Incorporation into Reichert's membrane of laminin-like extracellular proteins synthesized by parietal endoderm cells of the mouse embryo
1980; Elsevier BV; Volume: 80; Issue: 2 Linguagem: Inglês
10.1016/0012-1606(80)90405-4
ISSN1095-564X
AutoresBrigid L.M. Hogan, Ashley R. Cooper, Markku Kurkinen,
Tópico(s)RNA Interference and Gene Delivery
ResumoParietal endoderm cells attached to Reichert's membranes from 8.5- to 14.5-day mouse embryos synthesize the high molecular weight polypeptides PYSA (450K daltons), PYSB (230K and 240K daltons), and PYSC (150K daltons), in addition to Type IV procollagen. PYSA, B, and C can be immunoprecipitated from the culture medium with highly purified antibodies to laminin, a basement membrane glycoprotein recently characterized by R. Timpl, H. Rohde, P. G. Robey, S. I. Rennard, J.-M. Foidart, and G. R. Martin (1979,J. Biol. Chem. 254, 9933–9937). Newly synthesized PYSA, B, and C are incorporated into Reichert's membranein vitro, even when the incorporation of newly synthesized Type IV procollagen is blocked by incubating the cultures with α,α′-bipyridyl, which inhibits the hydroxylation of lysine and proline. PYSA, B, and C appear to form a major part of the protein of Reichert's membrane extractable with SDS at 100°C under reducing conditions.
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