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http://en.wikipedia.org/wiki/LAMP2 This page was last modified on 1 April 2009 at 22:24.

LAMP2

From Wikipedia, the free encyclopedia

Lysosomal-associated membrane protein 2 (LAMP2) also known asCD107b (Cluster of Differentiation 107b), is a human gene.

The protein encoded by this gene is a member of a family of membrane glycoproteins. This glycoprotein provides selectins with carbohydrate ligands. It may play a role in tumor cell metastasis. It may also function in the protection, maintenance, and adhesion of the lysosome. Alternative splicing of the gene produces two known products of unknown function. ^[1] Recently it has been determined that antibodies against LAMP-2 account for a fraction of patients who get a serious kidney disease termed focal necrotizing glomerulonephritis.

Identifiers

Lysosomal-associated membrane protein 2

External IDs

Symbols

OMIM: 309060 MGI: 96748 HomoloGene: 7809 GeneCards: LAMP2 Gene

LAMP2; CD107b; LAMP-2C; LAMPB; LGP96

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Gene ontology

RNA expression pattern

References

1. ^ "Entrez Gene: LAMP2 lysosomal-associated membrane protein 2".

Chang MH, Karageorgos LE, Meikle PJ (2003). "CD107a (LAMP-1) and CD107b (LAMP-2).". J. Biol. Regul. Homeost. Agents 16 (2): 147–51. PMID 12144129.
Schleutker J, Haataja L, Renlund M, et al. (1992). "Confirmation of the chromosomal localization of human lamp genes and their exclusion as candidate genes for Salla disease.". Hum. Genet. 88(1): 95–7.doi:10.1007/BF00204936. PMID 1959930.
Manoni M, Tribioli C, Lazzari B, et al. (1991). "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.". Genomics 9 (3): 551–4. doi:10.1016/0888-7543(91)90424-D. PMID 2032724.
Carlsson SR, Fukuda M (1990). "The polylactosaminoglycans of human lysosomal membrane glycoproteins lamp-1 and lamp-2. Localization on the peptide backbones.". J. Biol. Chem. 265(33): 20488–95. PMID 2243102.
Mattei MG, Matterson J, Chen JW,et al. (1990). "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.". J. Biol. Chem. 265(13): 7548–51. PMID 2332441.
Mane SM, Marzella L, Bainton DF,et al. (1989). "Purification and characterization of human lysosomal membrane glycoproteins.". Arch. Biochem. Biophys. 268 (1): 360–78.doi:10.1016/0003-9861(89)90597-3. PMID 2912382.
Fukuda M, Viitala J, Matteson J, Carlsson SR (1989). "Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid sequences.".J. Biol. Chem. 263 (35): 18920–8.PMID 3198605.
Dahlgren C, Carlsson SR, Karlsson A, et al. (1995). "The lysosomal membrane glycoproteins Lamp-1 and Lamp-2 are present in mobilizable organelles, but are absent from the azurophil granules of human neutrophils.". Biochem. J. 311 ( Pt 2): 667–74. PMID 7487911.
Konecki DS, Foetisch K, Zimmer KP, et al. (1995). "An alternatively spliced form of the human lysosome-associated membrane protein-2 gene is expressed in a tissue-specific manner.".Biochem. Biophys. Res. Commun. 215 (2): 757–67.doi:10.1006/bbrc.1995.2528.PMID 7488019.
Konecki DS, Foetisch K, Schlotter M, Lichter-Konecki U (1995). "Complete cDNA sequence of human lysosome-associated membrane protein-2.". Biochem. Biophys. Res. Commun. 205 (1): 1–5.doi:10.1006/bbrc.1994.2620.PMID 7999007.
Carlsson SR, Lycksell PO, Fukuda M (1993). "Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.". Arch. Biochem. Biophys. 304(1): 65–73.doi:10.1006/abbi.1993.1322.PMID 8323299.
Sawada R, Jardine KA, Fukuda M (1993). "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.". J. Biol. Chem. 268 (12): 9014–22.PMID 8517882.
Kannan K, Stewart RM, Bounds W, et al. (1996). "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.". Cell. Immunol. 171(1): 10–9.doi:10.1006/cimm.1996.0167.PMID 8660832.
Israels SJ, McMillan EM, Robertson C, et al. (1996). "The lysosomal granule membrane protein, LAMP-2, is also present in platelet dense granule membranes.". Thromb. Haemost.75 (4): 623–9. PMID 8743190.
Aumüller G, Renneberg H, Hasilik A (1997). "Distribution and subcellular localization of a lysosome-associated protein in human genital organs.". Cell Tissue Res. 287 (2): 335–42.doi:10.1007/s004410050758.PMID 8995204.
Akasaki K, Michihara A, Fujiwara Y, et al. (1997). "Biosynthetic transport of a major lysosome-associated membrane glycoprotein 2, lamp-2: a significant fraction of newly synthesized lamp-2 is delivered to lysosomes by way of early endosomes.". J. Biochem. 120(6): 1088–94. PMID 9010755.
Karlsson K, Carlsson SR (1998). "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.". J. Biol. Chem. 273 (30): 18966–73.doi:10.1074/jbc.273.30.18966.PMID 9668075.
Ayala P, Lin L, Hopper S, et al.(1998). "Infection of epithelial cells by pathogenic neisseriae reduces the levels of multiple lysosomal constituents.". Infect. Immun. 66 (10): 5001–7. PMID 9746610.
Furuta K, Yang XL, Chen JS, et al. (1999). "Differential expression of the lysosome-associated membrane proteins in normal human tissues.". Arch. Biochem. Biophys. 365 (1): 75–82.doi:10.1006/abbi.1999.1147.PMID 10222041.
Nishino I, Fu J, Tanji K, et al.(2000). "Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease).".Nature 406 (6798): 906–10.doi:10.1038/35022604. PMID 10972294.