Extracellular matrix proteoglycans and cell-substratum adhesion of human endothelial cells: the effect of methyl β-d-xylopyranoside

Portia B. Gordon, Diane R. Zanger, Victor Bernard Hatcher

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The influence of methyl β-d-xylopyranoside on human endothelial cell proteoglycans isolated from the medium and extracellular matrix was investigated. Confluent cultures of human endothelial cells incorporate significant amounts of heparan sulfate (78%), chondroitin sulfate (10%), and dermatan sulfate (12%) into the extracellular matrix. Chondroitin sulfate (35%) and dermatan sulfate (37%) were the major glycosaminoglycans present in the medium. In the presence of methyl β-d-xylopyranoside, incorporation of labeled proteoglycans into extracellular matrix was diminished by ∼ 70%. Heparan sulfate comprised the major proteoglycan present in extracellular matrix (89%) in cells grown in the presence of methyl β-d-xylopyranoside. In contrast to the incorporation of proteoglycan into extracellular matrix, methyl β-d-xylopyranoside stimulated the secretion of labeled glycosaminoglycan chains into the medium 2.5-fold. In the presence of methyl β-d-xylopyranoside, secretion of chondroitin sulfate into the medium was markedly stimulated, with a slight increase in secretion of heparan sulfate. Chondroitin sulfate (62%) and heparan sulfate (34%) were the major labele glycosaminoglycans present in medium from methyl β-d-xylopyranoside-treated cultures. Th effect of methyl β-d-xylopyranoside on cell adhesion and detachment was investigated. Cell detachment from extracellular matrix depleted of proteoglycan was significantly faster than detachment from normal matrix. Converedly, human endothelial cells adhered faster to normal matrix than to matrix depleted of proteoglycan.

Original languageEnglish (US)
Pages (from-to)121-134
Number of pages14
JournalCarbohydrate Research
Volume151
Issue numberC
DOIs
StatePublished - Aug 15 1986

Fingerprint

Cell adhesion
Endothelial cells
Proteoglycans
Cell Adhesion
Extracellular Matrix
Heparitin Sulfate
Endothelial Cells
Chondroitin Sulfates
Glycosaminoglycans
Dermatan Sulfate
Cell culture
methyl xylopyranoside
Cells

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry

Cite this

Extracellular matrix proteoglycans and cell-substratum adhesion of human endothelial cells : the effect of methyl β-d-xylopyranoside. / Gordon, Portia B.; Zanger, Diane R.; Hatcher, Victor Bernard.

In: Carbohydrate Research, Vol. 151, No. C, 15.08.1986, p. 121-134.

Research output: Contribution to journalArticle

@article{ee5ec6217b4c4f91bd0dbf07990875fa,
title = "Extracellular matrix proteoglycans and cell-substratum adhesion of human endothelial cells: the effect of methyl β-d-xylopyranoside",
abstract = "The influence of methyl β-d-xylopyranoside on human endothelial cell proteoglycans isolated from the medium and extracellular matrix was investigated. Confluent cultures of human endothelial cells incorporate significant amounts of heparan sulfate (78{\%}), chondroitin sulfate (10{\%}), and dermatan sulfate (12{\%}) into the extracellular matrix. Chondroitin sulfate (35{\%}) and dermatan sulfate (37{\%}) were the major glycosaminoglycans present in the medium. In the presence of methyl β-d-xylopyranoside, incorporation of labeled proteoglycans into extracellular matrix was diminished by ∼ 70{\%}. Heparan sulfate comprised the major proteoglycan present in extracellular matrix (89{\%}) in cells grown in the presence of methyl β-d-xylopyranoside. In contrast to the incorporation of proteoglycan into extracellular matrix, methyl β-d-xylopyranoside stimulated the secretion of labeled glycosaminoglycan chains into the medium 2.5-fold. In the presence of methyl β-d-xylopyranoside, secretion of chondroitin sulfate into the medium was markedly stimulated, with a slight increase in secretion of heparan sulfate. Chondroitin sulfate (62{\%}) and heparan sulfate (34{\%}) were the major labele glycosaminoglycans present in medium from methyl β-d-xylopyranoside-treated cultures. Th effect of methyl β-d-xylopyranoside on cell adhesion and detachment was investigated. Cell detachment from extracellular matrix depleted of proteoglycan was significantly faster than detachment from normal matrix. Converedly, human endothelial cells adhered faster to normal matrix than to matrix depleted of proteoglycan.",
author = "Gordon, {Portia B.} and Zanger, {Diane R.} and Hatcher, {Victor Bernard}",
year = "1986",
month = "8",
day = "15",
doi = "10.1016/S0008-6215(00)90334-3",
language = "English (US)",
volume = "151",
pages = "121--134",
journal = "Carbohydrate Research",
issn = "0008-6215",
publisher = "Elsevier BV",
number = "C",

