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Gene Review

LAMP1  -  lysosomal-associated membrane protein 1

Homo sapiens

Synonyms: CD107 antigen-like family member A, CD107a, LAMP-1, LAMPA, LGP120, ...
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Disease relevance of LAMP1


High impact information on LAMP1

  • We isolated pure, viable populations of tumor-cytolytic T cells directly from patient blood samples using flow cytometric quantification of the surface mobilization of CD107a-an integral membrane protein in cytolytic granules-as a marker for degranulation after tumor stimulation [6].
  • We combined CD107a mobilization with peptide-major histocompatibility complex (P-MHC) tetramer staining to directly correlate antigen specificity and cytolytic ability on a single-cell level [6].
  • In addition to their high endocytic capacity, DCs from GM-CSF + IL-4-dependent cultures are characterized by the presence of a large intracellular compartment that contains high levels of class II molecules, cathepsin D, and lysosomal-associated membrane protein-1, and is rapidly accessible to endocytic markers [7].
  • By contrast, MARCKS and PKC alpha remained associated with the phagosome membrane until after acquisition of the lysosomal marker Lamp-1 [8].
  • By contrast, depletion of RabGAP-5 results in increased endosome size, more endosome-associated EEA1, and disrupts the trafficking of EGF and LAMP1 [9].

Chemical compound and disease context of LAMP1


Biological context of LAMP1


Anatomical context of LAMP1

  • By electron and immunofluorescent microscopy analyses, we showed that these structures are acid autolysosomes, containing cellular debris, and labeled by LC3, Rab7, and LAMP1, markers of autophagosomes, late endosomes, and lysosomes, respectively [15].
  • Using specific antibodies to ABCA2 and various organelle marker proteins, ABCA2 was found to colocalize with the lysosomal/endosomal marker LAMP1, forming discrete, punctate intracellular vesicles [16].
  • LAMP1-positive vacuoles were depleted of PtdIns(3)P in the hVps34-knockdown cells, as judged by their inability to bind the PtdIns(3)P probe GFP-2xFYVE [17].
  • We also reported that the IgA1 protease plays a major role in the ability of the pathogenic neisseriae to survive within epithelial cells and hypothesized that this is due to alteration of lysosomes as a result of protease-mediated LAMP1 degradation [1].
  • Whereas both live and heat-killed bacteria reside transiently in early endosomes, only live bacteria escape from late endosomes to colocalize in vesicles positive for lysosomal membrane marker LAMP1, endoplasmic reticulum (ER) membrane marker calnexin, and autophagosome marker monodansylcadavarine (MDC) [18].

Associations of LAMP1 with chemical compounds

  • Aspirin inhibits surface glycoprotein IIb/IIIa, P-selectin, CD63, and CD107a receptor expression on human platelets [19].
  • HL-60 cells were induced to differentiate into granulocytic cells by dimethyl sulfoxide, and structures of Asn-linked oligosaccharides attached to lysosomal membrane glycoproteins (lamp-1 and lamp-2) were elucidated before and after differentiation [20].
  • The deduced amino acid sequences indicate that h-lamp-1 and h-lamp-2 consist of 416 and 408 amino acid residues, respectively, and suggest that 27 and 28 NH2-terminal residues are cleavable signal peptides [21].
  • These N-glycosylation sites are clustered into two domains separated by a hinge-like structure enriched with proline and serine in h-lamp-1 or proline and threonine in h-lamp-2 [21].
  • Toxoplasma-containing vacuoles remained segregated from all levels of the endocytic pathway, as shown by the absence of delivery of transferrin receptors, mannose phosphate receptors, and the lysosomal-associated protein LAMP1 to the vacuole [22].

Physical interactions of LAMP1


Co-localisations of LAMP1


Regulatory relationships of LAMP1


Other interactions of LAMP1

  • PRCP antigen does not colocalize with LAMP1 on nonpermeabilized HUVECs, but it partially colocalizes in permeabilized cells [32].
  • Kinetic analysis revealed that the majority of the increase in both lamp1 and lamp2 occurred within the first 2 hr of incubation and that a subset of PBMCs maintained expression for at least 96 hr [11].
  • In contrast, after ingestion, dead bacteria colocalized with late endosome marker Rab7, and lysosome markers LAMP1 and cathepsin D, but not with calnexin or MDC [18].
  • We conclude that HT, TRP-1, and Lamp-1 gene products may function together, being expressed as a multiprotein complex within the melanosomal compartment [23].
  • The virus-containing vacuoles were also labeled with antibodies against LAMP-1, CD81, and CD82, which were also incorporated into the viral envelope [33].

