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Background
Megalin, also called Lipoprotein receptor-related protein-2 (LRP2) or glycoprotein 330, is a 600- kDa transmembrane protein belonging to the LDL-receptor family. Members of this receptor family are characterized by a cluster of cysteine-rich class A repeats, epidermal growth factor (EGF)-like repeats, YWTD repeats and an O-linked sugar domain. Megalin was first discovered in 1982 as the pathogenic antigen of Heymann nephritis. The complete cDNA sequences have been characterized for rat and human Megalin. The protein contains a single transmembrane domain, is known to act as an endocytic receptor and is expressed primarily on the apical membrane domain of epithelial cells. Both the protein and its mRNA have been identified in human parathyroid cells, placental cytotrophoblasts and epididymal epithelial cells. The protein is also expressed in mammary epithelia, thyroid follicular cells, yolk sacs, the ciliary body of the eye, the intestinal brush border, the male reproductive tract, uterus and oviduct, and gallbladder epithelium. In addition, immortalised foetal rat alveolar pretype II cells, adult rat type II pneumocytes and human type II cells have all been reported to express megalin. It has been proposed that in adult lung megalin may be important in supplying vitamin E to type II pneumocytes. Specifically, Megalin mediates the uptake of apolipoprotein J, which is a binding protein for the beta-Amyloid peptide, a peptide implicated in Alzheimer's disease. It is also involved in renal uptake of Angiotensin and the reabsorption of various molecules including calcium, vitamin B12 and vitamin D.Synonyms: Glycoprotein 330, LRP-2, Low-density lipoprotein receptor-related protein 2, Megalin