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Open Access Articles- Top Results for LAMP2

LAMP2

Template:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/row
Identifiers
SymbolsLAMP2 ; CD107b; LAMP-2; LAMPB; LGP110
External IDsOMIM309060 MGI96748 HomoloGene7809 GeneCards: LAMP2 Gene
RNA expression pattern
File:PBB GE LAMP2 203041 s at tn.png
File:PBB GE LAMP2 203042 at tn.png
File:PBB GE LAMP2 200821 at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez392016784
EnsemblENSG00000005893ENSMUSG00000016534
UniProtP13473P17047
RefSeq (mRNA)NM_001122606NM_001017959
RefSeq (protein)NP_001116078NP_001017959
Location (UCSC)Chr X:
119.56 – 119.6 Mb
Chr X:
38.4 – 38.46 Mb
PubMed search[1][2]

Lysosome-associated membrane protein 2 (LAMP2) also known as CD107b (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 three variants - LAMP-2A, LAMP-2B and LAMP-2C. [1] LAMP-2A is the receptor for chaperone-mediated autophagy. 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.

LAMP-2B is associated with Danon disease.

See also

References

Further reading

  • 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. PMID 1959930. doi:10.1007/BF00204936. 
  • 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. PMID 2032724. doi:10.1016/0888-7543(91)90424-D. 
  • 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. PMID 2912382. doi:10.1016/0003-9861(89)90597-3. 
  • 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 (2): 667–74. PMC 1136051. 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. PMID 7488019. doi:10.1006/bbrc.1995.2528. 
  • 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. PMID 7999007. doi:10.1006/bbrc.1994.2620. 
  • 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. PMID 8323299. doi:10.1006/abbi.1993.1322. 
  • 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. PMID 8660832. doi:10.1006/cimm.1996.0167. 
  • 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. PMID 8995204. doi:10.1007/s004410050758. 
  • 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. doi:10.1093/oxfordjournals.jbchem.a021526. 
  • 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. PMID 9668075. doi:10.1074/jbc.273.30.18966. 
  • 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. PMC 108621. 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. PMID 10222041. doi:10.1006/abbi.1999.1147. 
  • 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. PMID 10972294. doi:10.1038/35022604. 
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External links

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