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Gene Review

LAMP2  -  lysosomal-associated membrane protein 2

Homo sapiens

Synonyms: CD107 antigen-like family member B, CD107b, LAMP-2, LAMPB, LGP110, ...
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Disease relevance of LAMP2

  • Here, we report that neisseria infection also reduces the levels of three other lysosomal markers: LAMP2, lysosomal acid phosphatase (LAP), and CD63 [1].
  • CONCLUSIONS: LAMP2 mutations may account for a significant proportion of cases of HCM in children, especially when skeletal myopathy and/or WPW is present, suggesting that Danon disease is an underrecognized entity in the pediatric cardiology community [2].
  • The teenage sister of the proband is a carrier of the same LAMP2 mutation and has HCM without skeletal myopathy or WPW [2].
  • CONCLUSIONS: LAMP2 mutations typically cause multisystem glycogen-storage disease (Danon's disease) but can also present as a primary cardiomyopathy [3].
  • Clinical features associated with defects in LAMP2 included male sex, severe hypertrophy, early onset (at 8 to 17 years of age), ventricular preexcitation, and asymptomatic elevations of two serum proteins [3].

Psychiatry related information on LAMP2


High impact information on LAMP2


Chemical compound and disease context of LAMP2


Biological context of LAMP2


Anatomical context of LAMP2

  • Cells that lack LAMP2 expression showed an enhanced accumulation of vacuoles carrying the marker LC3, yet a decreased colocalization of LC3 and lysosomes, suggesting that the fusion between autophagic vacuoles and lysosomes was inhibited [9].
  • While a fraction of mitochondria from starved LAMP2-expressing cells colocalized with lysosomal markers, within autophagolysosomes, no such colocalization was found on removal of LAMP2 from the experimental system [9].
  • METHODS AND RESULTS: LAMP2 was amplified from genomic DNA isolated from peripheral lymphocytes of 50 patients diagnosed with HCM and analyzed by direct DNA sequencing [2].
  • Six sarcomere gene mutations were found in 7 samples; no samples contained mutations in GLA, PRKAG2, or LAMP2 [13].
  • Functional analysis utilizing a fluorescence-based adhesion assay revealed that cell surface lamp2 mediates adhesion of PBMCs to vascular endothelium, possibly by interacting with endothelial selectins [11].

Associations of LAMP2 with chemical compounds


Physical interactions of LAMP2

  • The bacteria bound readily to Lamp-1 while there was almost no binding to Lamp-2 [18].

Co-localisations of LAMP2


Regulatory relationships of LAMP2


Other interactions of LAMP2

  • 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].
  • Genetic analyses of 20 subjects with massive hypertrophy (left ventricular wall thickness, > or =30 mm) but without electrophysiological abnormalities revealed mutations in neither LAMP2 nor PRKAG2 [3].
  • The findings are consistent with the results obtained by endo-beta-N-acetylglucosaminidase F treatment of h-lamp-1 and h-lamp-2 precursors, described in the preceding paper (Carlsson, S. R., Roth, J., Piller, F., and Fukuda, M. (1988) J. Biol. Chem. 263, 18911-18919) [16].
  • In contrast, the BACE-LL/AA mutant, in which Leu(499) and Leu(500) in the COOH-terminal sequence (DDISLLK) were replaced by alanines, only partially co-localized with LAMP2-positive compartments following inhibition of lysosomal hydrolases [21].
  • Furthermore, the selective degradation of LAMP-1 and LAMP-2, as well as LIMP-2, was also observed by treatment of the lysosomal membrane fraction isolated from wild-type macrophages with purified cathepsin E at pH 5 [22].

