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Volume 4 (2004), Pages 1017-1026
Research Article

Age-Related Molecular Polymorphism of the Heterodimeric Proteoglycan Bisdermican

1Departments of Obstetrics and Gynecology, Münster University Hospital, Münster, Germany
2Departments of Physiological Chemistry and Pathobiochemistry, Münster University Hospital, Münster, Germany

Received 28 October 2004; Revised 17 November 2004; Accepted 19 November 2004

Copyright © 2004 Martin Götte et al.


Bisdermican (PG760) is a large, heterodimeric, dermatan sulfate proteoglycan found in selected basement membranes, smooth muscle cell layers, and different extracellular matrices. Age-dependent and developmentally regulated alterations in glycosaminoglycan structure and quantity have been shown to be functionally relevant for a number of physiological and pathological processes. Bisdermican was purified from human skin fibroblast cultures of different age and confluency. Following β-elimination, glycosaminoglycan chains were analyzed by Sephacryl-S-300 chromatography. Glycosaminoglycan chains of Bisdermican from infantile fibroblasts had a molecular weight of 19 kDa, whereas the glycosaminoglycan chain of the large Bisdermican subunit purified from confluent fetal fibroblast secretions was slightly larger (Mr = 24 kDa). Bisdermican derived from subconfluent cultures of fetal fibroblasts displayed the largest glycosaminoglycan chains with a molecular weight of 31.5 kDa for the large subunit, and a molecular weight of 22 kDa for the small subunit. Thus, Bisdermican displays a molecular polymorphism that is related to its chronological age and proliferative state.