parker A., Fallon R.J. c-src tyrosine kinase is associated with the asialoglycoprotein receptor in human hepatoma cells. Mol. Cell. Biol. Res. Commun. 4:2001;331-336.
    • (2001) Mol. Cell. Biol. Res. Commun. , vol.4 , pp. 331-336
    • Parker, A.1    Fallon, R.J.2
  • 55
  • 56
    • 0028556894 scopus 로고
    • Inhibition of tyrosine phosphorylation in the rat hepatic lectin 1 subunit of the rat asialoglycoprotein receptor prevents ATP-dependent receptor inactivation in permeabilized hepatocytes
    • Haynes P.A., Medh J.D., Weigel P.H. Inhibition of tyrosine phosphorylation in the rat hepatic lectin 1 subunit of the rat asialoglycoprotein receptor prevents ATP-dependent receptor inactivation in permeabilized hepatocytes. J. Biol. Chem. 269:1994;33152-33158.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33152-33158
    • Haynes, P.A.1    Medh, J.D.2    Weigel, P.H.3
  • 57
    • 0028023783 scopus 로고
    • The two subunits of the asialoglycoprotein receptor contain different sorting information
    • Fuhrer C., Geffen I., Huggel K., Spiess M. The two subunits of the asialoglycoprotein receptor contain different sorting information. J. Biol. Chem. 269:1994;3277-3282.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3277-3282
    • Fuhrer, C.1    Geffen, I.2    Huggel, K.3    Spiess, M.4
  • 58
    • 0021209884 scopus 로고
    • Phosphorylation of the human asialoglycoprotein receptor
    • Schwartz A.L. Phosphorylation of the human asialoglycoprotein receptor. Biochem. J. 223:1984;481-486.
    • (1984) Biochem. J. , vol.223 , pp. 481-486
    • Schwartz, A.L.1
  • 60
    • 0023802461 scopus 로고
    • Asialoglycoprotein receptor phosphorylation and receptor-mediated endocytosis in hepatoma cells. Effect of phorbol esters
    • Fallon R.J., Schwartz A.L. Asialoglycoprotein receptor phosphorylation and receptor-mediated endocytosis in hepatoma cells. Effect of phorbol esters. J. Biol. Chem. 263:1988;13159-13166.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13159-13166
    • Fallon, R.J.1    Schwartz, A.L.2
  • 61
    • 0026049579 scopus 로고
    • Endocytosis by the asialoglycoprotein receptor is independent of cytoplasmic serine residues
    • Geffen I., Fuhrer C., Spiess M. Endocytosis by the asialoglycoprotein receptor is independent of cytoplasmic serine residues. Proc. Natl. Acad. Sci. U. S. A. 88:1991;8425-8429.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 8425-8429
    • Geffen, I.1    Fuhrer, C.2    Spiess, M.3
  • 62
    • 0026686365 scopus 로고
    • Alternatively spliced variants of the human hepatic asialoglycoprotein receptor, H2, differ in cellular trafficking and regulation of phosphorylation
    • Paietta E., Stockert R.J., Racevskis J. Alternatively spliced variants of the human hepatic asialoglycoprotein receptor, H2, differ in cellular trafficking and regulation of phosphorylation. J. Biol. Chem. 267:1992;11078-11084.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11078-11084
    • Paietta, E.1    Stockert, R.J.2    Racevskis, J.3
  • 63
    • 0029096545 scopus 로고
    • Fatty acylation of the rat asialoglycoprotein receptor. The three subunits from active receptors contain covalently bound palmitate and stearate
    • Zeng F.-Y., Kaphalia B.S., Ansari G.A.S., Weigel P.H. Fatty acylation of the rat asialoglycoprotein receptor. The three subunits from active receptors contain covalently bound palmitate and stearate. J. Biol. Chem. 270:1995;21382-21387.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21382-21387
    • Zeng, F.-Y.1    Kaphalia, B.S.2    Ansari, G.A.S.3    Weigel, P.H.4
  • 64
    • 0029096547 scopus 로고
    • Hydroxylamine treatment differentially inactivates purified rat hepatic asialoglycoprotein receptors and distinguishes two receptor populations
    • Zeng F.-Y., Weigel P.H. Hydroxylamine treatment differentially inactivates purified rat hepatic asialoglycoprotein receptors and distinguishes two receptor populations. J. Biol. Chem. 270:1995;21388-21395.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21388-21395
    • Zeng, F.-Y.1    Weigel, P.H.2
  • 65
    • 0029753239 scopus 로고    scopus 로고
    • Fatty acylation of the rat and human asialoglycoprotein receptors. A conserved cytoplasmic cysteine residue is acylated in all receptor subunits
    • Zeng F.-Y., Weigel P.H. Fatty acylation of the rat and human asialoglycoprotein receptors. A conserved cytoplasmic cysteine residue is acylated in all receptor subunits. J. Biol. Chem. 271:1996;32454-32460.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32454-32460
    • Zeng, F.-Y.1    Weigel, P.H.2
  • 66
    • 0001374628 scopus 로고    scopus 로고
    • Characterization of palmitoylation-defective human asialoglycoprotein receptor
    • Saxena A., Yik J.H.N., Weigel J.A., Weigel P.H. Characterization of palmitoylation-defective human asialoglycoprotein receptor. Mol. Biol. Cell. 12S:2001;215a.
    • (2001) Mol. Biol. Cell , vol.12 S
    • Saxena, A.1    Yik, J.H.N.2    Weigel, J.A.3    Weigel, P.H.4
  • 67
    • 0030034339 scopus 로고    scopus 로고
    • Ca(2+)-dependent sugar recognition by animal lectins
    • Drickamer K. Ca(2+)-dependent sugar recognition by animal lectins. Biochem. Soc. Trans. 24:1996;146-150.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 146-150
    • Drickamer, K.1
  • 68
    • 0028196754 scopus 로고
    • The C-type carbohydrate recognition domain (CRD) superfamily
    • Day A.J. The C-type carbohydrate recognition domain (CRD) superfamily. Biochem. Soc. Trans. 22:1994;83-88.
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 83-88
    • Day, A.J.1
  • 69
    • 0033805014 scopus 로고    scopus 로고
    • Lectin-mediated drug targeting: Selection of valency, sugar type (Gal/Lac), and spacer length for cluster glycosides as parameters to distinguish ligand binding to C-type asialoglycoprotein receptors and galectins
    • Andre S., Frisch B., Kaltner H., Desouza D.L., Schuber F., Gabius H.J. Lectin-mediated drug targeting: selection of valency, sugar type (Gal/Lac), and spacer length for cluster glycosides as parameters to distinguish ligand binding to C-type asialoglycoprotein receptors and galectins. Pharm. Res. 17:2000;985-990.
    • (2000) Pharm. Res. , vol.17 , pp. 985-990
    • Andre, S.1    Frisch, B.2    Kaltner, H.3    Desouza, D.L.4    Schuber, F.5    Gabius, H.J.6
  • 70
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: A lesson in complexity
    • Cooper D.N.W. Galectinomics: a lesson in complexity. Biochim. Biophys. Acta. 1572:2002;209-231.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 72
    • 0037136412 scopus 로고    scopus 로고
    • Binding and cross-linking properties of galectins
    • Brewer C.F., Dam T.K. Binding and cross-linking properties of galectins. Biochim. Biophys. Acta. 1572:2002;255-262.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 255-262
    • Brewer, C.F.1    Dam, T.K.2
  • 74
    • 0037136408 scopus 로고    scopus 로고
    • Role of galectins in inflammatory and immunomodulatory processes
    • Rabinovich G.A., Rubinstein N., Toscano M. Role of galectins in inflammatory and immunomodulatory processes. Biochim. Biophys. Acta. 1572:2002;274-284.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 274-284
    • Rabinovich, G.A.1    Rubinstein, N.2    Toscano, M.3
  • 77
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis W.I., Drickamer K., Hendrickson W.A. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature. 360:1992;127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 78
    • 0030069340 scopus 로고    scopus 로고
    • Structural analysis of monosaccharide recognition by rat liver mannose-binding protein
    • Ng K.K., Drickamer K., Weis W.I. Structural analysis of monosaccharide recognition by rat liver mannose-binding protein. J. Biol. Chem. 271:1996;663-674.
    • (1996) J. Biol. Chem. , vol.271 , pp. 663-674
    • Ng, K.K.1    Drickamer, K.2    Weis, W.I.3
  • 79
    • 0021999255 scopus 로고
    • Different modes of ligand binding to the hepatic galactose/N-acetylgalactosamine lectin on the surface of rabbit hepatocytes
    • Hardy M.R., Townsend R.R., Parkhurst S.M., Lee Y.C. Different modes of ligand binding to the hepatic galactose/N-acetylgalactosamine lectin on the surface of rabbit hepatocytes. Biochemistry. 24:1985;22-28.
    • (1985) Biochemistry , vol.24 , pp. 22-28
    • Hardy, M.R.1    Townsend, R.R.2    Parkhurst, S.M.3    Lee, Y.C.4
  • 80
    • 0034697981 scopus 로고    scopus 로고
    • Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor
    • Meier M., Bider M.D., Malashkevich V.N., Spiess M., Burkhard P. Crystal structure of the carbohydrate recognition domain of the H1 subunit of the asialoglycoprotein receptor. J. Mol. Biol. 300:2000;857-865.
