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Volumn 78, Issue 4, 1999, Pages 256-264

Serum albumin as a potential carrier for the apocrine secretion of proteins in the rat coagulating gland

Author keywords

Albumin; Apocrine secretion; Coagulating gland

Indexed keywords

CARBONATE DEHYDRATASE II; CARRIER PROTEIN; CELL PROTEIN; CYTOPLASM PROTEIN; LACTATE DEHYDROGENASE; MESSENGER RNA; POLYCLONAL ANTIBODY; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; SERUM ALBUMIN;

EID: 0032934028     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0171-9335(99)80059-4     Document Type: Article
Times cited : (11)

References (45)
  • 1
    • 0018762659 scopus 로고
    • Experimental studies of apocrine secretion in the dorsal prostate epithelium of the rat
    • Aumüller, G., G. Adler: Experimental studies of apocrine secretion in the dorsal prostate epithelium of the rat. Cell Tissue Res. 198, 145-158 (1979).
    • (1979) Cell Tissue Res. , vol.198 , pp. 145-158
    • Aumüller, G.1    Adler, G.2
  • 2
    • 0021341309 scopus 로고
    • In vitro synthesis and glycosylation of androgen-dependent secretory proteins of rat dorsal prostate and coagulating gland
    • Bartlett, R. J., F. S. French, E. M. Wilson: In vitro synthesis and glycosylation of androgen-dependent secretory proteins of rat dorsal prostate and coagulating gland. Prostate 5, 75-91 (1984).
    • (1984) Prostate , vol.5 , pp. 75-91
    • Bartlett, R.J.1    French, F.S.2    Wilson, E.M.3
  • 3
    • 0030779161 scopus 로고    scopus 로고
    • Detection of mRNAs encoding peroxisomal proteins by non-radioactive in situ hybridization with digoxigenin-labelled cRNAs
    • Baumgart, E., A. Schad, A. Völkl, H. D. Fahimi: Detection of mRNAs encoding peroxisomal proteins by non-radioactive in situ hybridization with digoxigenin-labelled cRNAs. Histochem. Cell Biol. 108, 371-379 (1997).
    • (1997) Histochem. Cell Biol. , vol.108 , pp. 371-379
    • Baumgart, E.1    Schad, A.2    Völkl, A.3    Fahimi, H.D.4
  • 4
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., H. Beier, H. J. Gross: Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99 (1987).
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 5
    • 0026098655 scopus 로고
    • The concentrations of transferrin, beta 2-microglobulin, and albumin in seminal plasma in relation to sperm count
    • Chard, T., J. Parslow, T. Rehmann, A. Dawnay: The concentrations of transferrin, beta 2-microglobulin, and albumin in seminal plasma in relation to sperm count. Fertil. Steril. 55, 211-213 (1991).
    • (1991) Fertil. Steril. , vol.55 , pp. 211-213
    • Chard, T.1    Parslow, J.2    Rehmann, T.3    Dawnay, A.4
  • 6
    • 0024595079 scopus 로고
    • Ultrastructure of secretory cells of male accessory sex glands of golden hamster and effect of melatonin
    • Chow, P. H., S. F. Pang: Ultrastructure of secretory cells of male accessory sex glands of golden hamster and effect of melatonin. Acta Anat. 134, 327-340 (1989).
    • (1989) Acta Anat. , vol.134 , pp. 327-340
    • Chow, P.H.1    Pang, S.F.2
  • 7
    • 0029861911 scopus 로고    scopus 로고
    • Transglutaminase from rat coagulating gland secretion. Post-translational modifications and activation by phosphatidic acids
    • Esposito, C., P. Pucci, A. Amoresano, G. Marino, A. Cozzolino, R. Porta: Transglutaminase from rat coagulating gland secretion. Post-translational modifications and activation by phosphatidic acids. J. Biol. Chem. 271, 27416-27423 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 27416-27423
    • Esposito, C.1    Pucci, P.2    Amoresano, A.3    Marino, G.4    Cozzolino, A.5    Porta, R.6
  • 8
    • 0031029256 scopus 로고    scopus 로고
    • Animal lectins
    • Gabius, H.-J.: Animal lectins. Eur. J. Biochem. 243, 543-576 (1997).
