Extracellular matrix in bone marrow cell cultures. Synthesis of a 45k non-collagenous protein and a 17k protein sensitive to bacterial collagenase.
Proteins produced by bone marrow constituents are of importance to hematopoiesis and osteogenesis. To elaborate the role of bone marrow in these functions the proteins synthesized by rat bone marrow cells in culture were evaluated. In addition to types I and III procollagen and fibronectin, two novel proteins were produced by the adherent stromal cells, a 45 kDa protein, and a 17 kDa protein which is sensitive to bacterial collagenase. The 45k protein is sensitive to pepsin digestion, contains no disulfide bonds, has no precursors or breakdown products on pulse-chase analysis and is maximally synthesized in young cultures (5 days old) with decreased synthesis as time in culture increases. The 17k protein is sensitive to digestion by bacterial collagenase and pepsin, appears without precursors or breakdown products on pulse-chase analysis and is maximally synthesized in 5 day old cultures. Synthesis decreases with longer times in culture. The 17k protein is not a degradation product of a collagen precursor and appears to be a novel protein in bone marrow cell cultures.
Boman
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Department of Orthopaedics, University of Virginia School of Medicine, Charlottesville 22908.
Balian
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D000818:Animals; D001853:Bone Marrow / Q000378:metabolism*; D001854:Bone Marrow Cells; D002352:Carrier Proteins / Q000096:biosynthesis*; D002478:Cells, Cultured; D005109:Extracellular Matrix / Q000378:metabolism*; D006023:Glycoproteins / Q000096:biosynthesis*; D003012:Microbial Collagenase / Q000494:pharmacology*; D008970:Molecular Weight; D015676:Osteonectin; D051381:Rats; D011919:Rats, Inbred Strains
D002352:Carrier Proteins; D006023:Glycoproteins; D015676:Osteonectin; D003012:Microbial Collagenase