Literature DB >> 1731524

Cell surface heparan sulfate proteoglycan and chondroitin sulfate proteoglycan of arterial smooth muscle cells.

I J Edwards1, W D Wagner.   

Abstract

Cell surface proteoglycans of aortic smooth muscle cells of atherosclerosis-susceptible White Carneau (WC) and atherosclerosis-resistant Show Racer (SR) pigeons were compared to determine differences that may be involved in the greater proliferative properties of cultured WC cells. Using [35S]-sodium sulfate and [3H]-glucosamine as labeling precursors, chondroitin sulfate-proteoglycan (CS-PG) and heparin sulfate-proteoglycan (HS-PG) were identified as distinct molecules associated with the plasma membrane. Heparan sulfate-proteoglycan was reduced up to 50% in WC compared with SR cells, and, based on interaction with ion-exchange resin, had a lower charge density. These differences were not observed for the CS-PG from the two cell types. The mode of association of the cell surface PG with the plasma membrane was examined. Dissociation with 1 mol/l (molar) sodium chloride indicated that less than 10% of total cell surface PG were ironically associated with the cells. The remainder required detergent extraction, suggesting hydrophobic interactions with the plasma membrane. Both CS-PG and HS-PG displayed affinity for octyl sepharose and both were identified in isolated plasma membranes. These data present the first description of a hydrophobic CS-PG that is a significant and distinct cell-associated PG in arterial smooth muscle cells. The observation of decreased and structurally altered HS-PG in WC compared with SR cells is consistent with a potential growth regulatory function for this molecule.

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Year:  1992        PMID: 1731524      PMCID: PMC1886247     

Source DB:  PubMed          Journal:  Am J Pathol        ISSN: 0002-9440            Impact factor:   4.307


  49 in total

1.  Structural analysis of chick-embryo cartilage proteoglycan by selective degradation with chondroitin lyases (chondroitinases) and endo-beta-D-galactosidase (keratanase).

Authors:  Y Oike; K Kimata; T Shinomura; K Nakazawa; S Suzuki
Journal:  Biochem J       Date:  1980-10-01       Impact factor: 3.857

2.  Cell-surface heparan sulfate. Mechanisms of proteoglycan-cell association.

Authors:  L Kjellén; A Oldberg; M Höök
Journal:  J Biol Chem       Date:  1980-11-10       Impact factor: 5.157

3.  Liver plasma membranes and proteoglycan prepared therefrom inhibit the growth of hepatoma cells in vitro.

Authors:  H Kawakami; H Terayama
Journal:  Biochim Biophys Acta       Date:  1981-08-06

4.  Phenyl--Sepharose chromatography of membrane proteins solubilized in Triton X-100.

Authors:  S D Carson; W H Konigsberg
Journal:  Anal Biochem       Date:  1981-09-15       Impact factor: 3.365

5.  Characterization of proteoglycans synthesized by cultured arterial smooth muscle cells of the rat.

Authors:  A Schmidt; A von Teutul; E Buddecke
Journal:  Hoppe Seylers Z Physiol Chem       Date:  1984-04

6.  Structural determinants of the capacity of heparin to inhibit the proliferation of vascular smooth muscle cells.

Authors:  J J Castellot; D L Beeler; R D Rosenberg; M J Karnovsky
Journal:  J Cell Physiol       Date:  1984-09       Impact factor: 6.384

7.  Proteoglycans synthesized by smooth muscle cells derived from monkey (Macaca nemestrina) aorta.

Authors:  Y Chang; M Yanagishita; V C Hascall; T N Wight
Journal:  J Biol Chem       Date:  1983-05-10       Impact factor: 5.157

8.  Structural determinants of the capacity of heparin to inhibit the proliferation of vascular smooth muscle cells. II. Evidence for a pentasaccharide sequence that contains a 3-O-sulfate group.

Authors:  J J Castellot; J Choay; J C Lormeau; M Petitou; E Sache; M J Karnovsky
Journal:  J Cell Biol       Date:  1986-05       Impact factor: 10.539

9.  Cultured endothelial cells produce a heparinlike inhibitor of smooth muscle cell growth.

Authors:  J J Castellot; M L Addonizio; R Rosenberg; M J Karnovsky
Journal:  J Cell Biol       Date:  1981-08       Impact factor: 10.539

10.  Proteoglycans in primate arteries. III. Characterization of the proteoglycans synthesized by arterial smooth muscle cells in culture.

Authors:  T N Wight; V C Hascall
Journal:  J Cell Biol       Date:  1983-01       Impact factor: 10.539

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  3 in total

1.  Complete 1H NMR assignments of synthetic glycopeptides from the carbohydrate-protein linkage region of serglycins.

Authors:  E V Curto; T T Sakai; M J Jablonsky; S Rio-Anneheim; J C Jacquinet; N R Krishna
Journal:  Glycoconj J       Date:  1996-08       Impact factor: 2.916

2.  Characterization of [3H]-heparin binding in human vascular smooth muscle cells and its relationship to the inhibition of DNA synthesis.

Authors:  M K Patel; J S Refson; M Schachter; A D Hughes
Journal:  Br J Pharmacol       Date:  1999-05       Impact factor: 8.739

3.  Glucosaminyl N-deacetylase in cultured fibroblasts; comparison of patients with and without diabetic nephropathy, and identification of a possible mechanism for diabetes-induced N-deacetylase inhibition.

Authors:  A Kofoed-Enevoldsen; J S Petersen; T Deckert
Journal:  Diabetologia       Date:  1993-06       Impact factor: 10.122

  3 in total

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