    • (2000) J. Mol. Biol. , vol.300 , pp. 857-865
    • Meier, M.1    Bider, M.D.2    Malashkevich, V.N.3    Spiess, M.4    Burkhard, P.5
  • 81
    • 0037136417 scopus 로고    scopus 로고
    • Principles of structures of animal and plant lectins
    • Loris R. Principles of structures of animal and plant lectins. Biochim. Biophys. Acta. 1572:2002;198-208.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 198-208
    • Loris, R.1
  • 82
    • 0026439234 scopus 로고
    • Engineering galactose-binding activity into a C-type mannose-binding protein
    • Drickamer K. Engineering galactose-binding activity into a C-type mannose-binding protein. Nature. 360:1992;183-186.
    • (1992) Nature , vol.360 , pp. 183-186
    • Drickamer, K.1
  • 83
    • 0029917167 scopus 로고    scopus 로고
    • Structural basis of galactose recognition by C-type animal lectins
    • Kolatkar A.R., Weis W.I. Structural basis of galactose recognition by C-type animal lectins. J. Biol. Chem. 271:1996;6679-6685.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6679-6685
    • Kolatkar, A.R.1    Weis, W.I.2
  • 84
    • 0024477287 scopus 로고
    • Synthesis and characterization of N-hydroxysuccinimide ester chemical affinity derivatives of asialoorosomucoid that covalently cross-link to galactosyl receptors on isolated rat hepatocytes
    • Herzig M.C.S., Weigel P.H. Synthesis and characterization of N-hydroxysuccinimide ester chemical affinity derivatives of asialoorosomucoid that covalently cross-link to galactosyl receptors on isolated rat hepatocytes. Biochemistry. 28:1989;600-610.
    • (1989) Biochemistry , vol.28 , pp. 600-610
    • Herzig, M.C.S.1    Weigel, P.H.2
  • 85
    • 0023691069 scopus 로고
    • Identification of a complex of the three forms of the rat liver asialoglycoprotein receptor
    • Sawyer J.T., Sanford J.P., Doyle D. Identification of a complex of the three forms of the rat liver asialoglycoprotein receptor. J. Biol. Chem. 263:1988;10534-10538.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10534-10538
    • Sawyer, J.T.1    Sanford, J.P.2    Doyle, D.3
  • 86
    • 0025162458 scopus 로고
    • Functional galactosyl receptors on isolated rat hepatocytes are hetero-oligomers
    • Oka J.A., Herzig M.C.S., Weigel P.H. Functional galactosyl receptors on isolated rat hepatocytes are hetero-oligomers. Biochem. Biophys. Res. Commun. 170:1990;1308-1313.
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 1308-1313
    • Oka, J.A.1    Herzig, M.C.S.2    Weigel, P.H.3
  • 87
    • 0023890608 scopus 로고
    • The H1 and H2 polypeptides associate to form the asialoglycoprotein receptor in human hepatoma cells
    • Bischoff J., Libresco S., Shia M.A., Lodish H.F. The H1 and H2 polypeptides associate to form the asialoglycoprotein receptor in human hepatoma cells. J. Cell Biol. 106:1988;1067-1074.
    • (1988) J. Cell Biol. , vol.106 , pp. 1067-1074
    • Bischoff, J.1    Libresco, S.2    Shia, M.A.3    Lodish, H.F.4
  • 88
    • 0022878963 scopus 로고
    • Formation of functional asialoglycoprotein receptor after transfection with cDNAs encoding the receptor proteins
    • McPhaul M., Berg P. Formation of functional asialoglycoprotein receptor after transfection with cDNAs encoding the receptor proteins. Proc. Natl. Acad. Sci. U. S. A. 83:1986;8863-8867.
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 8863-8867
    • McPhaul, M.1    Berg, P.2
  • 90
    • 0029731789 scopus 로고    scopus 로고
    • The oligomerization domain of the asialoglycoprotein receptor preferentially forms 2:2 heterotetramers in vitro
    • Bider M.D., Wahlberg J.M., Kammerer R.A., Spiess M. The oligomerization domain of the asialoglycoprotein receptor preferentially forms 2:2 heterotetramers in vitro. J. Biol. Chem. 271:1996;31996-32001.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31996-32001
    • Bider, M.D.1    Wahlberg, J.M.2    Kammerer, R.A.3    Spiess, M.4
  • 91
    • 0025285229 scopus 로고
    • Assembly of a heterooligomeric asialoglycoprotein receptor complex during cell-free translation
    • Sawyer J.T., Doyle D. Assembly of a heterooligomeric asialoglycoprotein receptor complex during cell-free translation. Proc. Natl. Acad. Sci. 87:1990;4854-4858.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 4854-4858
    • Sawyer, J.T.1    Doyle, D.2
  • 92
    • 0020490884 scopus 로고
    • Physical studies on the rabbit hepatic galactoside-binding protein. Effects of calcium and ligands
    • Andersen T.T., Freytag J.W., Hill R.L. Physical studies on the rabbit hepatic galactoside-binding protein. Effects of calcium and ligands. J. Biol. Chem. 257:1982;8036-8041.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8036-8041
    • Andersen, T.T.1    Freytag, J.W.2    Hill, R.L.3
  • 93
    • 0019876970 scopus 로고
    • Molecular size of the hepatic receptor for asialoglycoproteins determined in situ by radiation inactivation
    • Steer C.J., Kempner E.S., Ashwell G. Molecular size of the hepatic receptor for asialoglycoproteins determined in situ by radiation inactivation. J. Biol. Chem. 256:1981;5851-5856.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5851-5856
    • Steer, C.J.1    Kempner, E.S.2    Ashwell, G.3
  • 94
    • 0021160132 scopus 로고
    • Functional size of the human asialoglycoprotein receptor as determined by radiation inactivation
    • Schwartz A.L., Steer C.J., Kempner E.S. Functional size of the human asialoglycoprotein receptor as determined by radiation inactivation. J. Biol. Chem. 259:1984;12025-12029.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12025-12029
    • Schwartz, A.L.1    Steer, C.J.2    Kempner, E.S.3
  • 95
    • 0025145108 scopus 로고
    • Oligomeric structure of the human asialoglycoprotein receptor: Nature and stoichiometry of mutual complexes containing H1 and H2 polypeptides assessed by fluorescence photobleaching recovery
    • Henis Y.I., Katzir Z., Shia M.A., Lodish H.F. Oligomeric structure of the human asialoglycoprotein receptor: nature and stoichiometry of mutual complexes containing H1 and H2 polypeptides assessed by fluorescence photobleaching recovery. J. Cell Biol. 111:1990;1409-1418.
    • (1990) J. Cell Biol. , vol.111 , pp. 1409-1418
    • Henis, Y.I.1    Katzir, Z.2    Shia, M.A.3    Lodish, H.F.4
  • 96
    • 0029841498 scopus 로고    scopus 로고
    • Differential ligand binding by two subunits of the rat liver asialoglycoprotein receptor
    • Ruiz N.I., Drickamer K. Differential ligand binding by two subunits of the rat liver asialoglycoprotein receptor. Glycobiology. 6:1996;551-559.
    • (1996) Glycobiology , vol.6 , pp. 551-559
    • Ruiz, N.I.1    Drickamer, K.2
  • 97
    • 0023655646 scopus 로고
    • Major and minor forms of the rat liver asialoglycoprotein receptor are independent galactose-binding proteins. Primary structure and glycosylation heterogeneity of minor receptor forms
    • Halberg D.F., Wager R.E., Farrell D.C., Hildreth J. 4th, Quesenberry M.S., Loeb J.A., Holland E.C., Drickamer K. Major and minor forms of the rat liver asialoglycoprotein receptor are independent galactose-binding proteins. Primary structure and glycosylation heterogeneity of minor receptor forms. J. Biol. Chem. 262:1987;9828-9838.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9828-9838
    • Halberg, D.F.1    Wager, R.E.2    Farrell, D.C.3    Hildreth J. IV4    Quesenberry, M.S.5    Loeb, J.A.6    Holland, E.C.7    Drickamer, K.8
  • 98
    • 0029032449 scopus 로고
    • High-affinity ligand binding to subunit H1 of the asialoglycoprotein receptor in the absence of subunit H2
    • Bider M.D., Cescato R., Jeno P., Spiess M. High-affinity ligand binding to subunit H1 of the asialoglycoprotein receptor in the absence of subunit H2. Eur. J. Biochem. 230:1995;207-212.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 207-212
    • Bider, M.D.1    Cescato, R.2    Jeno, P.3    Spiess, M.4
  • 99
    • 0037144593 scopus 로고    scopus 로고
    • H2, the minor subunit of the human asialoglycoprotein receptor, trafficks intracellularly and forms homo-oligomers, but does not bind asialo-orosomucoid
    • in press
    • Saxena A., Yik J.H.N., Weigel P.H. H2, the minor subunit of the human asialoglycoprotein receptor, trafficks intracellularly and forms homo-oligomers, but does not bind asialo-orosomucoid. J. Biol. Chem. 277:2002;. in press.
    • (2002) J. Biol. Chem. , vol.277
    • Saxena, A.1    Yik, J.H.N.2    Weigel, P.H.3
  • 100
    • 0029937349 scopus 로고    scopus 로고
    • Renaturation and ligand blotting of the major subunit of the rat asialoglycoprotein receptor after denaturing polyacrylamide gel electrophoresis
    • Zeng F.-Y., Oka J.A., Weigel P.H. Renaturation and ligand blotting of the major subunit of the rat asialoglycoprotein receptor after denaturing polyacrylamide gel electrophoresis. Glycobiology. 1996;247-255.
