메뉴 건너뛰기




Volumn 246, Issue 1, 1997, Pages 243-251

Domain-specific N-glycosylation of the membrane glycoprotein dipeptidylpeptidase IV (CD26) influences its subcellular trafficking, biological stability, enzyme activity and protein folding

Author keywords

Dipeptidylpeptidase IV; N glycosylation; Protein stability; Protein trafficking; Site directed mutagenesis

Indexed keywords

DIPEPTIDYL PEPTIDASE IV;

EID: 0030916841     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00243.x     Document Type: Article
Times cited : (75)

References (49)
  • 2
    • 0022760449 scopus 로고
    • Cell surface glycosylations of hepatocytes and hepatoma cells identified by monoclonal antibodies
    • Becker, A., Neumeier, R., Heidrich, C., Loch, N., Hartel, S. & Reutter, W. (1986) Cell surface glycosylations of hepatocytes and hepatoma cells identified by monoclonal antibodies, Biol. Chem. Hoppe-Seyler 367, 681-688.
    • (1986) Biol. Chem. Hoppe-Seyler , vol.367 , pp. 681-688
    • Becker, A.1    Neumeier, R.2    Heidrich, C.3    Loch, N.4    Hartel, S.5    Reutter, W.6
  • 3
  • 4
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 5
    • 0024294338 scopus 로고
    • Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin
    • Copeland, C. S., Zimmer, K. P., Wagner, K. R., Healey, G. A., Mellman, I. & Helenius, A. (1988) Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin, Cell 53, 197-209.
    • (1988) Cell , vol.53 , pp. 197-209
    • Copeland, C.S.1    Zimmer, K.P.2    Wagner, K.R.3    Healey, G.A.4    Mellman, I.5    Helenius, A.6
  • 6
    • 0026583798 scopus 로고
    • Folding of intestinal brush border enzymes. Evidence that high-mannose glycosylation is an essential early event
    • Danielsen, E. M. (1992) Folding of intestinal brush border enzymes. Evidence that high-mannose glycosylation is an essential early event, Biochemistry 31, 2266-2272.
    • (1992) Biochemistry , vol.31 , pp. 2266-2272
    • Danielsen, E.M.1
  • 7
    • 0027236545 scopus 로고
    • Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidylpeptidase IV (CD26)
    • David, F., Bernard, A.-M., Pierres, M. & Marguet, D. (1993) Identification of serine 624, aspartic acid 702, and histidine 734 as the catalytic triad residues of mouse dipeptidylpeptidase IV (CD26), J. Biol. Chem. 268, 17 247-17 252.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17247-17252
    • David, F.1    Bernard, A.-M.2    Pierres, M.3    Marguet, D.4
  • 8
    • 0026317511 scopus 로고
    • Glycosidase inhibitors: Inhibitors of N-linked oligosaccharide processing
    • Elbein, A. D. (1991) Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing, FASEB J. 5, 3055-3063.
    • (1991) FASEB J. , vol.5 , pp. 3055-3063
    • Elbein, A.D.1
  • 9
    • 0019332627 scopus 로고
    • Biogenesis of plasma membrane glycoproteins: Purifucation and properties of two rat liver plasma membrane glycoproteins
    • Elovson, J. (1980) Biogenesis of plasma membrane glycoproteins: Purifucation and properties of two rat liver plasma membrane glycoproteins, J. Biol. Chem. 255, 5807-5815.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5807-5815
    • Elovson, J.1
  • 10
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A. P. & Vogelstein, B. (1983) A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity, Anal. Biochem. 132, 6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 11
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler, K. & Simons, K. (1995) The role of N-glycans in the secretory pathway, Cell 81, 309-312.
    • (1995) Cell , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 12
    • 0028323205 scopus 로고
    • CD26: A surface protease involved in T cell activation
    • Fleischer, B. (1994) CD26: a surface protease involved in T cell activation, Immunol. Today 15, 180-184.
    • (1994) Immunol. Today , vol.15 , pp. 180-184
    • Fleischer, B.1
  • 14
    • 0028844558 scopus 로고
    • The role of N-glycosylation for functional expression of the human platelet-activating factor receptor. Glycosylation is required for efficient membrane trafficking
