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Modifications of proteoglycans extracted from monolayer cultures of young and senescent human skin fibroblasts
Author(s) -
Passi Alberto,
Albertini Riccardo,
Campagnari Francesco,
De Luca Giancarlo
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01515-9
Subject(s) - hyaluronic acid , fibronectin , glycosaminoglycan , chemistry , polysaccharide , laminin , biochemistry , galactosamine , sulfation , proteoglycan , extracellular matrix , microbiology and biotechnology , glucosamine , biology , anatomy
Proteoglycans (PGs) were extracted from culture monolayers of human skin fibroblasts (HFs) at early and late passages. Total PGs from senescent cells had markedly reduced abilities to bind type I collagen and hyaluronic acid, but retained normal binding properties with fibronectin and laminin. The constituent polysaccharides of PGs were comparatively characterised. PGs recovered from young and senescent HF cultures had equivalent total polyanionic charges and similar size distributions of the glycosaminoglycan chains. This applied to both types of polysaccharide chains found in PGs, namely the galactosaminoglycuronans (GalN‐GAGs) and the glucosaminoglycuronans (GlcN‐GAGs). However, senescent HFs produced a greater proportion of PGs containing GlcN‐GAG chains and increased the sulphation of the remainding PG fraction with GalN‐GAG moieties, yielding a major gain of C6‐sulphate groups in the galactosamine residues.