    • (1997) Eur. J. Biochem. , vol.243 , pp. 543-576
    • Gabius, H.-J.1
  • 9
    • 0024524963 scopus 로고
    • Endothelial albumin-binding proteins are membrane-associated components exposed on the cell surface
    • Ghinea, N., M. Eskenasy, M. Simionescu, N. Simionescu: Endothelial albumin-binding proteins are membrane-associated components exposed on the cell surface. J. Biol. Chem. 264, 4755-4758 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 4755-4758
    • Ghinea, N.1    Eskenasy, M.2    Simionescu, M.3    Simionescu, N.4
  • 10
    • 0022551377 scopus 로고
    • Specific binding sites for albumin restricted to plasmalemmal vesicles of continuous capillary endothelium: Receptor-mediated transcytosis
    • Ghitescu, L., A. Fixman, M. Simionescu, N. Simionescu: Specific binding sites for albumin restricted to plasmalemmal vesicles of continuous capillary endothelium: receptor-mediated transcytosis. J. Cell Biol. 102, 1304-1311 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 1304-1311
    • Ghitescu, L.1    Fixman, A.2    Simionescu, M.3    Simionescu, N.4
  • 11
    • 0017683392 scopus 로고
    • Secretion in the rat coagulating gland after copulation
    • Hawkins, W. E., J. J. Geuze: Secretion in the rat coagulating gland after copulation. Cell Tissue Res. 181, 519-529 (1977).
    • (1977) Cell Tissue Res. , vol.181 , pp. 519-529
    • Hawkins, W.E.1    Geuze, J.J.2
  • 12
    • 0023931570 scopus 로고
    • Albumin in rabbit skeletal muscle. Origin, distribution and regulation by contractile activity
    • Heilig, A., D. Pette: Albumin in rabbit skeletal muscle. Origin, distribution and regulation by contractile activity. Eur. J. Biochem. 171, 503-508 (1988).
    • (1988) Eur. J. Biochem. , vol.171 , pp. 503-508
    • Heilig, A.1    Pette, D.2
  • 13
    • 0021950476 scopus 로고
    • Platelet tropomyosin-binding protein is identical with serum albumin
    • Hitchcock-De Gregori, S. E., M. D. Gerhard, W. E. Brown: Platelet tropomyosin-binding protein is identical with serum albumin. J. Biol. Chem. 260, 3228-3231 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 3228-3231
    • Hitchcock-De Gregori, S.E.1    Gerhard, M.D.2    Brown, W.E.3
  • 14
    • 0026771971 scopus 로고
    • Molecular cloning of rat prostate transglutaminase complementary DNA. The major androgen-regulated protein DP1 of rat dorsal prostate and coagulating gland
    • Ho, K. C., V. E. Quarmby, F. S. French, E. M. Wilson: Molecular cloning of rat prostate transglutaminase complementary DNA. The major androgen-regulated protein DP1 of rat dorsal prostate and coagulating gland. J. Biol. Chem. 267, 12660-12667 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 12660-12667
    • Ho, K.C.1    Quarmby, V.E.2    French, F.S.3    Wilson, E.M.4
  • 15
    • 0021691615 scopus 로고
    • Detection of an interferon antagonist, sarcolectin, in human sarcomas and muscles
    • Jiang, P. H., F. Chany-Fournier, M. Sarragne, A. Gregoire, C. Chany: Detection of an interferon antagonist, sarcolectin, in human sarcomas and muscles. Int. J. Cancer 34, 625-632 (1984).
    • (1984) Int. J. Cancer , vol.34 , pp. 625-632
    • Jiang, P.H.1    Chany-Fournier, F.2    Sarragne, M.3    Gregoire, A.4    Chany, C.5
  • 16
    • 0028225392 scopus 로고
    • Correlation of expression of binding sites for synthetic blood group A-,B-, and H-trisaccharides and for sarcolectin with survival of patients with bronchial carcinoma
    • Kayser, K., N. V. Bovin, E. Y. Korchagina, C. Zeilinger, F. Y. Zeng, H.-J. Gabius: Correlation of expression of binding sites for synthetic blood group A-,B-, and H-trisaccharides and for sarcolectin with survival of patients with bronchial carcinoma. Eur. J. Cancer 30A, 653-657 (1994).
