Lysosome-associated membrane glycoproteins (lamp) are integral membrane proteins, specific to lysosomes, and whose exact biological function is not yet clear. Structurally, the lamp proteins consist of two internally homologous lysosome-luminal domains separated by a proline-rich hinge region; at the C-terminal extremity there is a transmembrane region (TM) followed by a very short cytoplasmic tail (C). In each of the duplicated domains, there are two conserved disulfide bonds. This structure is schematically represented in the figure below.
In mammals, there are two closely related types of lamp: LAMP1 and LAMP2.
CD69 (also called gp110 or macrosialin) is a heavily glycosylated integral membrane protein whose structure consists of a mucin-like domain followed by a proline-rich hinge; a single lamp-like domain; a transmembrane region and a short cytoplasmic tail.
CD molecules are leucocyte antigens on cell surfaces. CD antigens nomenclature is updated at Protein Reviews On The Web (http://mpr.nci.nih.gov/prow/).
^Fukuda M (1991). "Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking". J. Biol. Chem.266 (32): 21327–21330. PMID1939168.
^Holness CL, da Silva RP, Fawcett J, Gordon S, Simmons DL (1993). "Macrosialin, a mouse macrophage-restricted glycoprotein, is a member of the lamp/lgp family". J. Biol. Chem.268 (13): 9661–9666. PMID8486654.