Laminin, beta 1

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
Gene location (Human) Chr. Chromosome 7 (human) [1] Band 7q31.1 Start 107,923,799 bp [1] End 108,003,213 bp [1]
Gene location (Mouse) Chr. Chromosome 12 (mouse) [2] Band 12 A2|12 13.39 cM Start 31,315,233 bp [2] End 31,379,643 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibial nerve right lung stromal cell of endometrium upper lobe of left lung parietal pleura sural nerve left uterine tube trigeminal ganglion gastric mucosa pericardium Top expressed in external carotid artery internal carotid artery iris secondary oocyte left lung lobe medullary collecting duct vas deferens sciatic nerve ciliary body primitive streak 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 [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Laminin subunit beta-1 is a protein that in humans is encoded by the LAMB1 gene. ^{[5] [6] [7] [8]}

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. ^[8]

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. ^[9]

References

1. GRCh38: Ensembl release 89: ENSG00000091136 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000002900 - 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. Ikonen J, Pikkarainen T, Savolainen ER, Tryggvason K (Feb 1989). "A Hpa I polymorphism in the human laminin B1 chain gene on 7q22". Nucleic Acids Res. 17 (1): 473. doi:10.1093/nar/17.1.473. PMC   331592 . PMID   2563160.
6. Roche KB, Moore JW, Surana RB, Wilson BE (May 1989). "Aortic root dilatation associated with partial trisomy 7(q31.2----qter)". Pediatr Cardiol. 10 (1): 53–5. doi:10.1007/BF02328637. PMID   2704655. S2CID   22352528.
7. Bonneau D, Huret JL, Godeau G, Couet D, Putterman M, Tanzer J, Babin P, Larregue M (Sep 1991). "Recurrent ctb(7)(q31.3) and possible laminin involvement in a neonatal cutis laxa with a Marfan phenotype". Hum Genet. 87 (3): 317–9. doi:10.1007/bf00200911. PMID   1864606. S2CID   32445071.
8. "Entrez Gene: LAMB1 laminin, beta 1".
9. Petz M, Them N, Huber H, Beug H, Mikulits W (January 2012). "La enhances IRES-mediated translation of laminin B1 during malignant epithelial to mesenchymal transition". Nucleic Acids Research. 40 (1): 290–302. doi: 10.1093/nar/gkr717 . PMC   3245933 . PMID   21896617.

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.