    • (1994) Eur. J. Cancer , vol.30 A , pp. 653-657
    • Kayser, K.1    Bovin, N.V.2    Korchagina, E.Y.3    Zeilinger, C.4    Zeng, F.Y.5    Gabius, H.-J.6
  • 17
    • 0024324355 scopus 로고
    • Albumin is a major protein component of transverse tubule vesicles isolated from skeletal muscle
    • Knudson, C. M., K. P. Campbell: Albumin is a major protein component of transverse tubule vesicles isolated from skeletal muscle. J. Biol. Chem. 264, 10795-10798 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 10795-10798
    • Knudson, C.M.1    Campbell, K.P.2
  • 18
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Andersen, J.: Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods 10, 203-209 (1984).
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0028263747 scopus 로고
    • Structural elements in glycoprotein 70 from polytropic Friend mink cell focus-inducing virus and glycoprotein 71 from ecotropic Friend murine leukemia virus, as defined by disulfide-bonding pattern and limited proteolysis
    • Linder, M., V. Wenzel, D. Linder, S. Stirm: Structural elements in glycoprotein 70 from polytropic Friend mink cell focus-inducing virus and glycoprotein 71 from ecotropic Friend murine leukemia virus, as defined by disulfide-bonding pattern and limited proteolysis. J. Virol. 68, 5133-5141 (1994).
    • (1994) J. Virol. , vol.68 , pp. 5133-5141
    • Linder, M.1    Wenzel, V.2    Linder, D.3    Stirm, S.4
  • 21
    • 0024515487 scopus 로고
    • Intracellular traffic of newly synthesized proteins
    • Lingappa, V. R: Intracellular traffic of newly synthesized proteins. J. Clin. Invest. 83, 739-751 (1989).
    • (1989) J. Clin. Invest. , vol.83 , pp. 739-751
    • Lingappa, V.R.1
  • 22
    • 0020567425 scopus 로고
    • Immunonephelometry of specific proteins in human seminal plasma
    • Lizana, J., E. Blad: Immunonephelometry of specific proteins in human seminal plasma. Clin. Chem. 29, 618-623 (1983).
    • (1983) Clin. Chem. , vol.29 , pp. 618-623
    • Lizana, J.1    Blad, E.2
  • 23
    • 0028896844 scopus 로고
    • Exportation of mouse vas deferens protein, a protein without signal peptide from mouse vas deferens epithelium: A model for apocrine secretion
    • Manin, M., P. Lecher, A. Martinez, S. Tournadre, C. I. Jean: Exportation of mouse vas deferens protein, a protein without signal peptide from mouse vas deferens epithelium: a model for apocrine secretion. Biol. Reprod. 52, 50-62 (1995).
    • (1995) Biol. Reprod. , vol.52 , pp. 50-62
    • Manin, M.1    Lecher, P.2    Martinez, A.3    Tournadre, S.4    Jean, C.I.5
  • 24
    • 0029803059 scopus 로고    scopus 로고
    • The macrophage migration inhibitory factor (MIF) production by Leydig cells: Evidence for a role in regulation of testicular function
    • Meinhardt, A., M. Bacher, J. R. McFarlane, C. N. Metz, J. Seitz, M. P. Hedger, D. M. de Kretser, R. Bucala: The macrophage migration inhibitory factor (MIF) production by Leydig cells: evidence for a role in regulation of testicular function. Endocrinology 137, 5090-5095 (1996).
    • (1996) Endocrinology , vol.137 , pp. 5090-5095
    • Meinhardt, A.1    Bacher, M.2    McFarlane, J.R.3    Metz, C.N.4    Seitz, J.5    Hedger, M.P.6    De Kretser, D.M.7    Bucala, R.8
  • 26
    • 0016203452 scopus 로고
    • Specific apocrine secretion in the anterior lobe of the prostate gland of rabbits
    • Nicander, L., L. Plöen, M. Larsson: Specific apocrine secretion in the anterior lobe of the prostate gland of rabbits. Cell Tissue Res. 151, 69-77 (1974).
