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MeSH Review

Basement Membrane

 
 
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Disease relevance of Basement Membrane

 

Psychiatry related information on Basement Membrane

 

High impact information on Basement Membrane

 

Chemical compound and disease context of Basement Membrane

 

Biological context of Basement Membrane

 

Anatomical context of Basement Membrane

 

Associations of Basement Membrane with chemical compounds

  • We examined the expression of laminin, a basement membrane glycoprotein, during this conversion [25].
  • Both integrin complexes are receptors for laminins, major components of basement membranes [26].
  • Both collagens resemble previously characterized type IV basement-membrane collagens with respect to their amino acid composition, cyanogen bromide peptides, chain size, immunological reactivity and tissue localization [27].
  • In the patients receiving placebo the mean width of the muscle capillary basement membrane increased from 135.9 +/- 9.0 nm (S.E.M.) to 169.3 +/- 9.5 nm (P = 0.01), but in those receiving glipizide the value decreased to a level no different from that in subjects without diabetes: from 152.9 +/- 2.9 to 127.5 +/- 5.1 nm (P = 0.01) [28].
  • We report here that in F9 12-1 cells exposed to retinoic acid, synthesis of the SV40 A gene product(s), T and tumour-associated specific antigens (TASA), parallels the appearance of the normal hallmarks of differentiation in this cell line, H-2 antigens and the basement membrane protein laminin [29].
 

Gene context of Basement Membrane

 

Analytical, diagnostic and therapeutic context of Basement Membrane

References

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  15. Glomerular basement membrane proteoglycans are derived from a large precursor. Klein, D.J., Brown, D.M., Oegema, T.R., Brenchley, P.E., Anderson, J.C., Dickinson, M.A., Horigan, E.A., Hassell, J.R. J. Cell Biol. (1988) [Pubmed]
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  21. Properties of a basement membrane-related glycoprotein synthesized in culture by a mouse embryonal carcinoma-derived cell line. Chung, A.E., Jaffe, R., Freeman, I.L., Vergnes, J.P., Braginski, J.E., Carlin, B. Cell (1979) [Pubmed]
  22. Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. Gautam, M., Noakes, P.G., Moscoso, L., Rupp, F., Scheller, R.H., Merlie, J.P., Sanes, J.R. Cell (1996) [Pubmed]
  23. The effect of diabetic control on the width of skeletal-muscle capillary basement membrane in patients with Type I diabetes mellitus. Raskin, P., Pietri, A.O., Unger, R., Shannon, W.A. N. Engl. J. Med. (1983) [Pubmed]
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  26. Absence of integrin alpha 6 leads to epidermolysis bullosa and neonatal death in mice. Georges-Labouesse, E., Messaddeq, N., Yehia, G., Cadalbert, L., Dierich, A., Le Meur, M. Nat. Genet. (1996) [Pubmed]
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  29. Expression of H-2, laminin and SV40 T and TASA on differentiation of transformed murine teratocarcinoma cells. Knowles, B.B., Pan, S., Solter, D., Linnenbach, A., Croce, C., Huebner, K. Nature (1980) [Pubmed]
  30. Chimaeric mice deficient in dystroglycans develop muscular dystrophy and have disrupted myoneural synapses. Côté, P.D., Moukhles, H., Lindenbaum, M., Carbonetto, S. Nat. Genet. (1999) [Pubmed]
  31. Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis. Aviezer, D., Hecht, D., Safran, M., Eisinger, M., David, G., Yayon, A. Cell (1994) [Pubmed]
  32. Mutation of a gene encoding a protein with extracellular matrix motifs in Usher syndrome type IIa. Eudy, J.D., Weston, M.D., Yao, S., Hoover, D.M., Rehm, H.L., Ma-Edmonds, M., Yan, D., Ahmad, I., Cheng, J.J., Ayuso, C., Cremers, C., Davenport, S., Moller, C., Talmadge, C.B., Beisel, K.W., Tamayo, M., Morton, C.C., Swaroop, A., Kimberling, W.J., Sumegi, J. Science (1998) [Pubmed]
  33. Products of the unc-52 gene in Caenorhabditis elegans are homologous to the core protein of the mammalian basement membrane heparan sulfate proteoglycan. Rogalski, T.M., Williams, B.D., Mullen, G.P., Moerman, D.G. Genes Dev. (1993) [Pubmed]
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  35. Identification of the cutaneous basement membrane zone antigen and isolation of antibody in linear immunoglobulin A bullous dermatosis. Zone, J.J., Taylor, T.B., Kadunce, D.P., Meyer, L.J. J. Clin. Invest. (1990) [Pubmed]
  36. Anti-IL-5 treatment reduces deposition of ECM proteins in the bronchial subepithelial basement membrane of mild atopic asthmatics. Flood-Page, P., Menzies-Gow, A., Phipps, S., Ying, S., Wangoo, A., Ludwig, M.S., Barnes, N., Robinson, D., Kay, A.B. J. Clin. Invest. (2003) [Pubmed]
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