Analytical, diagnostic and therapeutic context of LAMP1


  1. Infection of epithelial cells by pathogenic neisseriae reduces the levels of multiple lysosomal constituents. Ayala, P., Lin, L., Hopper, S., Fukuda, M., So, M. Infect. Immun. (1998) [Pubmed]
  2. The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2. Localization on the peptide backbones. Carlsson, S.R., Fukuda, M. J. Biol. Chem. (1990) [Pubmed]
  3. The genes of major lysosomal membrane glycoproteins, lamp-1 and lamp-2. 5'-flanking sequence of lamp-2 gene and comparison of exon organization in two genes. Sawada, R., Jardine, K.A., Fukuda, M. J. Biol. Chem. (1993) [Pubmed]
  4. CD56dimCD16neg cells are responsible for natural cytotoxicity against tumor targets. Penack, O., Gentilini, C., Fischer, L., Asemissen, A.M., Scheibenbogen, C., Thiel, E., Uharek, L. Leukemia (2005) [Pubmed]
  5. Expression of Lamp-1 and Lamp-2 and their interactions with galectin-3 in human tumor cells. Sarafian, V., Jadot, M., Foidart, J.M., Letesson, J.J., Van den Brûle, F., Castronovo, V., Wattiaux, R., Coninck, S.W. Int. J. Cancer (1998) [Pubmed]
  6. Ex vivo identification, isolation and analysis of tumor-cytolytic T cells. Rubio, V., Stuge, T.B., Singh, N., Betts, M.R., Weber, J.S., Roederer, M., Lee, P.P. Nat. Med. (2003) [Pubmed]
  7. Dendritic cells use macropinocytosis and the mannose receptor to concentrate macromolecules in the major histocompatibility complex class II compartment: downregulation by cytokines and bacterial products. Sallusto, F., Cella, M., Danieli, C., Lanzavecchia, A. J. Exp. Med. (1995) [Pubmed]
  8. A role for MARCKS, the alpha isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages. Allen, L.H., Aderem, A. J. Exp. Med. (1995) [Pubmed]
  9. A GTPase-activating protein controls Rab5 function in endocytic trafficking. Haas, A.K., Fuchs, E., Kopajtich, R., Barr, F.A. Nat. Cell Biol. (2005) [Pubmed]
  10. The Neisseria type 2 IgA1 protease cleaves LAMP1 and promotes survival of bacteria within epithelial cells. Lin, L., Ayala, P., Larson, J., Mulks, M., Fukuda, M., Carlsson, S.R., Enns, C., So, M. Mol. Microbiol. (1997) [Pubmed]
  11. Lysosome-associated membrane proteins h-LAMP1 (CD107a) and h-LAMP2 (CD107b) are activation-dependent cell surface glycoproteins in human peripheral blood mononuclear cells which mediate cell adhesion to vascular endothelium. Kannan, K., Stewart, R.M., Bounds, W., Carlsson, S.R., Fukuda, M., Betzing, K.W., Holcombe, R.F. Cell. Immunol. (1996) [Pubmed]
  12. Impaired recruitment of the small GTPase rab7 correlates with the inhibition of phagosome maturation by Leishmania donovani promastigotes. Scianimanico, S., Desrosiers, M., Dermine, J.F., Méresse, S., Descoteaux, A., Desjardins, M. Cell. Microbiol. (1999) [Pubmed]
  13. Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement. Carlsson, S.R., Fukuda, M. J. Biol. Chem. (1989) [Pubmed]
  14. Two human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2, are encoded by genes localized to chromosome 13q34 and chromosome Xq24-25, respectively. Mattei, M.G., Matterson, J., Chen, J.W., Williams, M.A., Fukuda, M. J. Biol. Chem. (1990) [Pubmed]
  15. Disruption of autophagy at the maturation step by the carcinogen lindane is associated with the sustained mitogen-activated protein kinase/extracellular signal-regulated kinase activity. Corcelle, E., Nebout, M., Bekri, S., Gauthier, N., Hofman, P., Poujeol, P., Fénichel, P., Mograbi, B. Cancer Res. (2006) [Pubmed]
  16. Cloning and characterization of human adenosine 5'-triphosphate-binding cassette, sub-family A, transporter 2 (ABCA2). Vulevic, B., Chen, Z., Boyd, J.T., Davis, W., Walsh, E.S., Belinsky, M.G., Tew, K.D. Cancer Res. (2001) [Pubmed]
  17. Gene silencing reveals a specific function of hVps34 phosphatidylinositol 3-kinase in late versus early endosomes. Johnson, E.E., Overmeyer, J.H., Gunning, W.T., Maltese, W.A. J. Cell. Sci. (2006) [Pubmed]
  18. Intracellular trafficking and replication of Burkholderia cenocepacia in human cystic fibrosis airway epithelial cells. Sajjan, U.S., Yang, J.H., Hershenson, M.B., LiPuma, J.J. Cell. Microbiol. (2006) [Pubmed]