    • (1974) Cell Tissue Res. , vol.151 , pp. 69-77
    • Nicander, L.1    Plöen, L.2    Larsson, M.3
  • 27
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade, G.: Intracellular aspects of the process of protein synthesis. Science 189, 347-358 (1975).
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 28
    • 0003626648 scopus 로고    scopus 로고
    • Academic Press, New York
    • Peters, T. Jr.: All about albumin. pp109-116, Academic Press, New York 1996.
    • (1996) All about Albumin , pp. 109-116
    • Peters T., Jr.1
  • 29
    • 0015292980 scopus 로고
    • The secretory pathways of rat serum glycoproteins and albumin
    • Redman, C. M., G. Cherian: The secretory pathways of rat serum glycoproteins and albumin. J. Cell Biol. 52, 231-245 (1972).
    • (1972) J. Cell Biol. , vol.52 , pp. 231-245
    • Redman, C.M.1    Cherian, G.2
  • 30
    • 0001164146 scopus 로고
    • Nucleotide sequence of cloned rat serum albumin messenger RNA
    • Sargent, T. D., M. Yang, J. Bonner: Nucleotide sequence of cloned rat serum albumin messenger RNA. Proc. Natl. Acad. Sci. USA 78, 243-246 (1981).
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 243-246
    • Sargent, T.D.1    Yang, M.2    Bonner, J.3
  • 32
    • 0028270799 scopus 로고
    • Membrane and secretory proteins are transported from the golgi complex to the sinusoidal plasmalemma of hepatocytes by distinct vesicular carriers
    • Saucan, L., G. E. Palade: Membrane and secretory proteins are transported from the Golgi complex to the sinusoidal plasmalemma of hepatocytes by distinct vesicular carriers. J. Cell Biol. 125, 733-741 (1994).
    • (1994) J. Cell Biol. , vol.125 , pp. 733-741
    • Saucan, L.1    Palade, G.E.2
  • 34
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., G. Jagow: Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379 (1987).
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Jagow, G.2
  • 35
    • 0012725836 scopus 로고
    • Die hautdrüsen des menschen und der säugetiere, ihre biologische und rassenanatomische bedeutung, sowie über muscularis sexualis
    • Schiefferdecker, P.: Die Hautdrüsen des Menschen und der Säugetiere, ihre biologische und rassenanatomische Bedeutung, sowie über Muscularis sexualis. Biol. Zentralbl. 37, 634-662 (1917).
    • (1917) Biol. Zentralbl. , vol.37 , pp. 634-662
    • Schiefferdecker, P.1
  • 36
    • 0025190238 scopus 로고
    • Immunohistochemistry of rat secretory transglutaminase from rodent prostate
    • Seitz, J., C. Keppler, U. Rausch, G. Aumüller: Immunohistochemistry of rat secretory transglutaminase from rodent prostate. Histochemistry 93, 525-530 (1990).
    • (1990) Histochemistry , vol.93 , pp. 525-530
    • Seitz, J.1    Keppler, C.2    Rausch, U.3    Aumüller, G.4
  • 37
    • 0028034887 scopus 로고
    • Hormonally induced changes in apocrine secretion of transglutaminase in the rat dorsal prostate and coagulating gland
    • Steinhoff, M., W. Eicheler, P. M. Holterhus, U. Rausch, J. Seitz, G. Aumüller: Hormonally induced changes in apocrine secretion of transglutaminase in the rat dorsal prostate and coagulating gland. Eur. J. Cell Biol. 65, 49-59 (1994).
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 49-59
    • Steinhoff, M.1    Eicheler, W.2    Holterhus, P.M.3    Rausch, U.4    Seitz, J.5    Aumüller, G.6
  • 38
    • 0016693889 scopus 로고
    • Components of human split ejaculates. I. Spermatozoa, fructose, immunoglobulins, albumin, lactoferrin, transferrin and other plasma proteins
    • Tauber, P. F., L. J. Zaneveld, D. Propping, G. F. Schumacher: Components of human split ejaculates. I. Spermatozoa, fructose, immunoglobulins, albumin, lactoferrin, transferrin and other plasma proteins. J. Reprod. Fertil. 43, 249-267 (1975).
