The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule.

作者: D.M. Noonan , A. Fulle , P. Valente , S. Cai , E. Horigan

DOI: 10.1016/S0021-9258(18)54445-8

关键词:

摘要: A heparan sulfate proteoglycan is a component of all basement membranes. This molecule consists three side chains linked to large core protein approximately 400 kDa. We have isolated seven overlapping murine cDNA clones that encode the entire mRNA sequence 12.685 kilobases this molecule. has single open reading frame 3,707 amino acids encodes for 396 Identical or near identical matchups with nine peptide sequences derived from Engelbreth-Holm-Swarm tumor were found deduced sequence. Sequence analysis and data base comparison show consist five different domains, most which contain internal repeats. Domain I contains start methionine followed by typical signal transfer unique segment 172 probable sites attachment, SGD. II four cysteine- acidic acid-rich repeats are very similar those in LDL receptor proteins such as GP330. III cysteine-rich globular regions, both similarity short arm laminin chain. IV 14 immunoglobulin superfamily highly immunoglobulin-like neural cell adhesion V chain G domain separated epidermal growth factor-like regions not As primary structural agree appearance electron microscope series globules rods, "beads on string," we adopted name perlecan The variety domains suggest multiple interactions other molecules.

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