    • (1996) Glycobiology , pp. 247-255
    • Zeng, F.-Y.1    Oka, J.A.2    Weigel, P.H.3
  • 101
    • 0031693811 scopus 로고    scopus 로고
    • Identification and analysis of a Ca(2+)-dependent lactoferrin receptor in rat liver. Lactoferrin binds to the asialoglycoprotein receptor in a galactose-independent manner
    • McAbee D.D., Bennatt D.J., Ling Y.Y. Identification and analysis of a Ca(2+)-dependent lactoferrin receptor in rat liver. Lactoferrin binds to the asialoglycoprotein receptor in a galactose-independent manner. Adv. Exp. Med. Biol. 443:1998;113-121.
    • (1998) Adv. Exp. Med. Biol. , vol.443 , pp. 113-121
    • McAbee, D.D.1    Bennatt, D.J.2    Ling, Y.Y.3
  • 102
    • 0034657165 scopus 로고    scopus 로고
    • Lactoferrin binding to the rat asialoglycoprotein receptor requires the receptor's lectin properties
    • McAbee D.D., Jiang X., Walsh K.B. Lactoferrin binding to the rat asialoglycoprotein receptor requires the receptor's lectin properties. Biochem. J. 348:2000;113-117.
    • (2000) Biochem. J. , vol.348 , pp. 113-117
    • McAbee, D.D.1    Jiang, X.2    Walsh, K.B.3
  • 103
    • 0019257349 scopus 로고
    • Rat hepatocytes bind to synthetic galactoside surfaces via a patch of asialoglycoprotein receptors
    • Weigel P.H. Rat hepatocytes bind to synthetic galactoside surfaces via a patch of asialoglycoprotein receptors. J. Cell Biol. 87:1980;855-861.
    • (1980) J. Cell Biol. , vol.87 , pp. 855-861
    • Weigel, P.H.1
  • 104
    • 0022977706 scopus 로고
    • Binding and spreading of hepatocytes on synthetic galactose culture surfaces occur as distinct and separable threshold responses
    • Oka J.A., Weigel P.H. Binding and spreading of hepatocytes on synthetic galactose culture surfaces occur as distinct and separable threshold responses. J. Cell Biol. 103:1986;1055-1060.
    • (1986) J. Cell Biol. , vol.103 , pp. 1055-1060
    • Oka, J.A.1    Weigel, P.H.2
  • 105
    • 0025847767 scopus 로고
    • The human asialoglycoprotein receptor is a possible binding site for low-density lipoproteins and chylomicron remnants
    • Windler E., Greeve J., Levkau B., Kolb-Bachofen V., Daerr W., Greten H. The human asialoglycoprotein receptor is a possible binding site for low-density lipoproteins and chylomicron remnants. Biochem. J. 276:1991;79-87.
    • (1991) Biochem. J. , vol.276 , pp. 79-87
    • Windler, E.1    Greeve, J.2    Levkau, B.3    Kolb-Bachofen, V.4    Daerr, W.5    Greten, H.6
  • 106
    • 0031903843 scopus 로고    scopus 로고
    • Circulating cellular fibronectin may be a natural ligand for the hepatic asialoglycoprotein receptor: Possible pathway for fibronectin deposition and turnover in the rat liver
    • Rotundo R.F., Rebres R.A., McKeown-Longo P.J., Bluemenstock F.A., Saba T.M. Circulating cellular fibronectin may be a natural ligand for the hepatic asialoglycoprotein receptor: possible pathway for fibronectin deposition and turnover in the rat liver. Hepatology. 28:1998;475-485.
    • (1998) Hepatology , vol.28 , pp. 475-485
    • Rotundo, R.F.1    Rebres, R.A.2    McKeown-Longo, P.J.3    Bluemenstock, F.A.4    Saba, T.M.5
  • 108
    • 0024603306 scopus 로고
    • Hepatic asialoglycoprotein receptor-mediated binding of human polymeric immunoglobulin A
    • Daniels C.K., Schmucker D.L., Jones A.L. Hepatic asialoglycoprotein receptor-mediated binding of human polymeric immunoglobulin A. Hepatology. 9:1989;229-234.
    • (1989) Hepatology , vol.9 , pp. 229-234
    • Daniels, C.K.1    Schmucker, D.L.2    Jones, A.L.3
  • 109
    • 0034686416 scopus 로고    scopus 로고
    • The N-glycans determine the differential blood clearance and hepatic uptake of human immunoglobulin (Ig)A1 and IgA2 isotypes
    • Rifai A., Fadden K., Morrison S.L., Chintalacharuvu K.R. The N-glycans determine the differential blood clearance and hepatic uptake of human immunoglobulin (Ig)A1 and IgA2 isotypes. J. Exp. Med. 191:2000;2171-2182.
    • (2000) J. Exp. Med. , vol.191 , pp. 2171-2182
    • Rifai, A.1    Fadden, K.2    Morrison, S.L.3    Chintalacharuvu, K.R.4
  • 110
    • 0026316609 scopus 로고
    • IgG is associated with the asialoglycoprotein receptor in the human liver
    • Inamoto T., Brown W.R. IgG is associated with the asialoglycoprotein receptor in the human liver. Hepatology. 14:1991;1070-1075.
    • (1991) Hepatology , vol.14 , pp. 1070-1075
    • Inamoto, T.1    Brown, W.R.2
  • 111
    • 0016151382 scopus 로고
    • Studies of the metabolism of asialotransferrins: Evidence that transferrin does not undergo desialylation in vivo
    • Wong K.-L., Charlwood P.A., Hatton M.W.C., Regoeczi E. Studies of the metabolism of asialotransferrins: evidence that transferrin does not undergo desialylation in vivo. Clin. Sci. Mol. Med. 46:1974;763-774.
    • (1974) Clin. Sci. Mol. Med. , vol.46 , pp. 763-774
    • Wong, K.-L.1    Charlwood, P.A.2    Hatton, M.W.C.3    Regoeczi, E.4
  • 112
    • 0020730902 scopus 로고
    • Asialoglycoprotein receptor is uninvolved in clearing intact glycoproteins from rat blood
    • Clarenburg R. Asialoglycoprotein receptor is uninvolved in clearing intact glycoproteins from rat blood. Am. J. Physiol. 244:1983;G247-G253.
    • (1983) Am. J. Physiol. , vol.244
    • Clarenburg, R.1
  • 113
    • 0025834944 scopus 로고
    • Prothrombin plasma clearance is not mediated by hepatic asialoglycoprotein receptors
    • Vostal J.G., McCauley R.B. Prothrombin plasma clearance is not mediated by hepatic asialoglycoprotein receptors. Thromb. Res. 63:1991;299-309.
    • (1991) Thromb. Res. , vol.63 , pp. 299-309
    • Vostal, J.G.1    McCauley, R.B.2
  • 114
    • 0028043948 scopus 로고
    • Asialoglycoprotein receptor deficiency in mice lacking the minor receptor subunit
    • Ishibashi S., Hammer R.E., Herz J. Asialoglycoprotein receptor deficiency in mice lacking the minor receptor subunit. J. Biol. Chem. 269:1994;27803-27806.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27803-27806
    • Ishibashi, S.1    Hammer, R.E.2    Herz, J.3
  • 115
    • 0029831383 scopus 로고    scopus 로고
    • The major subunit of the asialoglycoprotein receptor is expressed on the hepatocellular surface in mice lacking the minor receptor subunit
    • Braun J.R., Willnow T.E., Ishibashi S., Ashwell G., Herz J. The major subunit of the asialoglycoprotein receptor is expressed on the hepatocellular surface in mice lacking the minor receptor subunit. J. Biol. Chem. 271:1996;21160-21166.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21160-21166
    • Braun, J.R.1    Willnow, T.E.2    Ishibashi, S.3    Ashwell, G.4    Herz, J.5
  • 117
    • 0023867460 scopus 로고
    • Receptor-mediated binding and uptake of immunoglobulin A by human liver
    • Tomana M., Kulhavy R., Mestecky J. Receptor-mediated binding and uptake of immunoglobulin A by human liver. Gastroenterology. 94:1988;762-770.
    • (1988) Gastroenterology , vol.94 , pp. 762-770
    • Tomana, M.1    Kulhavy, R.2    Mestecky, J.3
  • 118
    • 0028467037 scopus 로고
    • Galactosyl and N-acetylgalactosaminyl homeostasis: A function for mammalian asialoglycoprotein receptors
    • Weigel P.H. Galactosyl and N-acetylgalactosaminyl homeostasis: a function for mammalian asialoglycoprotein receptors. BioEssays. 16:1994;519-524.
    • (1994) BioEssays , vol.16 , pp. 519-524
    • Weigel, P.H.1
  • 119
    • 0021471706 scopus 로고
    • Dissociation of clathrin coats coupled to the hydrolysis of ATP: Role of an uncoating ATPase
    • Braell W.A., Schlossman D.M., Schmid S.L., Rothman J.E. Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase. J. Cell Biol. 99:1984;734-741.
    • (1984) J. Cell Biol. , vol.99 , pp. 734-741
    • Braell, W.A.1    Schlossman, D.M.2    Schmid, S.L.3    Rothman, J.E.4
  • 120
    • 0022052012 scopus 로고
    • Immunoelectron microscopic localization of acidic intracellular compartments in hepatoma cells
    • Schwartz A.L., Strous G.J., Slot J.W., Geuze H.J. Immunoelectron microscopic localization of acidic intracellular compartments in hepatoma cells. EMBO J. 4:1985;899-904.
