Migration stimulating factor (MSF): its structure, mode of action and possible function in health and disease.

作者: S L Schor , I Ellis , A M Grey , A M Schor , B Coles

DOI:

关键词: Internal medicineChemistryGene productCell biologyCell migrationFibroblast migrationFibronectinEndocrinologyFibroblastProteolysisWound healingMolecular mass

摘要: We have previously reported that (a) fetal fibroblasts migrate into 3-dimensional collagen matrices to a significantly greater extent do adult cells, (b) this difference in migratory behaviour results from the secretion by of "migration stimulating factor" (MSF), and (c) retain responsiveness MSF, providing basis bioassay for monitoring factor activity. Using recently modified purification protocol, MSF isolated fibroblast conditioned medium elutes as single activity peak penultimate Mono Q anion exchange chromatography step. Analysis material SDS-PAGE indicates it consists three proteins, one with an apparent molecular mass 119 kDa doublet masses approximately 43 33 kDa, respectively. Our data suggest two proteins comprising result degradation larger molecule during procedure. Both species lower weight stimulate migration (with half maximal region 1-10 pg/ml) contain structural domain exhibiting significant amino acid sequence homology gelatin-binding fragment (GBF) fibronectin. Bona fide preparations GBF, obtained limited proteolysis plasma fibronectin, also similar dose-dependent manner MSF. In spite similarity, GBF differ terms number biological biochemical parameters, thereby suggesting is distinct gene product not proteolytic stimulates synthesis high hyaluronic (HA). current observed effect on cell actually secondary consequence accumulation HA matrix. TGF-beta potent inhibitor both its effects synthesis. As present wound fluid, we suggested inhibition may reflect antagonistic interaction these cytokines control healing process. recent indicate discrete minority subpopulations MSF-secreting are at specific sites healthy undergo transient local expansion healing.(ABSTRACT TRUNCATED AT 400 WORDS)

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