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Identification of a bone matrix-derived chemotactic factor (1983)

Somerman, M. ; Hewitt, A. T. ; Varner, H. H. ; [et al.]

Springer

Calcified tissue international 35 (1983), S. 481-485

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ISSN: 1432-0827

Keywords: Chemotaxis ; Bone ; Osteoblasts ; Bone proteins

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine , Physics

Notes: Summary When demineralized bone matrix powder is implanted subcutaneously in the rat, the early responses involve the appearance and proliferation of mesenchymal cells at the site of implantation, followed by cartilage and bone formation. The ability of cells to migrate to the implant suggests that chemotaxis may be a critical event in this process. Therefore, using the modified Boyden chamber assay, we tested extracts of demineralized bone matrix for chemotactic activity. We have identified and partially purified, on molecular sieve chromatography, a heat labile and trypsin-sensitive protein (Mr=60,000–70,000) that is a potent chemoattractant for mouse calvaria, osteoblast-like cells (MMB-1), but not for monocytes (putative osteoclast precursors). These findings suggest that chemotactic protein(s) have a significant role in the recruitment of osteoprogenitor cells to a site of bone repair.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02405081

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Cellular and metabolic specificity in the interaction of adhesion proteins with collagen and with cells (1979)

Kleinman, H. K. ; Hewitt, A. T. ; Murray, J. C. ; [et al.]

New York, N.Y. : Wiley-Blackwell

Journal of Supramolecular Structure 11 (1979), S. 69-78

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ISSN: 0091-7419

Keywords: cell adhesion ; adhesion proteins ; fibronectin ; chondronectin ; collagen substrates ; gangliosides ; cell surface ; Life Sciences ; Molecular Cell Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: Fibronectin mediates the adhesion of fibroblasts to collagen substrates, binding first to the collagen and then to the cells. We report here that the interaction of the cells with the fibronectin-collagen complex is blocked by specific gangliosides, GD1 a and GT1, and that the sugar moieties of these gangliosides contain the inhibitory activity. The gangliosides act by binding to fibronectin, suggesting that they may be the cell surface receptor for fibronectin. Evidence is presented that other adhesion proteins or mechanisms of attachment exist for chondrocytes, epidermal cells, and transformed tumorigenic cells, since adhesion of these cells is not stimulated by fibronectin. Chondrocytes adhere via a serum factor that is more temperature-sensitive and less basic than fibronectin. Unlike that of fibroblasts chondrocyte adhesion is stimulated by low levels of gangliosides. Epidermal cells adhere preferentially to type IV (basement membrane) collagen but at a much slower rate than fibroblasts or chondrocytes. This suggests that these epidermal cells synthesize their own specific adhesion factor. Metastatic cells cultured from the T241 fibrosarcoma adhere rapidly to type IV collagen in the absence of fibronectin and do not synthesize significant amounts of collagen or fibronectin. Their growth, in contrast to that of normal fibroblasts, is unaffected by a specific inhibitor of collagen synthesis. These data indicate the importance of specific collagens and adhesion proteins in the adhesion of certain cells and suggest that a reduction in the synthesis of collagen and of fibronectin is related to some of the abnormalities observed in transformed cells.

Additional Material: 4 Ill.