Heparan sulfate proteoglycans from mouse mammary epithelial cells. A putative membrane proteoglycan associates quantitatively with lipid vesicles.
作者： A C Rapraeger , M Bernfield
DOI: 10.1016/S0021-9258(18)32712-1
关键词:
摘要: Mouse mammary epithelial (NMuMG) cells produce both cellular and extracellular heparan sulfate-rich proteoglycans. A proteoglycan, but no proteoglycans, associates quantitatively vectorially with lipid vesicles, as assessed by column chromatography centrifugation. This lipophilic proteoglycan is extracted an aggregate when are treated 4 M guanidine HCl, a single component in the presence of detergent, suggesting that it aggregates lipid. An association confirmed intercalation into bilayer vesicles. Formation vesicles causes to have chromatographic sedimentation behavior while destruction detergent nullifies this effect. The intercalated its glycosaminoglycan-containing domain exposed exterior since mild trypsin treatment removes portion from vesicle. After cleavage vesicle, released chromatographs apparent molecular size similar whole longer Thus, which responsible for interaction presumably anchors membranes.
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sci-hub.st 参考文章(21)
K.G. Vogel, D.W. Peterson, Extracellular, surface, and intracellular proteoglycans produced by human embryo lung fibroblasts in culture (IMR-90). Journal of Biological Chemistry. ,vol. 256, pp. 13235- 13242 ,(1981) , 10.1016/S0021-9258(18)43034-7
Lena Kjellen, Ake Oldberg, M Höök, None, Cell-surface heparan sulfate. Mechanisms of proteoglycan-cell association. Journal of Biological Chemistry. ,vol. 255, pp. 10407- 10413 ,(1980) , 10.1016/S0021-9258(19)70479-7
Ake Oldberg, L Kjellen, M Höök, None, Cell-surface heparan sulfate. Isolation and characterization of a proteoglycan from rat liver membranes. Journal of Biological Chemistry. ,vol. 254, pp. 8505- 8510 ,(1979) , 10.1016/S0021-9258(19)86920-X
V C Hascall, S W Sajdera, Proteinpolysaccharide complex from bovine nasal cartilage. The function of glycoprotein in the formation of aggregates. Journal of Biological Chemistry. ,vol. 244, pp. 2384- 2396 ,(1969) , 10.1016/S0021-9258(19)78236-2
Yasuo Kagawa, Efraim Racker, Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation XXV. RECONSTITUTION OF VESICLES CATALYZING 32Pi—ADENOSINE TRIPHOSPHATE EXCHANGE Journal of Biological Chemistry. ,vol. 246, pp. 5477- 5487 ,(1966) , 10.1016/S0021-9258(18)61930-1
Seitaro MUTOH, Ikuo FUNAKOSHI, Ikuo YAMASHINA, Isolation and characterization of proteoheparan sulfate from plasma membranes of an ascites hepatoma, AH 66. Journal of Biochemistry. ,vol. 84, pp. 483- 489 ,(1978) , 10.1093/OXFORDJOURNALS.JBCHEM.A132150
Bengt Glimelius, Börje Norling, Bengt Westermark, Åke Wasteson, Turnover of cell surface associated glycosaminoglycans in cultures of human normal and malignant glial cells Experimental Cell Research. ,vol. 117, pp. 179- 189 ,(1978) , 10.1016/0014-4827(78)90440-8
J. R. Hassell, P. G. Robey, H. J. Barrach, J. Wilczek, S. I. Rennard, G. R. Martin, Isolation of a heparan sulfate-containing proteoglycan from basement membrane Proceedings of the National Academy of Sciences of the United States of America. ,vol. 77, pp. 4494- 4498 ,(1980) , 10.1073/PNAS.77.8.4494
P Ekblom, Formation of basement membranes in the embryonic kidney: an immunohistological study Journal of Cell Biology. ,vol. 91, pp. 1- 10 ,(1981) , 10.1083/JCB.91.1.1
Paul M. Kraemer, Heparan sulfates of cultured cells. I. Membrane-associated and cell-sap species in Chinese hamster cells Biochemistry. ,vol. 10, pp. 1437- 1445 ,(1971) , 10.1021/BI00784A026