    • Garcia Rodriguez, C., Cundell, D. R., Tuomanen, E. I., Kolakowski, L. F. Jr, Gerard, C. & Gerard, N. P. (1995) The role of N-glycosylation for functional expression of the human platelet-activating factor receptor. Glycosylation is required for efficient membrane trafficking, J. Biol. Chem. 270, 25 178-25 184.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25178-25184
    • Garcia Rodriguez, C.1    Cundell, D.R.2    Tuomanen, E.I.3    Kolakowski Jr., L.F.4    Gerard, C.5    Gerard, N.P.6
  • 15
    • 0026776768 scopus 로고
    • In vitro mutagenesis of potential N-glycosylation sites of arylsulfatase A. Effects on glycosylation, phosphorylation, and intracellular sorting
    • Gieselmann, V., Schmidt, B. & von Figura, K. (1992) In vitro mutagenesis of potential N-glycosylation sites of arylsulfatase A. Effects on glycosylation, phosphorylation, and intracellular sorting, J. Biol. Chem. 267, 13 262-13 266.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13262-13266
    • Gieselmann, V.1    Schmidt, B.2    Von Figura, K.3
  • 16
    • 0028880799 scopus 로고
    • The effects of the site-directed removal of N-glycosylation sites from β-1,4-N-acetylgalactosaminyltransferase on its function
    • Haraguchi, M. Yamashiro, S., Furukawa, K., Takamiya, K., Shiku, H. & Furukawa, K. (1995) The effects of the site-directed removal of N-glycosylation sites from β-1,4-N-acetylgalactosaminyltransferase on its function, Biochem. J. 312, 273-280.
    • (1995) Biochem. J. , vol.312 , pp. 273-280
    • Haraguchi, M.1    Yamashiro, S.2    Furukawa, K.3    Takamiya, K.4    Shiku, H.5    Furukawa, K.6
  • 17
    • 0026018986 scopus 로고
    • Development of monoclonal antibodies against different protein and carbohydrate epitopes of dipeptidyl peptidase IV from rat liver plasma membranes
    • Hartel-Schenk, S., Loch, N., Zimmermann, M. & Reutter, W. (1991) Development of monoclonal antibodies against different protein and carbohydrate epitopes of dipeptidyl peptidase IV from rat liver plasma membranes, Eur. J. Biochem. 196, 349-355.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 349-355
    • Hartel-Schenk, S.1    Loch, N.2    Zimmermann, M.3    Reutter, W.4
  • 18
    • 0028198111 scopus 로고
    • How N-linked oligosacchrides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius, A. (1994) How N-linked oligosacchrides affect glycoprotein folding in the endoplasmic reticulum, Mol. Biol. Cell 5, 253-265.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 19
    • 0023449851 scopus 로고
    • cDNA cloning for a bile canaliculus domain-specific membrane glycoprotein of rat hepatocytes
    • Hong, W. & Doyle, D. (1987) cDNA cloning for a bile canaliculus domain-specific membrane glycoprotein of rat hepatocytes, Proc. Natl Acad. Sci. USA 84, 7962-7966.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7962-7966
    • Hong, W.1    Doyle, D.2
  • 20
    • 0024436202 scopus 로고
    • Expression of enzymatically active rat dipeptidyl peptidase IV in Chinese hamster ovary cells after transfection
    • Hong, W., Piazza, G. A., Hixson, D. C. & Doyle, D. (1989) Expression of enzymatically active rat dipeptidyl peptidase IV in Chinese hamster ovary cells after transfection, Biochemistry 28, 8474-8478.
    • (1989) Biochemistry , vol.28 , pp. 8474-8478
    • Hong, W.1    Piazza, G.A.2    Hixson, D.C.3    Doyle, D.4
  • 21
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S. M. & Helenius, A. (1989) Protein oligomerization in the endoplasmic reticulum, Annu. Rev. Cell Biol. 5, 277-307.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 22
    • 0025853058 scopus 로고
    • Oligomerization and intracellular protein transport: Dimerization of intestinal dipeptidylpeptidase IV occurs in the Golgi apparatus
    • Jascur, T., Matter, K. & Hauri, H.-P. (1991) Oligomerization and intracellular protein transport: Dimerization of intestinal dipeptidylpeptidase IV occurs in the Golgi apparatus, Biochemistry 30, 1908-1915.
