Laminin, beta 2

Laminin subunit beta-2 is a protein that in humans is encoded by the LAMB2 gene.^[5][6][7]

LAMB2
Identifiers
Aliases	LAMB2, LAMS, NPHS5, Laminin, beta 2, laminin subunit beta 2, PIERS
External IDs	OMIM: 150325; MGI: 99916; HomoloGene: 1723; GeneCards: LAMB2; OMA:LAMB2 - orthologs
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3p21.31 Start 49,121,114 bp[1] End 49,133,118 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9 F2|9 59.4 cM Start 108,356,935 bp[2] End 108,367,729 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart right lobe of thyroid gland stromal cell of endometrium right ovary left ovary right adrenal cortex left lobe of thyroid gland ascending aorta Descending thoracic aorta canal of the cervix Top expressed in gastrula decidua external carotid artery muscle of thigh tunica media of zone of aorta internal carotid artery ascending aorta ankle joint myocardium of ventricle lip More reference expression data BioGPS More reference expression data
Gene ontology Molecular function structural molecule activity integrin binding extracellular matrix structural constituent Cellular component extracellular matrix synapse extracellular region basement membrane laminin-3 complex laminin-11 complex extracellular exosome laminin complex extracellular space synaptic cleft endoplasmic reticulum lumen neuromuscular junction collagen-containing extracellular matrix Biological process metanephric glomerular visceral epithelial cell development astrocyte development Schwann cell development synapse organization axon extension involved in regeneration extracellular matrix organization axon guidance cell adhesion neuromuscular junction development retina development in camera-type eye metanephric glomerular basement membrane development cell morphogenesis involved in differentiation neuron projection development visual perception post-translational protein modification animal organ morphogenesis tissue development cell migration substrate adhesion-dependent cell spreading basement membrane assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3913 16779 Ensembl ENSG00000172037 ENSMUSG00000052911 UniProt P55268 Q61292 RefSeq (mRNA) NM_002292 NM_008483 RefSeq (protein) NP_002283 NP_032509 Location (UCSC) Chr 3: 49.12 – 49.13 Mb Chr 9: 108.36 – 108.37 Mb PubMed search [3] [4]
Wikidata
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Function

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 were formerly designated by Arabic numerals in the order of their discovery, e.g. alpha1beta1gamma1 heterotrimer was known as laminin 1, but the nomenclature now calls for using the numbers of each individual laminin subunit isoform, e.g. what was formerly Laminin 1 is now Laminin 111, and what was formerly Laminin 5 is now Laminin 332.^[8] 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^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000172037 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000052911 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Hunter DD, Shah V, Merlie JP, Sanes JR (Mar 1989). "A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction". Nature. 338 (6212): 229–34. Bibcode:1989Natur.338..229H. doi:10.1038/338229a0. PMID 2922051. S2CID 4313384.
6. Durkin ME, Jäger 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)". Cytogenetics and Cell Genetics. 84 (3–4): 173–8. doi:10.1159/000015249. PMID 10393422. S2CID 36315977.
7. "Entrez Gene: LAMB2 laminin, beta 2 (laminin S)".
8. Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, Engel J, Engvall E, Hohenester E, Jones JC, Kleinman HK, Marinkovich MP, Martin GR, Mayer U, Meneguzzi G, Miner JH, Miyazaki K, Patarroyo M, Paulsson M, Quaranta V, Sanes JR, Sasaki T, Sekiguchi K, Sorokin LM, Talts JF, Tryggvason K, Uitto J, Virtanen I, von der Mark K, Wewer UM, Yamada Y, Yurchenco PD (Aug 2005). "A simplified laminin nomenclature". Matrix Biology. 24 (5): 326–32. doi:10.1016/j.matbio.2005.05.006. PMID 15979864.

