AI Article Synopsis
- Researchers established optimal conditions to measure platelet growth factor activity in human palmar fascia fibroblasts.
- The active fraction obtained from crude platelet extract was characterized, showing it had a molecular mass of about 12,000 daltons and an isoelectric point greater than pH 9.
- The growth factor not only stimulated DNA synthesis but also increased collagen and glycosaminoglycan production in fibroblasts, highlighting its importance in cellular growth and tissue repair.
Article Abstract
Optimal conditions for determining the mitogenic activity of platelet growth factor in a homologous system (human palmar fascia fibroblasts/human platelet growth factor) were established. With the aid of this system it was possible to test the active fraction from crude platelet extract following affinity chromatography on heparin-Sepharose, chromatofocusing and molecular sieve filtration. This fraction has an isoelectric point of pH greater than 9 with a molecular mass of about 12000 daltons and reacts with beta-thromboglobulin antiserum. The addition of protease inhibitors proved essential for the isolation of the active growth factor, in order to prevent proteolytic degradation to a biologically inactive substance that is immunologically identical to beta-thromboglobulin. In addition to stimulation of DNA synthesis, the isolated growth factor induces enhanced synthesis of collagen and glycosaminoglycans in fibroblasts in vitro.
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| http://dx.doi.org/10.1515/cclm.1984.22.8.527 | DOI Listing |
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