    • (1985) EMBO J. , vol.4 , pp. 899-904
    • Schwartz, A.L.1    Strous, G.J.2    Slot, J.W.3    Geuze, H.J.4
  • 121
    • 4243615134 scopus 로고    scopus 로고
    • Influence of vacuolar proton pump inhibitor BafilomycinA1 on intracellular processing of receptor-mediated and fluid phase endocytosis markers
    • Melikova M.S., Blagoveshchenskaya A.D., Nikolsky N.N., Kornilova E.S. Influence of vacuolar proton pump inhibitor BafilomycinA1 on intracellular processing of receptor-mediated and fluid phase endocytosis markers. Mol. Biol. Cell. 12S:2001;344a.
    • (2001) Mol. Biol. Cell , vol.12 S
    • Melikova, M.S.1    Blagoveshchenskaya, A.D.2    Nikolsky, N.N.3    Kornilova, E.S.4
  • 122
    • 4243882100 scopus 로고    scopus 로고
    • PH independent sorting and recycling of the chemokine receptor CCR5
    • Signoret N., Pelchen-Matthews A., Marsh M. pH independent sorting and recycling of the chemokine receptor CCR5. Mol. Biol. Cell. 12S:2001;253a.
    • (2001) Mol. Biol. Cell , vol.12 S
    • Signoret, N.1    Pelchen-Matthews, A.2    Marsh, M.3
  • 124
    • 0029013998 scopus 로고
    • Interaction of the microtubule cytoskeleton with endocytic vesicles and cytoplasmic dynein in cultured rat hepatocytes
    • Oda H., Stockert R.J., Collins C., Wang H., Novikoff P.M., Satir P., Wolkoff A.W. Interaction of the microtubule cytoskeleton with endocytic vesicles and cytoplasmic dynein in cultured rat hepatocytes. J. Biol. Chem. 270:1995;15242-15249.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15242-15249
    • Oda, H.1    Stockert, R.J.2    Collins, C.3    Wang, H.4    Novikoff, P.M.5    Satir, P.6    Wolkoff, A.W.7
  • 125
    • 0030025571 scopus 로고    scopus 로고
    • Three-dimensional organization of rat hepatocyte cytoskeleton: Relation to the asialoglycoprotein endocytosis pathway
    • Novikoff P.M., Cammer M., Tao L., Oda H., Stockert R.J., Wolkoff A.W., Satir P. Three-dimensional organization of rat hepatocyte cytoskeleton: relation to the asialoglycoprotein endocytosis pathway. J. Cell Sci. 109:1996;21-32.
    • (1996) J. Cell Sci. , vol.109 , pp. 21-32
    • Novikoff, P.M.1    Cammer, M.2    Tao, L.3    Oda, H.4    Stockert, R.J.5    Wolkoff, A.W.6    Satir, P.7
  • 126
    • 0019839990 scopus 로고
    • Evidence that the hepatic asialoglycoprotein receptor is internalized during endocytosis and that receptor recycling can be uncoupled from endocytosis at low temperature
    • Weigel P.H. Evidence that the hepatic asialoglycoprotein receptor is internalized during endocytosis and that receptor recycling can be uncoupled from endocytosis at low temperature. Biochem. Biophys. Res. Commun. 101:1981;1419-1425.
    • (1981) Biochem. Biophys. Res. Commun. , vol.101 , pp. 1419-1425
    • Weigel, P.H.1
  • 127
    • 0021075885 scopus 로고
    • Recycling of the asialoglycoprotein receptor in isolated rat hepatocytes. Dissociation of internalized ligand from receptor occurs in two kinetically and thermally distinguishable compartments
    • Oka J.A., Weigel P.H. Recycling of the asialoglycoprotein receptor in isolated rat hepatocytes. Dissociation of internalized ligand from receptor occurs in two kinetically and thermally distinguishable compartments. J. Biol. Chem. 258:1983;10253-10262.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10253-10262
    • Oka, J.A.1    Weigel, P.H.2
  • 128
    • 0021337903 scopus 로고
    • Intracellular segregation of asialoglycoproteins and their receptor: A prelysosomal event subsequent to dissociation of the ligand-receptor complex
    • Wolkoff A.W., Klausner R.D., Ashwell G., Harford J. Intracellular segregation of asialoglycoproteins and their receptor: a prelysosomal event subsequent to dissociation of the ligand-receptor complex. J. Cell Biol. 98:1984;375-381.
    • (1984) J. Cell Biol. , vol.98 , pp. 375-381
    • Wolkoff, A.W.1    Klausner, R.D.2    Ashwell, G.3    Harford, J.4
  • 129
    • 0022539758 scopus 로고
    • Receptor-mediated endocytosis of asialoglycoproteins by rat hepatocytes: Receptor-positive and receptor-negative endosomes
    • Mueller S.C., Hubbard A.L. Receptor-mediated endocytosis of asialoglycoproteins by rat hepatocytes: receptor-positive and receptor-negative endosomes. J. Cell Biol. 102:1986;932-942.
    • (1986) J. Cell Biol. , vol.102 , pp. 932-942
    • Mueller, S.C.1    Hubbard, A.L.2
  • 130
    • 0025806496 scopus 로고
    • Hydrolases in intracellular compartments of rat liver cells. Evidence for selective activation and/or delivery
    • Casciola-Rosen L.A.F., Hubbard A.L. Hydrolases in intracellular compartments of rat liver cells. Evidence for selective activation and/or delivery. J. Biol. Chem. 266:1991;4341-4347.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4341-4347
    • Casciola-Rosen, L.A.F.1    Hubbard, A.L.2
  • 131
    • 0021047222 scopus 로고
    • Microtubule-depolymerizing agents inhibit asialo-orosomucoid delivery to lysosomes but not its endocytosis or degradation in isolated rat hepatocytes
    • Oka J.A., Weigel P.H. Microtubule-depolymerizing agents inhibit asialo-orosomucoid delivery to lysosomes but not its endocytosis or degradation in isolated rat hepatocytes. Biochim. Biophys. Acta. 763:1983;368-376.
    • (1983) Biochim. Biophys. Acta , vol.763 , pp. 368-376
    • Oka, J.A.1    Weigel, P.H.2
  • 132
    • 0025328940 scopus 로고
    • The effect of vanadate on receptor-mediated endocytosis of asialoorosomucoid in rat liver parenchymal cells
    • Kindberg G.M., Gudmundsen O., Berg T. The effect of vanadate on receptor-mediated endocytosis of asialoorosomucoid in rat liver parenchymal cells. J. Biol. Chem. 265:1990;8999-9005.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8999-9005
    • Kindberg, G.M.1    Gudmundsen, O.2    Berg, T.3
  • 133
    • 0021363388 scopus 로고
    • Recycling of the hepatic asialoglycoprotein receptor in isolated rat hepatocytes. Receptor-ligand complexes in an intracellular slowly dissociating pool return to the cell surface prior to dissociation
    • Weigel P.H., Oka J.A. Recycling of the hepatic asialoglycoprotein receptor in isolated rat hepatocytes. Receptor-ligand complexes in an intracellular slowly dissociating pool return to the cell surface prior to dissociation. J. Biol. Chem. 259:1984;1150-1154.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1150-1154
    • Weigel, P.H.1    Oka, J.A.2
  • 134
    • 0019493831 scopus 로고
    • Turnover of the surface proteins and the receptor for serum asialoglycoproteins in primary cultures of rat hepatocytes
    • Warren R., Doyle D. Turnover of the surface proteins and the receptor for serum asialoglycoproteins in primary cultures of rat hepatocytes. J. Biol. Chem. 256:1981;1346-1355.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1346-1355
    • Warren, R.1    Doyle, D.2
  • 135
    • 0020562221 scopus 로고
    • Biosynthesis of the human asialoglycoprotein receptor
    • Schwartz A.L., Rup D. Biosynthesis of the human asialoglycoprotein receptor. J. Biol. Chem. 258:1983;11249-11255.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11249-11255
    • Schwartz, A.L.1    Rup, D.2
  • 136
    • 0021527854 scopus 로고
    • A cycloheximide-resistant pool of receptors for asialoglycoproteins and mannose 6-phosphate residues in the Golgi complex of hepatocytes
    • Geuze H.J., Slot J.W., Strous G.J., Luzio J.P., Schwartz A.L. A cycloheximide-resistant pool of receptors for asialoglycoproteins and mannose 6-phosphate residues in the Golgi complex of hepatocytes. EMBO J. 3:1984;2677-2685.
    • (1984) EMBO J. , vol.3 , pp. 2677-2685
    • Geuze, H.J.1    Slot, J.W.2    Strous, G.J.3    Luzio, J.P.4    Schwartz, A.L.5
  • 137
    • 0022343674 scopus 로고
    • Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation
    • Roth J., Taatjes D.J., Lucocq J.M., Weinstein J., Paulson J.C. Demonstration of an extensive trans-tubular network continuous with the Golgi apparatus stack that may function in glycosylation. Cell. 43:1985;287-295.
    • (1985) Cell , vol.43 , pp. 287-295
    • Roth, J.1    Taatjes, D.J.2    Lucocq, J.M.3    Weinstein, J.4    Paulson, J.C.5
  • 139
    • 0022606738 scopus 로고
    • Presence of asialoglycoprotein receptors in the Golgi complex in the absence of protein synthesis
    • Van den Bosch R.A., Geuze H.J., Strous G.J. Presence of asialoglycoprotein receptors in the Golgi complex in the absence of protein synthesis. Exp. Cell Res. 162:1986;231-242.
