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 (2). 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 (3).  Upon stimulation, a rapid translocation of intracellular LAMPs to the cell membrane is dependent on a carboxylterminal tyrosine ba based motif (YXXI) (1).  If there is a disturbance in this spacing, lysosome localization of LAMP1 is abolished and the mutant protein then cycles between the membrane and the endosome (3).  

This stimulation has also been shown to have an associated release of histamine, leukotriene C (4) and prostaglandin D (2), which shows that LAMP-1 and LAMP-2 are activation markers for normal mast cells (1).  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 (4).