Abstract
The complete primary structure of perlecan, the large low-density proteoglycan of basement membranes, has been deduced by cDNA cloning for the mouse and more recently the human gene products. Mouse perlecan contains a 396 kDa core protein with five distinct domains: a heparan sulfate attachment domain, a LDL receptor-like domain, two different laminin-like domains and an N-CAM-like domain. These domains are conserved to a striking degree between mouse and human, including alternate splicing of the N-CAM domain to generate variations of perlecan. These variant sequences also appear to be highly conserved between mouse and human. The strong conservation of these domains, including highly repetitive elements and potential alternative splices, suggest they have vital functions.
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