Characterization of chondroitin sulfate and dermatan sulfate proteoglycans of extracellular matrices of human umbilical cord blood vessels and Wharton's jelly

Manojkumar Valiyaveettil, Rajeshwara N. Achur, Arivalagan Muthusamy, Channe Gowda

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The chondroitin sulfate/dermatan sulfate proteoglycans (CS/DSPGs) of the human umbilical cord vein, arteries and Wharton's jelly matrices were characterized and localized by immunohistochemical analysis. The CS/DSPGs were found to be decorins and biglycans with 43-48 kDa core proteins and are distributed throughout the umbilical cord. A truncated form of decorin having only the ∼14 kDa NH 2-terminal portion of the core protein was found exclusively in the vein. The proteoglycans, regardless of their locations, have two types of CS/DS chains, one with ∼90% CS and ∼10% DS and the other with ∼65% CS and ∼35% DS. The glycosaminoglycan (GAG) chains of the truncated decorin consist of ∼53% CS and ∼47% DS. Both decorin and biglycan including the truncated form of decorin could efficiently bind collagen I and fibronectin. The decorin and biglycan with ∼10% DS and ∼90% CS were loosely bound in the extracellular matrices, whereas those with ∼35% DS bound strongly. Together, these data demonstrate that, the GAG chains with 35-47% DS but not those with 10% DS, interact strongly with the matrix. Our data also show that the GAG chain composition is a significant factor in binding of the decorin and biglycan to matrix proteins. The expression of decorin and biglycan with distinctively different CS/DS proportions implies specific biological functions for these PGs in the umbilical cord. The occurrence of the truncated form of decorin exclusively in the umbilical vein suggests a specific functional role.

Original languageEnglish (US)
Pages (from-to)361-375
Number of pages15
JournalGlycoconjugate Journal
Volume21
Issue number6
DOIs
StatePublished - Nov 10 2004

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Wharton Jelly
Decorin
Chondroitin Sulfates
Blood vessels
Fetal Blood
Extracellular Matrix
Blood Vessels
Biglycan
Umbilical Cord
Glycosaminoglycans
Umbilical Veins
dermatan sulfate proteoglycan
Sulfates
Cable cores
Proteins
Proteoglycans
Fibronectins
Veins
Collagen
Arteries

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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title = "Characterization of chondroitin sulfate and dermatan sulfate proteoglycans of extracellular matrices of human umbilical cord blood vessels and Wharton's jelly",
abstract = "The chondroitin sulfate/dermatan sulfate proteoglycans (CS/DSPGs) of the human umbilical cord vein, arteries and Wharton's jelly matrices were characterized and localized by immunohistochemical analysis. The CS/DSPGs were found to be decorins and biglycans with 43-48 kDa core proteins and are distributed throughout the umbilical cord. A truncated form of decorin having only the ∼14 kDa NH 2-terminal portion of the core protein was found exclusively in the vein. The proteoglycans, regardless of their locations, have two types of CS/DS chains, one with ∼90{\%} CS and ∼10{\%} DS and the other with ∼65{\%} CS and ∼35{\%} DS. The glycosaminoglycan (GAG) chains of the truncated decorin consist of ∼53{\%} CS and ∼47{\%} DS. Both decorin and biglycan including the truncated form of decorin could efficiently bind collagen I and fibronectin. The decorin and biglycan with ∼10{\%} DS and ∼90{\%} CS were loosely bound in the extracellular matrices, whereas those with ∼35{\%} DS bound strongly. Together, these data demonstrate that, the GAG chains with 35-47{\%} DS but not those with 10{\%} DS, interact strongly with the matrix. Our data also show that the GAG chain composition is a significant factor in binding of the decorin and biglycan to matrix proteins. The expression of decorin and biglycan with distinctively different CS/DS proportions implies specific biological functions for these PGs in the umbilical cord. The occurrence of the truncated form of decorin exclusively in the umbilical vein suggests a specific functional role.",
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Characterization of chondroitin sulfate and dermatan sulfate proteoglycans of extracellular matrices of human umbilical cord blood vessels and Wharton's jelly. / Valiyaveettil, Manojkumar; Achur, Rajeshwara N.; Muthusamy, Arivalagan; Gowda, Channe.

In: Glycoconjugate Journal, Vol. 21, No. 6, 10.11.2004, p. 361-375.

Research output: Contribution to journalArticle

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T1 - Characterization of chondroitin sulfate and dermatan sulfate proteoglycans of extracellular matrices of human umbilical cord blood vessels and Wharton's jelly

AU - Valiyaveettil, Manojkumar

AU - Achur, Rajeshwara N.

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AU - Gowda, Channe

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AB - The chondroitin sulfate/dermatan sulfate proteoglycans (CS/DSPGs) of the human umbilical cord vein, arteries and Wharton's jelly matrices were characterized and localized by immunohistochemical analysis. The CS/DSPGs were found to be decorins and biglycans with 43-48 kDa core proteins and are distributed throughout the umbilical cord. A truncated form of decorin having only the ∼14 kDa NH 2-terminal portion of the core protein was found exclusively in the vein. The proteoglycans, regardless of their locations, have two types of CS/DS chains, one with ∼90% CS and ∼10% DS and the other with ∼65% CS and ∼35% DS. The glycosaminoglycan (GAG) chains of the truncated decorin consist of ∼53% CS and ∼47% DS. Both decorin and biglycan including the truncated form of decorin could efficiently bind collagen I and fibronectin. The decorin and biglycan with ∼10% DS and ∼90% CS were loosely bound in the extracellular matrices, whereas those with ∼35% DS bound strongly. Together, these data demonstrate that, the GAG chains with 35-47% DS but not those with 10% DS, interact strongly with the matrix. Our data also show that the GAG chain composition is a significant factor in binding of the decorin and biglycan to matrix proteins. The expression of decorin and biglycan with distinctively different CS/DS proportions implies specific biological functions for these PGs in the umbilical cord. The occurrence of the truncated form of decorin exclusively in the umbilical vein suggests a specific functional role.

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