    • (1975) J. Reprod. Fertil. , vol.43 , pp. 249-267
    • Tauber, P.F.1    Zaneveld, L.J.2    Propping, D.3    Schumacher, G.F.4
  • 39
    • 0022423245 scopus 로고
    • Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: Genomic complexity and molecular evolution of the gene
    • Tso, J. Y., X. H. Sun, T. H. Kao, K. S. Reece, R. Wu: Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene. Nucleic Acids Res. 13, 2485-2502 (1985).
    • (1985) Nucleic Acids Res. , vol.13 , pp. 2485-2502
    • Tso, J.Y.1    Sun, X.H.2    Kao, T.H.3    Reece, K.S.4    Wu, R.5
  • 40
    • 4244056588 scopus 로고
    • Hormone regulation of carbonic anhydrase II expression
    • F. Botrè, G. Gros, B. T. Storey (eds): VCH. Weinheim
    • Väänänen, H. K., E. M. Valve, S. I. Mäkelä, M. Nevalainen, P. L. Härkönen: Hormone regulation of carbonic anhydrase II expression. In: F. Botrè, G. Gros, B. T. Storey (eds): Carbonic anhydrase. pp. 345-351. VCH. Weinheim 1991.
    • (1991) Carbonic Anhydrase , pp. 345-351
    • Väänänen, H.K.1    Valve, E.M.2    Mäkelä, S.I.3    Nevalainen, M.4    Härkönen, P.L.5
  • 41
    • 0345397423 scopus 로고    scopus 로고
    • Characterization of a merocrine secreted glycoprotein of rat coagulating gland
    • Wilhelm, B., C. Keppler, D. Linder, J. Seitz: Characterization of a merocrine secreted glycoprotein of rat coagulating gland. Biol. Chem. Hoppe-Seyler 378, 96 (1997).
    • (1997) Biol. Chem. Hoppe-seyler , vol.378 , pp. 96
    • Wilhelm, B.1    Keppler, C.2    Linder, D.3    Seitz, J.4
  • 43
    • 0027205380 scopus 로고
    • The major binding protein of interferon antagonist sarcolectin in human placenta is a macrophage migration inhibitory factor
    • Zeng, F.-Y., W. Y. Weiser, H. Kratzin, B. Stahl, H. Karas, H.-J. Gabius: The major binding protein of interferon antagonist sarcolectin in human placenta is a macrophage migration inhibitory factor. Arch. Biochem. Biophys. 303, 74-80 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 74-80
    • Zeng, F.-Y.1    Weiser, W.Y.2    Kratzin, H.3    Stahl, B.4    Karas, H.5    Gabius, H.-J.6
  • 44
    • 0028450074 scopus 로고
    • Migration inhibitory factor-binding sarcolectin from human placenta is indistinguishable from a subfraction of human serum albumin
    • Zeng, F.-Y., H. Kratzin, H.-J. Gabius: Migration inhibitory factor-binding sarcolectin from human placenta is indistinguishable from a subfraction of human serum albumin. Biol. Chem. Hoppe-Seyler 375, 393-399 (1994).
    • (1994) Biol. Chem. Hoppe-seyler , vol.375 , pp. 393-399
    • Zeng, F.-Y.1    Kratzin, H.2    Gabius, H.-J.3
  • 45
    • 0028335704 scopus 로고
    • Characterization of the macrophage migration inhibitory factor-binding site of sarcolectin and its relationship to human serum albumin
    • Zeng, F.-Y., V. Gerke, H.-J. Gabius: Characterization of the macrophage migration inhibitory factor-binding site of sarcolectin and its relationship to human serum albumin. Biochem. Biophys. Res. Commun. 200, 89-94 (1994).
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 89-94
    • Zeng, F.-Y.1    Gerke, V.2    Gabius, H.-J.3


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