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Amino acid sequence and domain structure of entactin

By Marian E. Durkin, Shukti Chakravarti, Barbara B. Bartos, Shu-huang Liu, Robert L. Friedman and Albert E. Chung


Abstract. Entactin (nidogen), a 150-kD sulfated glycoprotein, is a major component of basement membranes and forms a highly stable noncovalent complex with laminin. The complete amino acid sequence of mouse entactin has been derived from sequencing of cDNA clones. The 5.9-kb cDNA contains a 3,735-bp open reading frame followed by a 3'-untranslated region of 2.2 kb. The open reading frame encodes a 1,245-residue polypeptide with an unglycosylated Mr of 136,500, a 28-residue signal peptide, two Asnlinked glycosylation sites, and two potential Ca 2√∑binding sites. Analysis of the deduced amino acid se-B ASEMENT membranes are a type of extracellular matrix that form thin sheets separating epithelial, endothelial, muscle, fat, and nerve cells from connective tissue (51). Epithelial cells require contact with a basement membrane to maintain their morphology and differentiated phenotype, and this is a result of interactions between basement membrane molecules and cell surface receptors for them (26). The major components of basement membranes are type IV collagen, laminin, entactin, and heparan sulfate proteoglycan (reviewed in reference 48). Entactin is a 150-kD sulfated glycoprotein first identified as a product of a teratocarcinoma-derived parietal endoderm line (6). It is identical to nidogen, a polypeptide originally isolated as an 80-kD proteolytic fragment from the Engelbreth-Holm-Swarm tumor (49). Immunostaining has shown entactin to be a ubiquitous component of adult, fetal, and extraembryonic basemen

Year: 1988
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