Biological roles of dermatan sulphate proteoglycans.
Biological roles of dermatan sulphate proteoglycans.
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硫酸皮肤素蛋白聚糖的生物学作用。
DOI:
10.1002/9780470513385.ch4
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发表时间:
1986
期刊:
影响因子:
--
通讯作者:
Culp,LA
中科院分区:
文献类型:
--
作者:
Rosenberg,LC;Choi,HU;Poole,AR;Lewandowska,K;Culp,LA
Dermatan sulphate‐containing proteoglycans (DS‐PGs) are widely distributed in the extracellular matrix of skin, sclera, tendon, cartilage and a variety of other connective tissues. Two species of dermatan sulphate proteoglycans, called DS‐PGI and DS‐PGII, have recently been isolated from mature bovine articular cartilages. In their monomeric forms, both DS‐PGI and DS‐PGII are polydisperse, have relative molecular masses (Mr) ranging from 80K to 140K, and possess protein cores with apparentMrvalues of approximately 45K. DS‐PGI readily self‐associates whereas DS‐PGII does not. Polyclonal and monoclonal antibodies against DS‐PGII do not react with DS‐PGI. DS‐PGI and DS‐PGII appear to possess different core proteins and represent two different species of dermatan sulphate proteoglycans.DS‐PGs have dramatic effects on the biological functions of cells. For example, they inhibit the capacity of fibroblasts to adhere to a fibronectin substratum. BALB/c 3T3 cells were labelled with [3H]thymidine and plated onto dishes coated with plasma fibronectin, plasma fibronectin plus chondroitin sulphate proteoglycan (CS‐PG, cartilage‐specific proteoglycan monomer), or plasma fibronectin plus DS‐PGs. In the absence of proteoglycan, approximately 55% of the cells were attached at 1 h. In the presence of CS‐PG, cell attachment was slightly decreased. In the presence of DS‐PGs, the adhesion of the fibroblasts to fibronectin was essentially abolished. Similar results were obtained if a plasma fibronectin substratum was preadsorbed with the DS‐PGs and the DS‐PGs were left in the attachment medium.