    • (1986) Exp. Cell Res. , vol.162 , pp. 231-242
    • Van den Bosch, R.A.1    Geuze, H.J.2    Strous, G.J.3
  • 140
    • 0021955354 scopus 로고
    • Intracellular movement of cell surface receptors after endocytosis: Resialylation of asialo-transferrin receptor in human erythroleukemia cells
    • Snider M.D., Rogers O.C. Intracellular movement of cell surface receptors after endocytosis: resialylation of asialo-transferrin receptor in human erythroleukemia cells. J. Cell Biol. 100:1985;826-834.
    • (1985) J. Cell Biol. , vol.100 , pp. 826-834
    • Snider, M.D.1    Rogers, O.C.2
  • 141
    • 0021099317 scopus 로고
    • Intracellular dissociation of receptor-bound asialoglycoproteins in cultured hepatocytes. A pH-mediated nonlysosomal event
    • Harford J., Bridges K., Ashwell G., Klausner R.D. Intracellular dissociation of receptor-bound asialoglycoproteins in cultured hepatocytes. A pH-mediated nonlysosomal event. J. Biol. Chem. 258:1983;3191-3197.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3191-3197
    • Harford, J.1    Bridges, K.2    Ashwell, G.3    Klausner, R.D.4
  • 142
    • 0024294284 scopus 로고
    • ATP-dependent inactivation and reactivation of constitutively recycling galactosyl receptors in isolated rat hepatocytes
    • McAbee D.D., Weigel P.H. ATP-dependent inactivation and reactivation of constitutively recycling galactosyl receptors in isolated rat hepatocytes. Biochemistry. 27:1988;2061-2069.
    • (1988) Biochemistry , vol.27 , pp. 2061-2069
    • McAbee, D.D.1    Weigel, P.H.2
  • 143
    • 0025190008 scopus 로고
    • The surface activity of the same subpopulation of galactosyl receptors on isolated rat hepatocytes is modulated by colchicine, monensin, ATP depletion, and chloroquine
    • McAbee D.D., Clarke B.L., Oka J.A., Weigel P.H. The surface activity of the same subpopulation of galactosyl receptors on isolated rat hepatocytes is modulated by colchicine, monensin, ATP depletion, and chloroquine. J. Biol. Chem. 265:1990;629-635.
    • (1990) J. Biol. Chem. , vol.265 , pp. 629-635
    • McAbee, D.D.1    Clarke, B.L.2    Oka, J.A.3    Weigel, P.H.4
  • 144
    • 0025965456 scopus 로고
    • Total cellular activity and distribution of a subpopulation of galactosyl receptors in isolated rat hepatocytes are differentially affected by microtubule drugs, monensin, low temperature, and chloroquine
    • McAbee D.D., Lear M.C., Weigel P.H. Total cellular activity and distribution of a subpopulation of galactosyl receptors in isolated rat hepatocytes are differentially affected by microtubule drugs, monensin, low temperature, and chloroquine. J. Cell. Biochem. 45:1991;59-68.
    • (1991) J. Cell. Biochem. , vol.45 , pp. 59-68
    • McAbee, D.D.1    Lear, M.C.2    Weigel, P.H.3
  • 145
    • 0025934750 scopus 로고
    • Vanadate modulates the activity of a subpopulation of asialoglycoprotein receptors on isolated rat hepatocytes: Active surface receptors are internalized and replaced by inactive receptors
    • Oka J.A., Weigel P.H. Vanadate modulates the activity of a subpopulation of asialoglycoprotein receptors on isolated rat hepatocytes: active surface receptors are internalized and replaced by inactive receptors. Arch. Biochem. Biophys. 289:1991;362-370.
    • (1991) Arch. Biochem. Biophys. , vol.289 , pp. 362-370
    • Oka, J.A.1    Weigel, P.H.2
  • 146
    • 0023520055 scopus 로고
    • Monensin inhibits ligand dissociation only transiently and partially and distinguishes two galactosyl receptor pathways in isolated rat hepatocytes
    • J.A. Oka, P.H. Weigel, Monensin inhibits ligand dissociation only transiently and partially and distinguishes two galactosyl receptor pathways in isolated rat hepatocytes, J. Cell. Physiol. 133 (1987) 243-252, 257
    • (1987) J. Cell. Physiol. , vol.133 , pp. 243-252
    • Oka, J.A.1    Weigel, P.H.2
  • 147
    • 0017348228 scopus 로고
    • Biological applications and evolutionary origins of ionophores
    • Pressman B.C., de Guzman N.T. Biological applications and evolutionary origins of ionophores. Adv. Exp. Med. Biol. 84:1977;285-300.
    • (1977) Adv. Exp. Med. Biol. , vol.84 , pp. 285-300
    • Pressman, B.C.1    De Guzman, N.T.2
  • 148
    • 0023612487 scopus 로고
    • Degradation of asialoglycoproteins mediated by the galactosyl receptor system in isolated hepatocytes. Evidence for two parallel pathways
    • Clarke B.L., Oka J.A., Weigel P.H. Degradation of asialoglycoproteins mediated by the galactosyl receptor system in isolated hepatocytes. Evidence for two parallel pathways. J. Biol. Chem. 262:1987;17384-17392.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17384-17392
    • Clarke, B.L.1    Oka, J.A.2    Weigel, P.H.3
  • 149
    • 0024419894 scopus 로고
    • Differential effects of leupeptin, monensin and colchicine on ligand degradation mediated by the two asialoglycoprotein receptor pathways in isolated rat hepatocytes
    • Clarke B.L., Weigel P.H. Differential effects of leupeptin, monensin and colchicine on ligand degradation mediated by the two asialoglycoprotein receptor pathways in isolated rat hepatocytes. Biochem. J. 262:1989;277-284.
    • (1989) Biochem. J. , vol.262 , pp. 277-284
    • Clarke, B.L.1    Weigel, P.H.2
  • 150
    • 0019877097 scopus 로고
    • Diacytosis of human asialotransferrin type 3 by isolated rat hepatocytes
    • Tolleshaug H., Chindemi P.A., Regoeczi E. Diacytosis of human asialotransferrin type 3 by isolated rat hepatocytes. J. Biol. Chem. 256:1981;6526-6528.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6526-6528
    • Tolleshaug, H.1    Chindemi, P.A.2    Regoeczi, E.3
  • 151
    • 0027765506 scopus 로고
    • Regulation of asialoglycoprotein receptor activity by a novel inactivation/reactivation cycle. Receptor reactivation in permeable rat hepatocytes is mediated by fatty acyl coenzyme A
    • Weigel P.H., Oka J.A. Regulation of asialoglycoprotein receptor activity by a novel inactivation/reactivation cycle. Receptor reactivation in permeable rat hepatocytes is mediated by fatty acyl coenzyme A. J. Biol. Chem. 268:1993;27186-27190.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27186-27190
    • Weigel, P.H.1    Oka, J.A.2
  • 152
    • 0028330440 scopus 로고
    • A novel cycle involving fatty acyl-coenzyme A regulates asialoglycoprotein receptor activity in permeable hepatocytes
    • Weigel P.H., Medh J.D., Oka J.A. A novel cycle involving fatty acyl-coenzyme A regulates asialoglycoprotein receptor activity in permeable hepatocytes. Mol. Biol. Cell. 5:1994;227-235.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 227-235
    • Weigel, P.H.1    Medh, J.D.2    Oka, J.A.3
  • 153
    • 0029022326 scopus 로고
    • Human hepatoma cell mutant defective in cell surface protein trafficking
    • Stockert R.J., Potvin B., Tao L., Stanley P., Wolkoff A.W. Human hepatoma cell mutant defective in cell surface protein trafficking. J. Biol. Chem. 270:1995;16107-16113.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16107-16113
    • Stockert, R.J.1    Potvin, B.2    Tao, L.3    Stanley, P.4    Wolkoff, A.W.5
  • 155
    • 0019466766 scopus 로고
    • Analysis of the effect of amines on inhibition of receptor-mediated and fluid-phase pinocytosis in rabbit alveolar macrophages
    • Kaplan J., Keogh E.A. Analysis of the effect of amines on inhibition of receptor-mediated and fluid-phase pinocytosis in rabbit alveolar macrophages. Cell. 24:1981;925-932.
    • (1981) Cell , vol.24 , pp. 925-932
    • Kaplan, J.1    Keogh, E.A.2
  • 156
    • 0021251432 scopus 로고
    • Monensin inhibits recycling of macrophage mannose-glycoprotein receptors and ligand delivery to lysosomes
    • Wileman T., Boshans R.L., Schlesinger P., Stahl P. Monensin inhibits recycling of macrophage mannose-glycoprotein receptors and ligand delivery to lysosomes. Biochem. J. 220:1984;665-675.
    • (1984) Biochem. J. , vol.220 , pp. 665-675
    • Wileman, T.1    Boshans, R.L.2    Schlesinger, P.3    Stahl, P.4
  • 157
    • 0019307389 scopus 로고
    • Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling
    • Gonzalez-Noriega A., Grubb J.H., Talkad V., Sly W.S. Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling. J. Cell Biol. 85:1980;839-852.
