Fogerty F J, Fessler L I, Bunch T A, Yaron Y, Parker C G, Nelson R E, Brower D L, Gullberg D, Fessler J H
Department of Biology, University of California, Los Angeles 90024-1606.
Development. 1994 Jul;120(7):1747-58. doi: 10.1242/dev.120.7.1747.
Genetic and other studies of Drosophila integrins have implicated these extracellular matrix receptors in various morphogenetic events, but identification of their endogenous ligands has been elusive. We report the biochemical purification and cloning of tiggrin, a novel extracellular matrix protein from Drosophila. This 255 x 10(3) M(r) polypeptide contains the potential integrin recognition sequence Arg-Gly-Asp (RGD) and 16 repeats of a novel 73-77 amino acid motif. The tiggrin gene is at chromosome locus 26D1-2 and is expressed by embryonic hemocytes and fat body cells. Tiggrin protein is detected in matrices, especially at muscle attachment sites that also strongly express integrins. Tiggrin-coated surfaces support primary embryo cell culture and provide excellent substrates for alpha PS2 beta PS integrin-mediated cell spreading. Soluble RGD-peptides inhibit this cell spreading.
对果蝇整合素的遗传学及其他研究表明，这些细胞外基质受体参与了各种形态发生事件，但它们内源性配体的鉴定一直难以实现。我们报告了从果蝇中生化纯化和克隆出的tiggrin，一种新型细胞外基质蛋白。这种255×10³ M(r)的多肽包含潜在的整合素识别序列精氨酸-甘氨酸-天冬氨酸（RGD）以及一个由73 - 77个氨基酸组成的新型基序的16个重复序列。tiggrin基因位于染色体位点26D1 - 2，由胚胎血细胞和脂肪体细胞表达。在基质中可检测到tiggrin蛋白，尤其是在也强烈表达整合素的肌肉附着位点。包被有tiggrin的表面支持原代胚胎细胞培养，并为αPS2βPS整合素介导的细胞铺展提供了优良的底物。可溶性RGD肽可抑制这种细胞铺展。