}

TY - JOUR

T1 - Extracellular matrix proteoglycans and cell-substratum adhesion of human endothelial cells

T2 - the effect of methyl β-d-xylopyranoside

AU - Gordon, Portia B.

AU - Zanger, Diane R.

AU - Hatcher, Victor Bernard

PY - 1986/8/15

Y1 - 1986/8/15

N2 - The influence of methyl β-d-xylopyranoside on human endothelial cell proteoglycans isolated from the medium and extracellular matrix was investigated. Confluent cultures of human endothelial cells incorporate significant amounts of heparan sulfate (78%), chondroitin sulfate (10%), and dermatan sulfate (12%) into the extracellular matrix. Chondroitin sulfate (35%) and dermatan sulfate (37%) were the major glycosaminoglycans present in the medium. In the presence of methyl β-d-xylopyranoside, incorporation of labeled proteoglycans into extracellular matrix was diminished by ∼ 70%. Heparan sulfate comprised the major proteoglycan present in extracellular matrix (89%) in cells grown in the presence of methyl β-d-xylopyranoside. In contrast to the incorporation of proteoglycan into extracellular matrix, methyl β-d-xylopyranoside stimulated the secretion of labeled glycosaminoglycan chains into the medium 2.5-fold. In the presence of methyl β-d-xylopyranoside, secretion of chondroitin sulfate into the medium was markedly stimulated, with a slight increase in secretion of heparan sulfate. Chondroitin sulfate (62%) and heparan sulfate (34%) were the major labele glycosaminoglycans present in medium from methyl β-d-xylopyranoside-treated cultures. Th effect of methyl β-d-xylopyranoside on cell adhesion and detachment was investigated. Cell detachment from extracellular matrix depleted of proteoglycan was significantly faster than detachment from normal matrix. Converedly, human endothelial cells adhered faster to normal matrix than to matrix depleted of proteoglycan.

AB - The influence of methyl β-d-xylopyranoside on human endothelial cell proteoglycans isolated from the medium and extracellular matrix was investigated. Confluent cultures of human endothelial cells incorporate significant amounts of heparan sulfate (78%), chondroitin sulfate (10%), and dermatan sulfate (12%) into the extracellular matrix. Chondroitin sulfate (35%) and dermatan sulfate (37%) were the major glycosaminoglycans present in the medium. In the presence of methyl β-d-xylopyranoside, incorporation of labeled proteoglycans into extracellular matrix was diminished by ∼ 70%. Heparan sulfate comprised the major proteoglycan present in extracellular matrix (89%) in cells grown in the presence of methyl β-d-xylopyranoside. In contrast to the incorporation of proteoglycan into extracellular matrix, methyl β-d-xylopyranoside stimulated the secretion of labeled glycosaminoglycan chains into the medium 2.5-fold. In the presence of methyl β-d-xylopyranoside, secretion of chondroitin sulfate into the medium was markedly stimulated, with a slight increase in secretion of heparan sulfate. Chondroitin sulfate (62%) and heparan sulfate (34%) were the major labele glycosaminoglycans present in medium from methyl β-d-xylopyranoside-treated cultures. Th effect of methyl β-d-xylopyranoside on cell adhesion and detachment was investigated. Cell detachment from extracellular matrix depleted of proteoglycan was significantly faster than detachment from normal matrix. Converedly, human endothelial cells adhered faster to normal matrix than to matrix depleted of proteoglycan.

UR - http://www.scopus.com/inward/record.url?scp=0023050041&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023050041&partnerID=8YFLogxK

U2 - 10.1016/S0008-6215(00)90334-3

DO - 10.1016/S0008-6215(00)90334-3

M3 - Article

C2 - 3768884

AN - SCOPUS:0023050041

VL - 151

SP - 121

EP - 134

JO - Carbohydrate Research

JF - Carbohydrate Research

SN - 0008-6215

IS - C

ER -