    • (1980) J. Cell Biol. , vol.85 , pp. 839-852
    • Gonzalez-Noriega, A.1    Grubb, J.H.2    Talkad, V.3    Sly, W.S.4
  • 158
    • 0021711637 scopus 로고
    • Complete inhibition of transferrin recycling by monensin in K562 cells
    • Stein B.S., Bensch K.G., Sussman H.H. Complete inhibition of transferrin recycling by monensin in K562 cells. J. Biol. Chem. 259:1984;14762-14772.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14762-14772
    • Stein, B.S.1    Bensch, K.G.2    Sussman, H.H.3
  • 159
    • 0019427474 scopus 로고
    • Monensin interrupts the recycling of low-density lipoprotein receptors in human fibroblasts
    • Basu S.K., Goldstein J.L., Anderson R.G.W., Brown M.S. Monensin interrupts the recycling of low-density lipoprotein receptors in human fibroblasts. Cell. 24:1981;493-502.
    • (1981) Cell , vol.24 , pp. 493-502
    • Basu, S.K.1    Goldstein, J.L.2    Anderson, R.G.W.3    Brown, M.S.4
  • 160
    • 0024230493 scopus 로고
    • Rapid constitutive internalization and externalization of epidermal growth factor receptors in isolated rat hepatocytes. Monensin inhibits receptor externalization and reduces the capacity for continued endocytosis of epidermal growth factor
    • Gladhaug I.P., Christofferse T. Rapid constitutive internalization and externalization of epidermal growth factor receptors in isolated rat hepatocytes. Monensin inhibits receptor externalization and reduces the capacity for continued endocytosis of epidermal growth factor. J. Biol. Chem. 263:1988;12199-12203.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12199-12203
    • Gladhaug, I.P.1    Christofferse, T.2
  • 161
    • 0032577247 scopus 로고    scopus 로고
    • The dual coated pit pathway hypothesis: Vertebrate cells have both ancient and modern coated pit pathways for receptor mediated endocytosis
    • Weigel P.H., Oka J.A. The dual coated pit pathway hypothesis: vertebrate cells have both ancient and modern coated pit pathways for receptor mediated endocytosis. Biochem. Biophys. Res. Commun. 246:1998;563-569.
    • (1998) Biochem. Biophys. Res. Commun. , vol.246 , pp. 563-569
    • Weigel, P.H.1    Oka, J.A.2
  • 163
    • 2142765005 scopus 로고    scopus 로고
    • Molecular chaperone binding to phosphorylated cytoplasmic domain regulates receptor trafficking to the cell surface
    • Huang T., Deng H., Wolkoff A.W., Stockert R.J. Molecular chaperone binding to phosphorylated cytoplasmic domain regulates receptor trafficking to the cell surface. Mol. Biol. Cell. 12S:2001;330a.
    • (2001) Mol. Biol. Cell , vol.12 S
    • Huang, T.1    Deng, H.2    Wolkoff, A.W.3    Stockert, R.J.4
  • 164
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh M.D. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta. 1451:1999;1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 165
    • 0030020733 scopus 로고    scopus 로고
    • The protein machinery of vesicle budding and fusion
    • Rothman J.E. The protein machinery of vesicle budding and fusion. Protein Sci. 5:1996;185-194.
    • (1996) Protein Sci. , vol.5 , pp. 185-194
    • Rothman, J.E.1
  • 166
    • 0029670903 scopus 로고    scopus 로고
    • Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting
    • Schweizer A., Kornfeld S., Rohrer J. Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6-phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting. J. Cell Biol. 132:1996;577-584.
    • (1996) J. Cell Biol. , vol.132 , pp. 577-584
    • Schweizer, A.1    Kornfeld, S.2    Rohrer, J.3
  • 168
    • 0034634584 scopus 로고    scopus 로고
    • Mechanism of pH-dependent N-acetylgalactosamine binding by a functional mimic of the hepatocyte asialoglycoprotein receptor
    • Feinberg H., Torgersen D., Drickamer K., Weiss W.I. Mechanism of pH-dependent N-acetylgalactosamine binding by a functional mimic of the hepatocyte asialoglycoprotein receptor. J. Biol. Chem. 275:2000;35176-35184.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35176-35184
    • Feinberg, H.1    Torgersen, D.2    Drickamer, K.3    Weiss, W.I.4
  • 169
    • 0023654009 scopus 로고
    • ATP depletion causes a reversible redistribution and inactivation of a subpopulation of galactosyl receptors in isolated rat hepatocytes
    • McAbee D.D., Weigel P.H. ATP depletion causes a reversible redistribution and inactivation of a subpopulation of galactosyl receptors in isolated rat hepatocytes. J. Biol. Chem. 262:1987;1942-1945.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1942-1945
    • McAbee, D.D.1    Weigel, P.H.2
  • 170
    • 0025816849 scopus 로고
    • Reconstitution of galactosyl receptor inactivation in permeabilized rat hepatocytes is ATP-dependent
    • Medh J.D., Weigel P.H. Reconstitution of galactosyl receptor inactivation in permeabilized rat hepatocytes is ATP-dependent. J. Biol. Chem. 266:1991;8771-8778.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8771-8778
    • Medh, J.D.1    Weigel, P.H.2
  • 171
    • 0005128318 scopus 로고    scopus 로고
    • Palmitoylation and depalmitoylation directly regulate the ligand-binding activity of State 2 rat asialoglycoprotein receptors
    • Oka J.-A., Zeng F.Y., Weigel P.H. Palmitoylation and depalmitoylation directly regulate the ligand-binding activity of State 2 rat asialoglycoprotein receptors. Mol. Biol. Cell. 7S:1996;433a.
    • (1996) Mol. Biol. Cell , vol.7 S
    • Oka, J.-A.1    Zeng, F.Y.2    Weigel, P.H.3
  • 172
    • 0037174951 scopus 로고    scopus 로고
    • Nonpalmitoylated human asialoglycoprotein receptors recycle constitutively, but are defective in coated pit-mediated endocytosis, dissociation and delivery of ligand to lysosomes
    • in press
    • Yik J.H.N., Saxena A., Weigel J.A., Weigel P.H. Nonpalmitoylated human asialoglycoprotein receptors recycle constitutively, but are defective in coated pit-mediated endocytosis, dissociation and delivery of ligand to lysosomes. J. Biol. Chem. 277:2002;. in press.
    • (2002) J. Biol. Chem. , vol.277
    • Yik, J.H.N.1    Saxena, A.2    Weigel, J.A.3    Weigel, P.H.4
  • 173
    • 0001413280 scopus 로고
    • The polysaccharide of the vitreous humor
    • Meyer K., Palmer J.W. The polysaccharide of the vitreous humor. J. Biol. Chem. 107:1934;629-634.
    • (1934) J. Biol. Chem. , vol.107 , pp. 629-634
    • Meyer, K.1    Palmer, J.W.2
  • 175
    • 0026603974 scopus 로고
    • Molecular mechanisms of cell motility
    • Turley E.A. Molecular mechanisms of cell motility. Cancer Metastasis Rev. 11:1992;1-3.
    • (1992) Cancer Metastasis Rev. , vol.11 , pp. 1-3
    • Turley, E.A.1
  • 176
    • 0027504082 scopus 로고
    • Hyaluronan-binding proteins in development, tissue homeostasis, and disease
    • Knudson C.B., Knudson W. Hyaluronan-binding proteins in development, tissue homeostasis, and disease. FASEB J. 7:1993;1233-1241.
    • (1993) FASEB J. , vol.7 , pp. 1233-1241
    • Knudson, C.B.1    Knudson, W.2
  • 177
    • 0030766519 scopus 로고    scopus 로고
    • Hyaluronan in morphogenesis
    • Toole B.P. Hyaluronan in morphogenesis. J. Intern. Med. 242:1997;35-40.
    • (1997) J. Intern. Med. , vol.242 , pp. 35-40
    • Toole, B.P.1
  • 181
    • 0032899955 scopus 로고    scopus 로고
    • Functions of hyaluronan in wound repair
    • Chen W.Y., Abatangelo G. Functions of hyaluronan in wound repair. Wound Repair Regen. 7:1999;79-89.
    • (1999) Wound Repair Regen. , vol.7 , pp. 79-89
    • Chen, W.Y.1    Abatangelo, G.2
  • 182
    • 0021834944 scopus 로고
    • Angiogenesis induced by degradation products of hyaluronic acid
    • West D.C., Hampson I.N., Arnold F., Kumar S. Angiogenesis induced by degradation products of hyaluronic acid. Science. 14:1985;1324-1326.
    • (1985) Science , vol.14 , pp. 1324-1326
    • West, D.C.1    Hampson, I.N.2    Arnold, F.3    Kumar, S.4
  • 183
    • 0030953252 scopus 로고    scopus 로고
    • Early-response gene signalling is induced by angiogenic oligosaccharides of hyaluronan in endothelial cells. Inhibition by non-angiogenic, high-molecular-weight hyaluronan
    • Deed R., Rooney P., Kumar P., Norton J.D., Smith J., Freemont A.J., Kumar S. Early-response gene signalling is induced by angiogenic oligosaccharides of hyaluronan in endothelial cells. Inhibition by non-angiogenic, high-molecular-weight hyaluronan. Int. J. Cancer. 71:1997;251-256.
    • (1997) Int. J. Cancer , vol.71 , pp. 251-256
    • Deed, R.1    Rooney, P.2    Kumar, P.3    Norton, J.D.4    Smith, J.5    Freemont, A.J.6    Kumar, S.7
  • 187
    • 0028286068 scopus 로고
    • The chondrodystrophy, nanomelia: Biosynthesis and processing of the defective aggrecan precursor
    • Vertel B.M., Grier B.L., Li H., Schwartz N.B. The chondrodystrophy, nanomelia: biosynthesis and processing of the defective aggrecan precursor. Biochem. J. 301:1994;211-216.