  19. Aspirin inhibits surface glycoprotein IIb/IIIa, P-selectin, CD63, and CD107a receptor expression on human platelets. McKenzie, M.E., Malinin, A.I., Bell, C.R., Dzhanashvili, A., Horowitz, E.D., Oshrine, B.R., Atar, D., Serebruany, V.L. Blood Coagul. Fibrinolysis (2003) [Pubmed]
  20. Granulocytic differentiation of HL-60 cells is associated with increase of poly-N-acetyllactosamine in Asn-linked oligosaccharides attached to human lysosomal membrane glycoproteins. Lee, N., Wang, W.C., Fukuda, M. J. Biol. Chem. (1990) [Pubmed]
  21. Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences. Fukuda, M., Viitala, J., Matteson, J., Carlsson, S.R. J. Biol. Chem. (1988) [Pubmed]
  22. Toxoplasma gondii resides in a vacuole that avoids fusion with host cell endocytic and exocytic vesicular trafficking pathways. Mordue, D.G., Håkansson, S., Niesman, I., Sibley, L.D. Exp. Parasitol. (1999) [Pubmed]
  23. Cotransfection of genes encoding human tyrosinase and tyrosinase-related protein-1 prevents melanocyte death and enhances melanin pigmentation and gene expression of Lamp-1. Luo, D., Chen, H., Jimbow, K. Exp. Cell Res. (1994) [Pubmed]
  24. Identification of the lysosomal membrane glycoprotein Lamp-1 as a receptor for type-1-fimbriated (mannose-specific) Escherichia coli. Karlsson, A., Carlsson, S.R., Dahlgren, C. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  25. Cellular uptake of amelogenin, and its localization to CD63, and Lamp1-positive vesicles. Shapiro, J.L., Wen, X., Okamoto, C.T., Wang, H.J., Lyngstadaas, S.P., Goldberg, M., Snead, M.L., Paine, M.L. Cell. Mol. Life Sci. (2007) [Pubmed]
  26. Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation. Chang, M.H., Hua, C.T., Isaac, E.L., Litjens, T., Hodge, G., Karageorgos, L.E., Meikle, P.J. Biochem. J. (2004) [Pubmed]
  27. The growth-regulatory protein HCRP1/hVps37A is a subunit of mammalian ESCRT-I and mediates receptor down-regulation. Bache, K.G., Slagsvold, T., Cabezas, A., Rosendal, K.R., Raiborg, C., Stenmark, H. Mol. Biol. Cell (2004) [Pubmed]
  28. Identification of lysosome-associated membrane protein-2 as an activation-dependent platelet surface glycoprotein. Silverstein, R.L., Febbraio, M. Blood (1992) [Pubmed]
  29. Lysosome-associated membrane protein-1-mediated targeting of the HIV-1 envelope protein to an endosomal/lysosomal compartment enhances its presentation to MHC class II-restricted T cells. Rowell, J.F., Ruff, A.L., Guarnieri, F.G., Staveley-O'Carroll, K., Lin, X., Tang, J., August, J.T., Siliciano, R.F. J. Immunol. (1995) [Pubmed]
  30. Forskolin blocks the apical expression of dipeptidyl peptidase IV in Caco-2 cells and induces its retention in lamp-1-containing vesicles. Baricault, L., Garcia, M., Cibert, C., Sapin, C., Geraud, G., Codogno, P., Trugnan, G. Exp. Cell Res. (1993) [Pubmed]
  31. Neisseria gonorrhoeae porin P1.B induces endosome exocytosis and a redistribution of Lamp1 to the plasma membrane. Ayala, P., Vasquez, B., Wetzler, L., So, M. Infect. Immun. (2002) [Pubmed]
  32. Recombinant prolylcarboxypeptidase activates plasma prekallikrein. Shariat-Madar, Z., Mahdi, F., Schmaier, A.H. Blood (2004) [Pubmed]
  33. Infectious HIV-1 assembles in late endosomes in primary macrophages. Pelchen-Matthews, A., Kramer, B., Marsh, M. J. Cell Biol. (2003) [Pubmed]
  34. Abnormal lysosomal trafficking and enhanced exosomal export of cisplatin in drug-resistant human ovarian carcinoma cells. Safaei, R., Larson, B.J., Cheng, T.C., Gibson, M.A., Otani, S., Naerdemann, W., Howell, S.B. Mol. Cancer Ther. (2005) [Pubmed]
  35. Lysosomal integral membrane glycoproteins are expressed at high levels in the inclusion bodies of I-cell disease fibroblasts. Sandoval, I.V., Chen, J.W., Yuan, L., August, J.T. Arch. Biochem. Biophys. (1989) [Pubmed]
  36. Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2. Carlsson, S.R., Lycksell, P.O., Fukuda, M. Arch. Biochem. Biophys. (1993) [Pubmed]
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