Rat monoclonal to LAMP2 (PerCP). Lysosme associated membrane proteins, or LAMP1 and LAMP2, are major constituents of the lysosomal membrane. The two have closely related structures, with 37% sequence homology. They are both transmembrane glycoproteins that are localized primarily in lysosomes and late endosomes. Newly synthesized molecules are mostly transported from the trans-Golgi network directly to endosomes and then to lysosomes. A second pathway involves the lamps being delivered from the Golgi to the cell surface, and then along the endocytic pathway to the lysosomes. A minor pathway involves transport via the plasma membrane. LAMP2 has also been detected at the plasma membrane of cells, as well as in cells that secrete lysosomal hydrolases. A study in the developmental expresses patterns of membrane LAMP2 transcripts indicate a possible involvement of this protein in cell-cell or cell-extracellular matrix interaction, and appear to reflect tissue and cell type specific roles of lysosomes during morphogenesis. Upon stimulation, a rapid translocation of intracellular LAMPs to the cell membrane is dependent on a carboxyl-terminal tyrosine based motif (YXXI). This stimulation has also been shown to have an associated release of histamine, leukotriene C 9$) and prostaglandin D 9@), which shows that LAMP1 and LAMP2 are activation markers for normal mast cells. They have also been linked to the inflammatory response in that they promote adhesion of human peripheral blood mononuclear cells (PBMC) to vascular endothelium, and therefore possibly the adhesion of PBMC to the site of inflammation. LAMP2 has also been shown to be critical for autophagy, in conversion of early autophagic vacuoles to vacuoles which rapidly degrade their content.