    • (1994) Biochem. J. , vol.301 , pp. 211-216
    • Vertel, B.M.1    Grier, B.L.2    Li, H.3    Schwartz, N.B.4
  • 188
    • 0030806072 scopus 로고    scopus 로고
    • Developmental expression of perlecan during murine embryogenesis
    • Handler M., Yurchenco P.D., Iozzo R.V. Developmental expression of perlecan during murine embryogenesis. Dev. Dyn. 210:1997;130-145.
    • (1997) Dev. Dyn. , vol.210 , pp. 130-145
    • Handler, M.1    Yurchenco, P.D.2    Iozzo, R.V.3
  • 190
    • 0031961752 scopus 로고    scopus 로고
    • Stimulation of inducible nitric oxide synthase in rat liver by hyaluronan fragments
    • Rockey D.C., Chung J.J., Mckee C.M., Noble P.W. Stimulation of inducible nitric oxide synthase in rat liver by hyaluronan fragments. Hepatology. 27:1998;86-92.
    • (1998) Hepatology , vol.27 , pp. 86-92
    • Rockey, D.C.1    Chung, J.J.2    Mckee, C.M.3    Noble, P.W.4
  • 191
    • 0025038449 scopus 로고
    • Hyaluronan and its binding proteins, the hyaladherins
    • Toole B.P. Hyaluronan and its binding proteins, the hyaladherins. Curr. Opin. Cell Biol. 2:1990;839-844.
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 839-844
    • Toole, B.P.1
  • 192
    • 0028297463 scopus 로고
    • Hyaluronic acid. A review of its pharmacology and use as a surgical aid in ophthalmology, and its therapeutic potential in joint disease and wound healing
    • Goa K.L., Benfield P. Hyaluronic acid. A review of its pharmacology and use as a surgical aid in ophthalmology, and its therapeutic potential in joint disease and wound healing. Drugs. 47:1994;536-566.
    • (1994) Drugs , vol.47 , pp. 536-566
    • Goa, K.L.1    Benfield, P.2
  • 194
    • 0034653742 scopus 로고    scopus 로고
    • Osteoarthritis: Current concepts in diagnosis and management
    • Manek N.J., Lane N.E. Osteoarthritis: current concepts in diagnosis and management. Am. Fam. Phys. 61:2000;1795-1804.
    • (2000) Am. Fam. Phys. , vol.61 , pp. 1795-1804
    • Manek, N.J.1    Lane, N.E.2
  • 195
    • 0024244988 scopus 로고
    • Hyaluronan improves the healing of experimental tympanic membrane perforations. A comparison of preparations with different rheologic properties
    • Laurent C., Hellstrom S., Fellenius E. Hyaluronan improves the healing of experimental tympanic membrane perforations. A comparison of preparations with different rheologic properties. Arch. Otolaryngol. Head Neck Surg. 114:1988;1435-1441.
    • (1988) Arch. Otolaryngol. Head Neck Surg. , vol.114 , pp. 1435-1441
    • Laurent, C.1    Hellstrom, S.2    Fellenius, E.3
  • 196
    • 0032763954 scopus 로고    scopus 로고
    • New directions in the prevention of adhesion in laparoscopic surgery
    • Panay N., Lower A.M. New directions in the prevention of adhesion in laparoscopic surgery. Curr. Opin. Obstet. Gynecol. 11:1999;379-385.
    • (1999) Curr. Opin. Obstet. Gynecol. , vol.11 , pp. 379-385
    • Panay, N.1    Lower, A.M.2
  • 197
    • 0031953083 scopus 로고    scopus 로고
    • Aerosolized hyaluronic acid decreases alveolar injury induced by human neutrophil elastase
    • Cantor J.O., Cerreta J.M., Armand G., Turino G.M. Aerosolized hyaluronic acid decreases alveolar injury induced by human neutrophil elastase. Proc. Soc. Exp. Biol. Med. 217:1998;471-475.
    • (1998) Proc. Soc. Exp. Biol. Med. , vol.217 , pp. 471-475
    • Cantor, J.O.1    Cerreta, J.M.2    Armand, G.3    Turino, G.M.4
  • 198
    • 0034601831 scopus 로고    scopus 로고
    • Cross-linked hyaluronic acid hydrogel films: New biomaterials for drug delivery
    • Luo Y., Kirker K.R., Prestwich G.D. Cross-linked hyaluronic acid hydrogel films: new biomaterials for drug delivery. J. Control. Release. 69:2000;169-184.
    • (2000) J. Control. Release , vol.69 , pp. 169-184
    • Luo, Y.1    Kirker, K.R.2    Prestwich, G.D.3
  • 200
    • 0025754329 scopus 로고
    • Degradation of newly synthesized high molecular mass hyaluronan in the epidermal and dermal compartments of human skin in organ culture
    • Tammi R., Saamanen A.M., Maibach H.I., Tammi M. Degradation of newly synthesized high molecular mass hyaluronan in the epidermal and dermal compartments of human skin in organ culture. J. Invest. Dermatol. 97:1991;126-130.
    • (1991) J. Invest. Dermatol. , vol.97 , pp. 126-130
    • Tammi, R.1    Saamanen, A.M.2    Maibach, H.I.3    Tammi, M.4
  • 201
    • 0033231406 scopus 로고    scopus 로고
    • Internalization of the hyaluronan receptor CD44 by chondrocytes
    • Aguiar D.J., Knudson W., Knudson C.B. Internalization of the hyaluronan receptor CD44 by chondrocytes. Exp. Cell Res. 252:1999;292-302.
    • (1999) Exp. Cell Res. , vol.252 , pp. 292-302
    • Aguiar, D.J.1    Knudson, W.2    Knudson, C.B.3
  • 202
    • 0020523327 scopus 로고
    • Tissue uptake of circulating hyaluronic acid. A whole body autoradiographic study
    • Fraser J.R., Appelgren L.E., Laurent T.C. Tissue uptake of circulating hyaluronic acid. A whole body autoradiographic study. Cell Tissue Res. 233:1983;285-293.
    • (1983) Cell Tissue Res. , vol.233 , pp. 285-293
    • Fraser, J.R.1    Appelgren, L.E.2    Laurent, T.C.3
  • 203
    • 0019813898 scopus 로고
    • Plasma clearance, tissue distribution and metabolism of hyaluronic acid injected intravenously in the rabbit
    • Fraser J.R., Laurent T.C., Pertoft H., Baxter E. Plasma clearance, tissue distribution and metabolism of hyaluronic acid injected intravenously in the rabbit. Biochem. J. 200:1981;415-424.
    • (1981) Biochem. J. , vol.200 , pp. 415-424
    • Fraser, J.R.1    Laurent, T.C.2    Pertoft, H.3    Baxter, E.4
  • 204
    • 0031961562 scopus 로고    scopus 로고
    • Serum hyaluronan as a marker of liver fibrosis in hemophiliacs with hepatitis C virus-associated chronic liver disease
    • Yamada M., Fukuda Y., Nakano I., Katano Y., Takamatsu J., Hayakawa T. Serum hyaluronan as a marker of liver fibrosis in hemophiliacs with hepatitis C virus-associated chronic liver disease. Acta Haematol. 99:1998;212-216.
    • (1998) Acta Haematol. , vol.99 , pp. 212-216
    • Yamada, M.1    Fukuda, Y.2    Nakano, I.3    Katano, Y.4    Takamatsu, J.5    Hayakawa, T.6
  • 207
    • 0033501681 scopus 로고    scopus 로고
    • Serum levels of hyaluronan, antigenic keratan sulfate, matrix metalloproteinase 3, and tissue inhibitor of metalloproteinases 1 change predictably in rheumatoid arthritis patients who have begun activity after a night of bed rest
    • Manicourt D.H., Poilvache P., Nzeusseu A., van Egeren A., Devogelaer J.P., Lenz M.E., Thonar E.J. Serum levels of hyaluronan, antigenic keratan sulfate, matrix metalloproteinase 3, and tissue inhibitor of metalloproteinases 1 change predictably in rheumatoid arthritis patients who have begun activity after a night of bed rest. Arthritis Rheum. 42:1999;1861-1869.
    • (1999) Arthritis Rheum. , vol.42 , pp. 1861-1869
    • Manicourt, D.H.1    Poilvache, P.2    Nzeusseu, A.3    Van Egeren, A.4    Devogelaer, J.P.5    Lenz, M.E.6    Thonar, E.J.7
  • 210
    • 0033570965 scopus 로고    scopus 로고
    • Hyaluronan in serum as an indicator of progressive disease in hyaluronan-producing malignant mesothelioma
    • Thylen A., Wallin J., Martensson G. Hyaluronan in serum as an indicator of progressive disease in hyaluronan-producing malignant mesothelioma. Cancer. 86:1999;2000-2005.
    • (1999) Cancer , vol.86 , pp. 2000-2005
    • Thylen, A.1    Wallin, J.2    Martensson, G.3
  • 211
    • 0023816599 scopus 로고
    • Affinity and distribution of surface and intracellular hyaluronic acid receptors in isolated rat liver endothelial cells
    • Raja R.H., McGary C.T., Weigel P.H. Affinity and distribution of surface and intracellular hyaluronic acid receptors in isolated rat liver endothelial cells. J. Biol. Chem. 263:1988;16661-16668.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16661-16668
    • Raja, R.H.1    McGary, C.T.2    Weigel, P.H.3
  • 212
    • 0024545265 scopus 로고
    • Endocytosis of hyaluronic acid by rat liver endothelial cells. Evidence for receptor recycling
    • McGary C.T., Raja R.H., Weigel P.H. Endocytosis of hyaluronic acid by rat liver endothelial cells. Evidence for receptor recycling. Biochem. J. 257:1989;875-884.
