Laminin, beta 1

Laminin subunit beta-1 is a protein that in humans is encoded by the LAMB1 gene.

LAMB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4AQS
Identifiers
Aliases	LAMB1, CLM, LIS5, Laminin, beta 1, laminin subunit beta 1
External IDs	OMIM: 150240; MGI: 96743; HomoloGene: 1722; GeneCards: LAMB1; OMA:LAMB1 - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7q31.1 Start 107,923,799 bp End 108,003,213 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12 A2|12 13.39 cM Start 31,315,233 bp End 31,379,643 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibial nerve right lung epithelium of colon muscle layer of sigmoid colon stromal cell of endometrium upper lobe of left lung parietal pleura sural nerve left uterine tube trigeminal ganglion Top expressed in external carotid artery internal carotid artery primary oocyte tail of embryo iris secondary oocyte left lung lobe Gonadal ridge medullary collecting duct Epithelium of choroid plexus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function extracellular matrix structural constituent structural molecule activity protein binding integrin binding Cellular component laminin-8 complex extracellular matrix laminin-2 complex extracellular region basement membrane laminin-10 complex perinuclear region of cytoplasm laminin-1 complex extracellular exosome extracellular space endoplasmic reticulum lumen collagen-containing extracellular matrix laminin complex Biological process endodermal cell differentiation positive regulation of epithelial cell proliferation positive regulation of cell migration neuronal-glial interaction involved in cerebral cortex radial glia guided migration extracellular matrix organization odontogenesis cell adhesion substrate adhesion-dependent cell spreading neuron projection development post-translational protein modification animal organ morphogenesis tissue development cell migration basement membrane assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3912 16777 Ensembl ENSG00000091136 ENSMUSG00000002900 UniProt P07942 P02469 RefSeq (mRNA) NM_002291 NM_008482 RefSeq (protein) NP_002282 NP_032508 Location (UCSC) Chr 7: 107.92 – 108 Mb Chr 12: 31.32 – 31.38 Mb PubMed search
Wikidata
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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 1. The beta 1 chain has 7 structurally distinct domains, which it shares with other beta chain isomers. The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation. Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor. A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis.

5′-UTR of Laminin-B1 harbors IRES (internal ribosome entry site) between −293 and −1 upstream of the start codon. IRES are involved in cancer malignancy.

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 (1): 81–8. doi:10.2741/1781. PMC 3506377. PMID 16146715.
• Vuolteenaho R, Chow LT, Tryggvason K (1990). "Structure of the human laminin B1 chain gene". J. Biol. Chem. 265 (26): 15611–6. doi:10.1016/S0021-9258(18)55441-7. PMID 1975589.
• Sasaki M, Kato S, Kohno K, et al. (1987). "Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats". Proc. Natl. Acad. Sci. U.S.A. 84 (4): 935–9. Bibcode:1987PNAS...84..935S. doi:10.1073/pnas.84.4.935. PMC 304334. PMID 3493487.
• Pikkarainen T, Eddy R, Fukushima Y, et al. (1987). "Human laminin B1 chain. A multidomain protein with gene (LAMB1) locus in the q22 region of chromosome 7". J. Biol. Chem. 262 (22): 10454–62. doi:10.1016/S0021-9258(18)60982-2. PMID 3611077.
• Jaye M, Modi WS, Ricca GA, et al. (1987). "Isolation of a cDNA clone for the human laminin-B1 chain and its gene localization". Am. J. Hum. Genet. 41 (4): 605–15. PMC 1684322. PMID 3661559.
• 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.
• Lohi J, Leivo I, Franssila K, Virtanen I (1997). "Changes in the distribution of integrins and their basement membrane ligands during development of human thyroid follicular epithelium". Histochem. J. 29 (4): 337–45. doi:10.1023/A:1026482700109. PMID 9184849. S2CID 25517944.
• Taylor J, Muntoni F, Robb S, et al. (1997). "Early onset autosomal dominant myopathy with rigidity of the spine: a possible role for laminin beta 1?". Neuromuscul. Disord. 7 (4): 211–6. doi:10.1016/S0960-8966(97)00461-6. PMID 9196901. S2CID 11981067.
• Sewry CA, D'Alessandro M, Wilson LA, et al. (1997). "Expression of laminin chains in skin in merosin-deficient congenital muscular dystrophy". Neuropediatrics. 28 (4): 217–22. doi:10.1055/s-2007-973703. PMID 9309712. S2CID 260243267.
• Mahida YR, Beltinger J, Makh S, et al. (1998). "Adult human colonic subepithelial myofibroblasts express extracellular matrix proteins and cyclooxygenase-1 and -2". Am. J. Physiol. 273 (6 Pt 1): G1341–8. doi:10.1152/ajpgi.1997.273.6.G1341. PMID 9435560.
• O'Grady P, Thai TC, Saito H (1998). "The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR". J. Cell Biol. 141 (7): 1675–84. doi:10.1083/jcb.141.7.1675. PMC 2133008. PMID 9647658.
• Koch M, Olson PF, Albus A, et al. (1999). "Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain". J. Cell Biol. 145 (3): 605–18. doi:10.1083/jcb.145.3.605. PMC 2185082. PMID 10225960.
• Merlini L, Villanova M, Sabatelli P, et al. (1999). "Decreased expression of laminin beta 1 in chromosome 21-linked Bethlem myopathy". Neuromuscul. Disord. 9 (5): 326–9. doi:10.1016/S0960-8966(99)00022-X. PMID 10407855. S2CID 53256492.
• 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. ( Pt 5) (5): 869–76. doi:10.1242/jcs.113.5.869. PMID 10671376.
• Hirosaki T, Mizushima H, Tsubota Y, et al. (2000). "Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5". J. Biol. Chem. 275 (29): 22495–502. doi:10.1074/jbc.M001326200. PMID 10801807.
• 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.
• Pedraza C, Geberhiwot T, Ingerpuu S, et al. (2000). "Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1)". J. Immunol. 165 (10): 5831–8. doi:10.4049/jimmunol.165.10.5831. PMID 11067943.