NDLI: A dorso-ventral asymmetry in the embryonic retina defined by protein conformation.

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A dorso-ventral asymmetry in the embryonic retina defined by protein conformation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Neve, R. L. Mccaffery, P. Dräger, U. C.
Description	Author Affiliation: McCaffery P ( Department of Neurobiology, Harvard Medical School, Boston, MA 02115.);
Abstract	In a search for determinants of retinotopic specification we previously identified an antigen in the dorsal embryonic retina as a protein called the 68-kDa laminin receptor. A dorso-ventral asymmetry in a laminin receptor seemed consistent with the known responsiveness of embryonic optic axons to laminin, but there were three peculiar points. (i) The molecular mass of this presumed laminin receptor in immunoblots is not 68 kDa but 43 kDa, and the molecular mass of the protein deduced from the mRNA is only 33 kDa. (ii) The antigen does not have the localization expected of a receptor for the extracellular matrix: the antibodies label mainly a granular cytoplasmic antigen in dorsal retina; an additional sparse cell-surface antigen present on a few cells does not show a dorso-ventral asymmetry. (iii) Despite the pronounced dorso-ventral difference seen immunohistochemically, in immunoblots the 43-kDa protein (p40) is evenly distributed throughout the retina. Here we show that (i) native p40 and in vitro-translated gene product are indistinguishable and their anomalous migration in denaturing gels probably is due to low pI; (ii) p40 is bound in a Mg2(+)-dependent manner to large cytoplasmic complexes that appear to include ribosomes; and (iii) there is a labile conformational difference in p40 between dorsal and ventral retina: dorsally it is more accessible to proteolysis, suggesting a more open conformation. In conjunction with the recent hypothesis that p40 constitutes a translation initiation factor (D. Auth and G. Brawerman, personal communication), these observations point to a dorso-ventral asymmetry in some aspect of protein translation, which in turn may set up differences in recognition factors on retinal growth cones.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	87
Language	English
Publisher	National Academy of Sciences
Publisher Date	1990-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Receptors, Antigen Receptors, Immunologic Retina Embryology Animals Antibodies, Monoclonal Axons Physiology Cell Line Fluorescent Antibody Technique Laminin Molecular Weight Protein Biosynthesis Protein Conformation RNA, Messenger Genetics Isolation & Purification Receptors, Laminin Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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