    • (1991) Biochemistry , vol.30 , pp. 1908-1915
    • Jascur, T.1    Matter, K.2    Hauri, H.-P.3
  • 23
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner, R. D. & Sitia, R. (1990) Protein degradation in the endoplasmic reticulum, Cell 62, 611-614.
    • (1990) Cell , vol.62 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 24
    • 0026655996 scopus 로고
    • Structures and functions of the sugar chains of glycoproteins
    • Kobata, A. (1992) Structures and functions of the sugar chains of glycoproteins, Eur. J. Biochem. 209, 483-501.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 483-501
    • Kobata, A.1
  • 25
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R. & Kornfeld, S. (1985) Assembly of asparagine-linked oligosaccharides, Annu. Rev. Biochem. 54, 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 26
    • 0022550932 scopus 로고
    • Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface
    • Kreis, T. E. & Lodsh, H. F. (1986) Oligomerization is essential for transport of vesicular stomatitis viral glycoprotein to the cell surface, Cell 46, 929-937.
    • (1986) Cell , vol.46 , pp. 929-937
    • Kreis, T.E.1    Lodsh, H.F.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0028928202 scopus 로고
    • Glycosylation of human truncated Fc ε Rl α chain is necessary for efficient folding in the endoplasmic reticulum
    • Letourneur, O., Sechi, S., Willette-Brown, J., Robertson, M. W. & Kinet, J. P. (1995) Glycosylation of human truncated Fc ε Rl α chain is necessary for efficient folding in the endoplasmic reticulum, J. Biol. Chem. 270, 8249-8256.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8249-8256
    • Letourneur, O.1    Sechi, S.2    Willette-Brown, J.3    Robertson, M.W.4    Kinet, J.P.5
  • 29
    • 0027519943 scopus 로고
    • Protein glycosylation: Structural and functional aspects
    • Lis, H. & Sharon, N. (1993) Protein glycosylation: Structural and functional aspects, Eur. J. Biochem. 218, 1-27.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 30
    • 0026485263 scopus 로고
    • Biosynthesis and metabolism of dipeptidyl peptidase IV in primary cultured rat hepatocytes and Morris hepatoma 7777 cells
    • Loch, N., Tauber, R., Becker, A., Hartel-Schenk, S. & Reutter, W. (1992) Biosynthesis and metabolism of dipeptidyl peptidase IV in primary cultured rat hepatocytes and Morris hepatoma 7777 cells, Eur. J. Biochem. 210, 161-168.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 161-168
    • Loch, N.1    Tauber, R.2    Becker, A.3    Hartel-Schenk, S.4    Reutter, W.5
  • 31
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • Marquardt, T. & Helenius, A. (1992) Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum, J. Cell Biol. 117, 505-513.
    • (1992) J. Cell Biol. , vol.117 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 32
    • 0001409550 scopus 로고
    • CD26 - A key costimulatory molecule in CD4 memory T cells
    • Morimoto, C. & Schlossman, S. F. (1994) CD26 - a key costimulatory molecule in CD4 memory T cells, The Immunologist 2, 4-7.
    • (1994) The Immunologist , vol.2 , pp. 4-7
    • Morimoto, C.1    Schlossman, S.F.2
  • 34
    • 0024420303 scopus 로고
    • Proalbumin is processed to serum albumin in COS-1 cells transfected with cDNA for rat albumin
    • Oda, K., Takami, N., Fujiwara, T. Misumi, Y. & Ikehara, Y. (1989) Proalbumin is processed to serum albumin in COS-1 cells transfected with cDNA for rat albumin, Biochem. Biophys. Res. Commun. 163, 194-200.
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 194-200
    • Oda, K.1    Takami, N.2    Fujiwara, T.3    Misumi, Y.4    Ikehara, Y.5
  • 35
    • 0024516896 scopus 로고
    • 2-terminal signal sequence as the membrane-anchoring domain
    • 2-terminal signal sequence as the membrane-anchoring domain, J. Biol. Chem. 264, 3596-3601.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3596-3601
    • Ogata, S.1    Misumi, Y.2    Ikehara, Y.3
  • 36
    • 0026579515 scopus 로고
    • Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenisis
    • Ogata, S., Misumi, Y., Tsuji, E., Takama, N., Oda, K. & Ikehara, Y. (1992) Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenisis, Biochemistry 31, 2582-2587.
    • (1992) Biochemistry , vol.31 , pp. 2582-2587
    • Ogata, S.1    Misumi, Y.2    Tsuji, E.3    Takama, N.4    Oda, K.5    Ikehara, Y.6
  • 37
    • 0028930710 scopus 로고
    • The role of N-glycosylation in the targeting and activity of the GLYT1 glycine transporter
    • Olivares, L., Aragon, C., Gimenez, C. & Zafra, F. (1995) The role of N-glycosylation in the targeting and activity of the GLYT1 glycine transporter, J. Biol. Chem. 270, 9437-9442.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9437-9442
    • Olivares, L.1    Aragon, C.2    Gimenez, C.3    Zafra, F.4
  • 39
    • 0024826667 scopus 로고
    • Biochemical properties of dipeptidyl peptidase IV in liver and hepatoma plasma membranes
    • Reutter, W., Hartel, S., Hanski, C., Huhle, T., Zimmer, T. & Gossrau, R. (1989) Biochemical properties of dipeptidyl peptidase IV in liver and hepatoma plasma membranes, Adv. Enzyme Regul. 28, 253-269.
    • (1989) Adv. Enzyme Regul. , vol.28 , pp. 253-269
    • Reutter, W.1    Hartel, S.2    Hanski, C.3    Huhle, T.4    Zimmer, T.5    Gossrau, R.6
  • 40
    • 0002190040 scopus 로고
    • Functional aspects of the three extracellular domains of dipeptidyl peptidase IV: Characterization of glycosylation events, of the collagen-binding site and of endopeptidase activity
    • (Fleischer, B., ed.) Springer, New York
    • Reutter, W., Baum, O., Löster, K., Fan, H., Bork, J. P., Bernt, K., Hanski, Ch. & Tauber, R. (1995) Functional aspects of the three extracellular domains of dipeptidyl peptidase IV: Characterization of glycosylation events, of the collagen-binding site and of endopeptidase activity, in Dipeptidyl peptidase IV (CD26) in metabolism and the immune response (Fleischer, B., ed.) pp. 55-78, Springer, New York.
    • (1995) Dipeptidyl Peptidase IV (CD26) in Metabolism and the Immune Response , pp. 55-78
    • Reutter, W.1    Baum, O.2    Löster, K.3    Fan, H.4    Bork, J.P.5    Bernt, K.6    Hanski, Ch.7    Tauber, R.8
  • 43
    • 0028989689 scopus 로고
    • N-glycosylation of human interferon-γ: Glycans at Asn-25 are critical for protease resistance
    • Sareneva, T., Pirhonen, J., Cantell, K. & Julkunen, I. (1995) N-glycosylation of human interferon-γ: glycans at Asn-25 are critical for protease resistance, Biochem. J. 308, 9-14.
    • (1995) Biochem. J. , vol.308 , pp. 9-14
    • Sareneva, T.1    Pirhonen, J.2    Cantell, K.3    Julkunen, I.4
  • 44
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa, M. & Parodi, A. J. (1995) The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase, EMBO J. 14, 4196-4203.
    • (1995) EMBO J. , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 45
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct, Glycobiology 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 46
  • 48
    • 0023748633 scopus 로고
    • Comparative studies of the sugar chains of aminopeptidase N and dipeptidyl peptidase IV purified from rat kidney brush-border membrane
    • Yamashita, K., Tachibana, Y., Matsuda, Y., Katsunuma, N., Kochibe, N. & Kobata, A. (1988) Comparative studies of the sugar chains of aminopeptidase N and dipeptidyl peptidase IV purified from rat kidney brush-border membrane, Biochemistry 27, 5565-5573.
    • (1988) Biochemistry , vol.27 , pp. 5565-5573
    • Yamashita, K.1    Tachibana, Y.2    Matsuda, Y.3    Katsunuma, N.4    Kochibe, N.5    Kobata, A.6
  • 49
    • 0027512245 scopus 로고
    • Role of oligosaccharides in the processing and function of human transferrin receptors
    • Yang, B., Hoe, M. H., Black, P. & Hunt, R. C. (1993) Role of oligosaccharides in the processing and function of human transferrin receptors, J. Biol. Chem. 268, 7453-7441.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7453-17441
    • Yang, B.1    Hoe, M.H.2    Black, P.3    Hunt, R.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.