TY - JOUR
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.
AU - Muthusamy, Arivalagan
AU - Gowda, D. Channe
N1 - Funding Information:
This study was supported by the grant AI45086 from the National Institute of Allergy and Infectious Diseases, NIH. We thank Professor Keiichi Takagaki, Department of Biochemistry, Hirosaki University School of Medicine, Hirosaki, Japan, for protein sequencing; Dr. Larry Fisher, Craniofacial and Skeletal Disease Branch, NIDR, NIH, for providing anti-decorin, and anti-biglycan antibodies.
PY - 2004
Y1 - 2004
N2 - 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.
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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U2 - 10.1023/B:GLYC.0000046276.77147.b2
DO - 10.1023/B:GLYC.0000046276.77147.b2
M3 - Article
C2 - 15514483
AN - SCOPUS:7244226481
SN - 0282-0080
VL - 21
SP - 361
EP - 375
JO - Glycoconjugate Journal
JF - Glycoconjugate Journal
IS - 6
ER -