Analytical, diagnostic and therapeutic context of LAMP2


  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. Danon disease as an underrecognized cause of hypertrophic cardiomyopathy in children. Yang, Z., McMahon, C.J., Smith, L.R., Bersola, J., Adesina, A.M., Breinholt, J.P., Kearney, D.L., Dreyer, W.J., Denfield, S.W., Price, J.F., Grenier, M., Kertesz, N.J., Clunie, S.K., Fernbach, S.D., Southern, J.F., Berger, S., Towbin, J.A., Bowles, K.R., Bowles, N.E. Circulation (2005) [Pubmed]
  3. Glycogen storage diseases presenting as hypertrophic cardiomyopathy. Arad, M., Maron, B.J., Gorham, J.M., Johnson, W.H., Saul, J.P., Perez-Atayde, A.R., Spirito, P., Wright, G.B., Kanter, R.J., Seidman, C.E., Seidman, J.G. N. Engl. J. Med. (2005) [Pubmed]
  4. Generalized lysosome-associated membrane protein-2 defect explains multisystem clinical involvement and allows leukocyte diagnostic screening in danon disease. Fanin, M., Nascimbeni, A.C., Fulizio, L., Spinazzi, M., Melacini, P., Angelini, C. Am. J. Pathol. (2006) [Pubmed]
  5. Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease). Nishino, I., Fu, J., Tanji, K., Yamada, T., Shimojo, S., Koori, T., Mora, M., Riggs, J.E., Oh, S.J., Koga, Y., Sue, C.M., Yamamoto, A., Murakami, N., Shanske, S., Byrne, E., Bonilla, E., Nonaka, I., DiMauro, S., Hirano, M. Nature (2000) [Pubmed]
  6. Lamp-2a facilitates MHC class II presentation of cytoplasmic antigens. Zhou, D., Li, P., Lin, Y., Lott, J.M., Hislop, A.D., Canaday, D.H., Brutkiewicz, R.R., Blum, J.S. Immunity (2005) [Pubmed]
  7. At the acidic edge: emerging functions for lysosomal membrane proteins. Eskelinen, E.L., Tanaka, Y., Saftig, P. Trends Cell Biol. (2003) [Pubmed]
  8. Influences of the lysosomal associated membrane proteins (Lamp-1, Lamp-2) and Mac-2 binding protein (Mac-2-BP) on the prognosis of pancreatic carcinoma. Künzli, B.M., Berberat, P.O., Zhu, Z.W., Martignoni, M., Kleeff, J., Tempia-Caliera, A.A., Fukuda, M., Zimmermann, A., Friess, H., Büchler, M.W. Cancer (2002) [Pubmed]
  9. The apoptosis/autophagy paradox: autophagic vacuolization before apoptotic death. González-Polo, R.A., Boya, P., Pauleau, A.L., Jalil, A., Larochette, N., Souquère, S., Eskelinen, E.L., Pierron, G., Saftig, P., Kroemer, G. J. Cell. Sci. (2005) [Pubmed]
  10. Single-gene mutations and increased left ventricular wall thickness in the community: the Framingham Heart Study. Morita, H., Larson, M.G., Barr, S.C., Vasan, R.S., O'Donnell, C.J., Hirschhorn, J.N., Levy, D., Corey, D., Seidman, C.E., Seidman, J.G., Benjamin, E.J. Circulation (2006) [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. 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]
  13. Gene mutations in apical hypertrophic cardiomyopathy. Arad, M., Penas-Lado, M., Monserrat, L., Maron, B.J., Sherrid, M., Ho, C.Y., Barr, S., Karim, A., Olson, T.M., Kamisago, M., Seidman, J.G., Seidman, C.E. Circulation (2005) [Pubmed]
  14. The nucleotide sequence of a CpG island demonstrates the presence of the first exon of the gene encoding the human lysosomal membrane protein lamp2 and assigns the gene to Xq24. Manoni, M., Tribioli, C., Lazzari, B., DeBellis, G., Patrosso, C., Pergolizzi, R., Pellegrini, M., Maestrini, E., Rivella, S., Vezzoni, P. Genomics (1991) [Pubmed]
  15. Sorting of lysosomal membrane glycoproteins lamp-1 and lamp-2 into vesicles distinct from mannose 6-phosphate receptor/gamma-adaptin vesicles at the trans-Golgi network. Karlsson, K., Carlsson, S.R. J. Biol. Chem. (1998) [Pubmed]
  16. 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]
  17. 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]
  18. 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]
  19. Retrovirus-mediated gene transfer and galactocerebrosidase uptake into twitcher glial cells results in appropriate localization and phenotype correction. Luddi, A., Volterrani, M., Strazza, M., Smorlesi, A., Rafi, M.A., Datto, J., Wenger, D.A., Costantino-Ceccarini, E. Neurobiol. Dis. (2001) [Pubmed]
  20. The lysosomal granule membrane protein, LAMP-2, is also present in platelet dense granule membranes. Israels, S.J., McMillan, E.M., Robertson, C., Singhory, S., McNicol, A. Thromb. Haemost. (1996) [Pubmed]
  21. BACE is degraded via the lysosomal pathway. Koh, Y.H., von Arnim, C.A., Hyman, B.T., Tanzi, R.E., Tesco, G. J. Biol. Chem. (2005) [Pubmed]
  22. Cathepsin E deficiency induces a novel form of lysosomal storage disorder showing the accumulation of lysosomal membrane sialoglycoproteins and the elevation of lysosomal pH in macrophages. Yanagawa, M., Tsukuba, T., Nishioku, T., Okamoto, Y., Okamoto, K., Takii, R., Terada, Y., Nakayama, K.I., Kadowaki, T., Yamamoto, K. J. Biol. Chem. (2007) [Pubmed]
  23. 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]
  24. LAMP-1 and LAMP-2, but not LAMP-3, are reliable markers for activation-induced secretion of human mast cells. Grützkau, A., Smorodchenko, A., Lippert, U., Kirchhof, L., Artuc, M., Henz, B.M. Cytometry. Part A : the journal of the International Society for Analytical Cytology. (2004) [Pubmed]
  25. 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]
  26. A PEST deletion mutant of ABCA1 shows impaired internalization and defective cholesterol efflux from late endosomes. Chen, W., Wang, N., Tall, A.R. J. Biol. Chem. (2005) [Pubmed]
  27. Familial X-linked cardiomyopathy (Danon disease): diagnostic confirmation by mutation analysis of the LAMP2gene. Balmer, C., Ballhausen, D., Bosshard, N.U., Steinmann, B., Boltshauser, E., Bauersfeld, U., Superti-Furga, A. Eur. J. Pediatr. (2005) [Pubmed]
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