VONDERMARK, H and DURR, J and SONNENBERG, A and VONDERMARK, K and DEUTZMANN, R and GOODMAN, SL (1991) SKELETAL MYOBLASTS UTILIZE A NOVEL BETA-1-SERIES INTEGRIN AND NOT ALPHA-6-BETA-1 FOR BINDING TO THE E8 AND T8 FRAGMENTS OF LAMININ. JOURNAL OF BIOLOGICAL CHEMISTRY, 266 (35). pp. 23593-23601. ISSN 0021-9258,
Full text not available from this repository.Abstract
The E8 fragment of laminin stimulates myoblast attachment and locomotion. Myoblast attachment to laminin/E8 was blocked by anti-integrin antibodies against beta-1-chains but not by antibodies against alpha-6-chains. By contrast, other cell lines (e.g. B16, HT1080, P19, F9, Pys2, 3T3, and 3T6) were blocked both by anti-beta-1 and anti-alpha-6. All cells tested also bound to almost-equal-to 125-kDa C-terminal fragments of E8 (T8 and T8'). Immunoprecipitation of surface-iodinated myoblasts revealed beta-1-, alpha-3-, and alpha-5-integrin chains and a novel chain that co-precipitated with anti-beta-1 antibodies running at almost-equal-to 95 kDa (reduced). I-125-alpha-6-beta-1 was immunoprecipitated from cells whose attachment to E8 was blocked by anti-alpha-6 antibodies. By contrast, little alpha-6-beta-1 could be immunoprecipitated from myoblasts. Beta-1-integrin and the novel alpha-chain (alpha'), M(r) almost-equal-to 120,000/almost-equal-to 95,000 (nonreduced/reduced), from myoblast lysates were retained during affinity chromatography on Engelbreth-Holm-Swarm-laminin affinity columns. Beta-1, alpha-1, and the novel alpha' were retained from Rugli cell lysates on Engelbreth-Holm-Swarm-laminin columns. alpha-3 was not bound. When E8 was used as affinity matrix, only beta-1 and alpha' were retained. The N-terminal sequence of Rugli alpha' was homologous to alpha-chains of beta-1-series integrins and was most similar to alpha-6 (9 identical residues out of 14). However, there were distinctive differences; in particular, 2 residues were deleted in comparison with alpha-6.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | AMINO-ACID SEQUENCE; LEUKOCYTE ADHESION GLYCOPROTEIN; COMPLEMENT RECEPTOR TYPE-3; CELL-ADHESION; ALPHA-SUBUNIT; FIBRONECTIN RECEPTOR; ONCOGENIC TRANSFORMATION; EXTRACELLULAR-MATRIX; VONWILLEBRAND-FACTOR; NEURITE OUTGROWTH; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:46 |
| URI: | https://pred.uni-regensburg.de/id/eprint/54761 |
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