Laminin, beta 2

From Wikipedia, the free encyclopedia
Laminin, beta 2 (laminin S)
Identifiers
SymbolsLAMB2; LAMS; NPHS5
External IDsOMIM: 150325 MGI: 99916 HomoloGene: 1723 GeneCards: LAMB2 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez391316779
EnsemblENSG00000172037ENSMUSG00000052911
UniProtP55268Q61292
RefSeq (mRNA)NM_002292NM_008483
RefSeq (protein)NP_002283NP_032509
Location (UCSC)Chr 3:
49.16 – 49.17 Mb		Chr 9:
108.48 – 108.49 Mb
PubMed search
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Laminin subunit beta-2 is a protein that in humans is encoded by the LAMB2 gene.[1][2][3]

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms, which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform laminin, beta 2. The beta 2 chain contains the 7 structural domains typical of beta chains of laminin, including the short alpha region. However, unlike beta 1 chain, beta 2 has a more restricted tissue distribution. It is enriched in the basement membrane of muscles at the neuromuscular junctions, kidney glomerulus and vascular smooth muscle. Transgenic mice in which the beta 2 chain gene was inactivated by homologous recombination, showed defects in the maturation of neuromuscular junctions and impairment of glomerular filtration. Alternative splicing involving a non consensus 5' splice site (gc) in the 5' UTR of this gene has been reported. It was suggested that inefficient splicing of this first intron, which does not change the protein sequence, results in a greater abundance of the un[3]

References

  1. ↑ Hunter DD, Shah V, Merlie JP, Sanes JR (Apr 1989). "A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction". Nature 338 (6212): 229–34. doi:10.1038/338229a0. PMID 2922051. 
  2. ↑ Durkin ME, Jager AC, Khurana TS, Nielsen FC, Albrechtsen R, Wewer UM (Jul 1999). "Characterization of the human laminin beta2 chain locus (LAMB2): linkage to a gene containing a nonprocessed, transcribed LAMB2-like pseudogene (LAMB2L) and to the gene encoding glutaminyl tRNA synthetase (QARS)". Cytogenet Cell Genet 84 (3–4): 173–8. doi:10.1159/000015249. PMID 10393422. 
  3. ↑ 3.0 3.1 "Entrez Gene: LAMB2 laminin, beta 2 (laminin S)". 

Further reading

  • Ljubimova JY, Fujita M, Khazenzon NM et al. (2006). "Changes in laminin isoforms associated with brain tumor invasion and angiogenesis". Front. Biosci. 11: 81–8. doi:10.2741/1781. PMID 16146715. 
  • Wewer UM, Gerecke DR, Durkin ME et al. (1995). "Human beta 2 chain of laminin (formerly S chain): cDNA cloning, chromosomal localization, and expression in carcinomas". Genomics 24 (2): 243–52. doi:10.1006/geno.1994.1612. PMID 7698745. 
  • Iivanainen A, Vuolteenaho R, Sainio K et al. (1995). "The human laminin beta 2 chain (S-laminin): structure, expression in fetal tissues and chromosomal assignment of the LAMB2 gene". Matrix Biol. 14 (6): 489–97. doi:10.1016/0945-053X(95)90006-3. PMID 7795887. 
  • Burgeson RE, Chiquet M, Deutzmann R et al. (1994). "A new nomenclature for the laminins". Matrix Biol. 14 (3): 209–11. doi:10.1016/0945-053X(94)90184-8. PMID 7921537. 
  • Wewer UM, Wayner EA, Hoffstrom BG et al. (1994). "Selective assembly of laminin variants by human carcinoma cells". Lab. Invest. 71 (5): 719–30. PMID 7967523. 
  • Durkin ME, Gautam M, Loechel F et al. (1996). "Structural organization of the human and mouse laminin beta2 chain genes, and alternative splicing at the 5' end of the human transcript". J. Biol. Chem. 271 (23): 13407–16. doi:10.1074/jbc.271.23.13407. PMID 8662701. 
  • Vogel W, Kanz L, Brugger W et al. (1999). "Expression of laminin beta2 chain in normal human bone marrow". Blood 94 (3): 1143–5. PMID 10454804. 
  • Kikkawa Y, Sanzen N, Fujiwara H et al. (2000). "Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins". J. Cell. Sci. 113 (5): 869–76. PMID 10671376. 
  • Champliaud MF, Virtanen I, Tiger CF et al. (2000). "Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta". Exp. Cell Res. 259 (2): 326–35. doi:10.1006/excr.2000.4980. PMID 10964500. 
  • McArthur CP, Wang Y, Heruth D, Gustafson S (2001). "Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53". Arch. Oral Biol. 46 (6): 545–55. doi:10.1016/S0003-9969(01)00014-0. PMID 11311202. 
  • Gu J, Fujibayashi A, Yamada KM, Sekiguchi K (2002). "Laminin-10/11 and fibronectin differentially prevent apoptosis induced by serum removal via phosphatidylinositol 3-kinase/Akt- and MEK1/ERK-dependent pathways". J. Biol. Chem. 277 (22): 19922–8. doi:10.1074/jbc.M200383200. PMID 11891225. 
  • Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
  • Brandenberger R, Wei H, Zhang S et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. 
  • Suzuki Y, Yamashita R, Shirota M et al. (2004). "Sequence Comparison of Human and Mouse Genes Reveals a Homologous Block Structure in the Promoter Regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556. 
  • Zenker M, Aigner T, Wendler O et al. (2005). "Human laminin beta2 deficiency causes congenital nephrosis with mesangial sclerosis and distinct eye abnormalities". Hum. Mol. Genet. 13 (21): 2625–32. doi:10.1093/hmg/ddh284. PMID 15367484. 
  • Fukuda Y, Yotsuyanagi H, Ooka S et al. (2005). "Identification of a new autoantibody in patients with chronic hepatitis". Hum. Immunol. 65 (12): 1530–8. doi:10.1016/j.humimm.2004.08.186. PMID 15603881. 
  • Zurowska A, Załuska-Leśniewska I, Zenker M (2006). "[LAMB2 gene mutation as a cause of congenital nephrotic syndrome with distinct eye abnormalities and hypotonia]". Prz. Lek. 63 Suppl 3: 37–9. PMID 16898484. 
Extracellular matrix
Collagen
Fibril forming
Other
Enzymes
Laminin
Other
Other
See also
diseases B proteins: BY STRUCTURE: membrane, globular (en, ca, an), fibrous
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