    • (1989) Biochem. J. , vol.257 , pp. 875-884
    • McGary, C.T.1    Raja, R.H.2    Weigel, P.H.3
  • 214
    • 0020530819 scopus 로고
    • Endothelial cells are a site of uptake and degradation of hyaluronic acid in the liver
    • Eriksson S., Fraser J.R., Laurent T.C., Pertoft H., Smedsrod B. Endothelial cells are a site of uptake and degradation of hyaluronic acid in the liver. Exp. Cell Res. 144:1983;223-228.
    • (1983) Exp. Cell Res. , vol.144 , pp. 223-228
    • Eriksson, S.1    Fraser, J.R.2    Laurent, T.C.3    Pertoft, H.4    Smedsrod, B.5
  • 215
    • 0022552324 scopus 로고
    • Binding of hyaluronate and chondroitin sulphate to liver endothelial cells
    • Laurent T.C., Fraser J.R., Pertoft H., Smedsrod B. Binding of hyaluronate and chondroitin sulphate to liver endothelial cells. Biochem. J. 234:1986;653-658.
    • (1986) Biochem. J. , vol.234 , pp. 653-658
    • Laurent, T.C.1    Fraser, J.R.2    Pertoft, H.3    Smedsrod, B.4
  • 216
    • 0023927631 scopus 로고
    • Morphological studies on endocytosis of chondroitin sulphate proteoglycan by rat liver endothelial cells
    • Smedsrod B., Malmgren M., Ericsson J., Laurent T.C. Morphological studies on endocytosis of chondroitin sulphate proteoglycan by rat liver endothelial cells. Cell Tissue Res. 253:1988;39-45.
    • (1988) Cell Tissue Res. , vol.253 , pp. 39-45
    • Smedsrod, B.1    Malmgren, M.2    Ericsson, J.3    Laurent, T.C.4
  • 217
    • 0026515301 scopus 로고
    • The endocytic hyaluronan receptor in rat liver sinusoidal endothelial cells is Ca(+2)-independent and distinct from a Ca(+2)-dependent hyaluronan binding activity
    • Yannariello-Brown J., McGary C.T., Weigel P.H. The endocytic hyaluronan receptor in rat liver sinusoidal endothelial cells is Ca(+2)-independent and distinct from a Ca(+2)-dependent hyaluronan binding activity. J. Cell. Biochem. 48:1992;73-80.
    • (1992) J. Cell. Biochem. , vol.48 , pp. 73-80
    • Yannariello-Brown, J.1    McGary, C.T.2    Weigel, P.H.3
  • 218
    • 0026657466 scopus 로고
    • Identification of the Ca(+2)-independent endocytic hyaluronan receptor in rat liver sinusoidal endothelial cells using a photoaffinity cross-linking reagent
    • Yannariello-Brown J., Frost S.J., Weigel P.H. Identification of the Ca(+2)-independent endocytic hyaluronan receptor in rat liver sinusoidal endothelial cells using a photoaffinity cross-linking reagent. J. Biol. Chem. 267:1992;20451-20456.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20451-20456
    • Yannariello-Brown, J.1    Frost, S.J.2    Weigel, P.H.3
  • 219
    • 0030057486 scopus 로고    scopus 로고
    • A novel ligand blot assay detects different hyaluronan-binding proteins in rat liver hepatocytes and sinusoidal endothelial cells
    • Yannariello-Brown J., Zhou B., Ritchie D., Oka J.A., Weigel P.H. A novel ligand blot assay detects different hyaluronan-binding proteins in rat liver hepatocytes and sinusoidal endothelial cells. Biochem. Biophys. Res. Commun. 218:1996;314-319.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 314-319
    • Yannariello-Brown, J.1    Zhou, B.2    Ritchie, D.3    Oka, J.A.4    Weigel, P.H.5
  • 220
    • 0031054240 scopus 로고    scopus 로고
    • Identification of a 175 kDa protein as the ligand-binding subunit of the rat liver sinusoidal endothelial cell hyaluronan receptor
    • Yannariello-Brown J., Zhou B., Weigel P.H. Identification of a 175 kDa protein as the ligand-binding subunit of the rat liver sinusoidal endothelial cell hyaluronan receptor. Glycobiology. 7:1997;15-21.
    • (1997) Glycobiology , vol.7 , pp. 15-21
    • Yannariello-Brown, J.1    Zhou, B.2    Weigel, P.H.3
  • 221
    • 0033607639 scopus 로고    scopus 로고
    • Purification and subunit characterization of the rat liver endocytic hyaluronan receptor
    • Zhou B., Oka J.A., Singh A., Weigel P.H. Purification and subunit characterization of the rat liver endocytic hyaluronan receptor. J. Biol. Chem. 274:1999;33831-33834.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33831-33834
    • Zhou, B.1    Oka, J.A.2    Singh, A.3    Weigel, P.H.4
  • 222
    • 0005131411 scopus 로고    scopus 로고
    • Purification and characterization of the human hyaluronan receptor for endocytosis (HARE)
    • Zhou B., McGary C.T., Weigel J.A., Saxena A., Weigel P.H. Purification and characterization of the human hyaluronan receptor for endocytosis (HARE). Glycobiology. 10:2001;877.
    • (2001) Glycobiology , vol.10 , pp. 877
    • Zhou, B.1    McGary, C.T.2    Weigel, J.A.3    Saxena, A.4    Weigel, P.H.5
  • 223
    • 0034529081 scopus 로고    scopus 로고
    • Identification of the hyaluronan receptor for endocytosis (HARE)
    • Zhou B., Weigel J.A., Fauss L., Weigel P.H. Identification of the hyaluronan receptor for endocytosis (HARE). J. Biol. Chem. 275:2000;37733-37741.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37733-37741
    • Zhou, B.1    Weigel, J.A.2    Fauss, L.3    Weigel, P.H.4
  • 224
    • 0031864528 scopus 로고    scopus 로고
    • The intercellular adhesion molecule (ICAM) family of proteins. New members and novel functions
    • Hayflick J.S., Kilgannon P., Gallatin W.M. The intercellular adhesion molecule (ICAM) family of proteins. New members and novel functions. Immunol. Res. 17:1998;313-327.
    • (1998) Immunol. Res. , vol.17 , pp. 313-327
    • Hayflick, J.S.1    Kilgannon, P.2    Gallatin, W.M.3
  • 225
    • 0028090359 scopus 로고
    • Intercellular adhesion molecule-1 is a cell surface receptor for hyaluronan
    • McCourt P.A., Ek B., Forsberg N., Gustafson S. Intercellular adhesion molecule-1 is a cell surface receptor for hyaluronan. J. Biol. Chem. 269:1994;30081-30084.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30081-30084
    • McCourt, P.A.1    Ek, B.2    Forsberg, N.3    Gustafson, S.4
  • 226
    • 0030774117 scopus 로고    scopus 로고
    • On the adsorption of hyaluronan and ICAM-1 to modified hydrophobic resins
    • McCourt P.A., Gustafson S. On the adsorption of hyaluronan and ICAM-1 to modified hydrophobic resins. Int. J. Biochem. Cell Biol. 29:1997;1179-1189.
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 1179-1189
    • McCourt, P.A.1    Gustafson, S.2
  • 227
    • 0032713816 scopus 로고    scopus 로고
    • Characterization of a hyaluronan receptor on rat sinusoidal liver endothelial cells and its functional relationship to scavenger receptors
    • McCourt P.A., Smedsrod B.H., Melkko J., Johansson S. Characterization of a hyaluronan receptor on rat sinusoidal liver endothelial cells and its functional relationship to scavenger receptors. Hepatology. 30:1999;1276-1286.
    • (1999) Hepatology , vol.30 , pp. 1276-1286
    • McCourt, P.A.1    Smedsrod, B.H.2    Melkko, J.3    Johansson, S.4
  • 228
    • 0033593793 scopus 로고    scopus 로고
    • LYVE-1, a new homologue of the CD44 glycoprotein, is a lymph-specific receptor for hyaluronan
    • Banerji S., Ni J., Wang S.X., Clasper S., Su J., Tammi R., Jones M., Jackson D.G. LYVE-1, a new homologue of the CD44 glycoprotein, is a lymph-specific receptor for hyaluronan. J. Cell Biol. 144:1999;789-801.
    • (1999) J. Cell Biol. , vol.144 , pp. 789-801
    • Banerji, S.1    Ni, J.2    Wang, S.X.3    Clasper, S.4    Su, J.5    Tammi, R.6    Jones, M.7    Jackson, D.G.8
  • 229
    • 0036679228 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of the rat 175 kDa HARE - The Hyaluronan Receptor for Endocytosis
    • in press
    • Zhou B., McGary C.T., Weigel J.A., Saxena A., Weigel P.H. Molecular cloning and functional expression of the rat 175 kDa HARE - the Hyaluronan Receptor for Endocytosis. Mol. Biol. Cell. 13:2002;. in press.
    • (2002) Mol. Biol. Cell , vol.13
    • Zhou, B.1    McGary, C.T.2    Weigel, J.A.3    Saxena, A.4    Weigel, P.H.5
  • 230
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman I. Endocytosis and molecular sorting. Annu. Rev. Cell Biol. 12:1996;575-625.
    • (1996) Annu. Rev. Cell Biol. , vol.12 , pp. 575-625
    • Mellman, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.