Laminin, beta 1

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Laminin, beta 1

Identifiers

LAMB1; CLM; MGC142015

External IDs

OMIM: 150240 MGI: 96743 HomoloGene: 1722

Gene ontology
Molecular Function:	• extracellular matrix structural constituent • enzyme binding
Cellular Component:	• basement membrane • laminin-1 complex • laminin-2 complex • laminin-8 complex • laminin-10 complex • perinuclear region of cytoplasm
Biological Process:	• cell adhesion • embryo implantation • positive regulation of cell migration • neurite development • odontogenesis • positive regulation of epithelial cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002291 (mRNA)
NP_002282 (protein)

NM_008482 (mRNA)
NP_032508 (protein)

Location

Chr 7: 107.35 - 107.43 Mb

Chr 12: 31.85 - 31.92 Mb

Pubmed search

[1]

[2]

Laminin, beta 1, also known as LAMB1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: LAMB1 laminin, beta 1.

[edit] 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. PMID 16146715.
Bonneau D, Huret JL, Godeau G, et al. (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. PMID 1864606.
Vuolteenaho R, Chow LT, Tryggvason K (1990). "Structure of the human laminin B1 chain gene.". J. Biol. Chem. 265 (26): 15611–6. PMID 1975589.
Ikonen J, Pikkarainen T, Savolainen ER, Tryggvason K (1989). "A Hpa I polymorphism in the human laminin B1 chain gene on 7q22.". Nucleic Acids Res. 17 (1): 473. PMID 2563160.
Roche KB, Moore JW, Surana RB, Wilson BE (1989). "Aortic root dilatation associated with partial trisomy 7(q31.2----qter).". Pediatric cardiology 10 (1): 53–5. PMID 2704655.
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. 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. 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. PMID 3661559.
Burgeson RE, Chiquet M, Deutzmann R, et al. (1994). "A new nomenclature for the laminins.". Matrix Biol. 14 (3): 209–11. 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. PMID 9184849.
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. PMID 9196901.
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. PMID 9309712.
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. 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. 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. 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. PMID 10407855.
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): 869–76. 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. PMID 11067943.