Lysosome-associated membrane proteins (LAMP1 and LAMP2) are major constituents of the lysosomal membrane. These two proteins have closely related structures with 37% sequence homology. Both are transmembrane glycoproteins localized primarily in lysosomes and late endosomes. LAMP2 has also been detected at the plasma membrane of cells undergoing differentiation and activation and in cells that secrete lysosomal hydrolases. In addition, it has been suggested that LAMP2 is involved in cell-cell or cell-extracellular matrix interactions. Cell surface LAMP1 and LAMP2 promote adhesion of human peripheral blood mononuclear cells (PBMC) to vascular endothelium which suggests that the LAMP proteins are involved in adhesion of PBMC to sites of inflammation. Studies with LAMP2-deficient mice indicate that involvement of LAMP2 is critical in the conversion of early autophagic vacuoles to vacuoles which rapidly degrade their contents. Defects in LAMP2 are associated with Danon disease.
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