Further reading

• Ljubimova JY, Fujita M, Khazenzon NM, Ljubimov AV, Black KL (2006). "Changes in laminin isoforms associated with brain tumor invasion and angiogenesis". Frontiers in Bioscience. 11: 81–8. doi:10.2741/1781. PMC 3506377. PMID 16146715.
• Wewer UM, Gerecke DR, Durkin ME, Kurtz KS, Mattei MG, Champliaud MF, Burgeson RE, Albrechtsen R (Nov 1994). "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, Eddy R, Shows TB, Sariola H, Tryggvason K (Feb 1995). "The human laminin beta 2 chain (S-laminin): structure, expression in fetal tissues and chromosomal assignment of the LAMB2 gene". Matrix Biology. 14 (6): 489–97. doi:10.1016/0945-053X(95)90006-3. PMID 7795887.
• Burgeson RE, Chiquet M, Deutzmann R, Ekblom P, Engel J, Kleinman H, Martin GR, Meneguzzi G, Paulsson M, Sanes J (Apr 1994). "A new nomenclature for the laminins". Matrix Biology. 14 (3): 209–11. doi:10.1016/0945-053X(94)90184-8. PMID 7921537.
• Wewer UM, Wayner EA, Hoffstrom BG, Lan F, Meyer-Nielsen B, Engvall E, Albrechtsen R (Nov 1994). "Selective assembly of laminin variants by human carcinoma cells". Laboratory Investigation. 71 (5): 719–30. PMID 7967523.
• Durkin ME, Gautam M, Loechel F, Sanes JR, Merlie JP, Albrechtsen R, Wewer UM (Jun 1996). "Structural organization of the human and mouse laminin beta2 chain genes, and alternative splicing at the 5' end of the human transcript". The Journal of Biological Chemistry. 271 (23): 13407–16. doi:10.1074/jbc.271.23.13407. PMID 8662701.
• Vogel W, Kanz L, Brugger W, Berndt A, Kosmehl H (Aug 1999). "Expression of laminin beta2 chain in normal human bone marrow". Blood. 94 (3): 1143–5. PMID 10454804.
• Kikkawa Y, Sanzen N, Fujiwara H, Sonnenberg A, Sekiguchi K (Mar 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". Journal of Cell Science. 113 (5): 869–76. doi:10.1242/jcs.113.5.869. PMID 10671376.
• Champliaud MF, Virtanen I, Tiger CF, Korhonen M, Burgeson R, Gullberg D (Sep 2000). "Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta". Experimental Cell Research. 259 (2): 326–35. doi:10.1006/excr.2000.4980. PMID 10964500.
• McArthur CP, Wang Y, Heruth D, Gustafson S (Jun 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". Archives of Oral Biology. 46 (6): 545–55. doi:10.1016/S0003-9969(01)00014-0. PMID 11311202.
• Gu J, Fujibayashi A, Yamada KM, Sekiguchi K (May 2002). "Laminin-10/11 and fibronectin differentially prevent apoptosis induced by serum removal via phosphatidylinositol 3-kinase/Akt- and MEK1/ERK-dependent pathways". The Journal of Biological Chemistry. 277 (22): 19922–8. doi:10.1074/jbc.M200383200. PMID 11891225.
• Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (Jun 2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nature Biotechnology. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
• Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (Sep 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• Zenker M, Aigner T, Wendler O, Tralau T, Müntefering H, Fenski R, Pitz S, Schumacher V, Royer-Pokora B, Wühl E, Cochat P, Bouvier R, Kraus C, Mark K, Madlon H, Dötsch J, Rascher W, Maruniak-Chudek I, Lennert T, Neumann LM, Reis A (Nov 2004). "Human laminin beta2 deficiency causes congenital nephrosis with mesangial sclerosis and distinct eye abnormalities". Human Molecular Genetics. 13 (21): 2625–32. doi:10.1093/hmg/ddh284. PMID 15367484.
• Fukuda Y, Yotsuyanagi H, Ooka S, Sekine T, Koike J, Takano T, Suzuki M, Itoh F, Nishioka K, Kato T (Dec 2004). "Identification of a new autoantibody in patients with chronic hepatitis". Human Immunology. 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]". Przegla̧d Lekarski. 63 (Suppl 3): 37–9. PMID 16898484.