Laminin, gamma 1

Laminin, gamma 1 (formerly LAMB2)
PDB rendering based on 1klo.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1klo​, 1npe​, 1tle​
Identifiers
Symbols	LAMC1 ; LAMB2
External IDs	OMIM: 150290 MGI: 99914 HomoloGene: 1724 GeneCards: LAMC1 Gene
Gene ontology Molecular function • extracellular matrix structural constituent • glycosphingolipid binding Cellular component • extracellular region • basement membrane • laminin-1 complex • extracellular space • extracellular matrix • laminin-10 complex • laminin-11 complex • extracellular exosome Biological process • protein complex assembly • cell adhesion • axon guidance • endoderm development • cell migration • extracellular matrix disassembly • extracellular matrix organization • hemidesmosome assembly • substrate adhesion-dependent cell spreading • positive regulation of epithelial cell proliferation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3915	226519
Ensembl	ENSG00000135862	ENSMUSG00000026478
UniProt	P11047	P02468
RefSeq (mRNA)	NM_002293	NM_010683
RefSeq (protein)	NP_002284	NP_034813
Location (UCSC)	Chr 1: 183.02 – 183.15 Mb	Chr 1: 153.22 – 153.33 Mb
PubMed search

Laminin subunit gamma-1 is a protein that in humans is encoded by the LAMC1 gene.^[1][2]

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 gamma chain isoform laminin, gamma 1. The gamma 1 chain, formerly thought to be a beta chain, contains structural domains similar to beta chains, however, lacks the short alpha region separating domains I and II. The structural organization of this gene also suggested that it had diverged considerably from the beta chain genes. Embryos of transgenic mice in which both alleles of the gamma 1 chain gene were inactivated by homologous recombination, lacked basement membranes, indicating that laminin, gamma 1 chain is necessary for laminin heterotrimer assembly. It has been inferred by analogy with the strikingly similar 3' UTR sequence in mouse laminin gamma 1 cDNA, that multiple polyadenylation sites are utilized in human to generate the 2 different sized mRNAs (5.5 and 7.5 kb) seen on Northern analysis.^[2]

References

1. Fukushima Y, Pikkarainen T, Kallunki T, Eddy RL, Byers MG, Haley LL, Henry WM, Tryggvason K, Shows TB (May 1989). "Isolation of a human laminin B2 (LAMB2) cDNA clone and assignment of the gene to chromosome region 1q25----q31". Cytogenet Cell Genet 48 (3): 137–41. doi:10.1159/000132610. PMID 3234037.
2. "Entrez Gene: LAMC1 laminin, gamma 1 (formerly LAMB2)".

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.
• Santos CL, Sabbaga J, Brentani R (1992). "Differences in human laminin B2 sequences.". DNA Seq. 1 (4): 275–7. doi:10.3109/10425179109020782. PMID 1806043.
• Kallunki T, Ikonen J, Chow LT, et al. (1991). "Structure of the human laminin B2 chain gene reveals extensive divergence from the laminin B1 chain gene.". J. Biol. Chem. 266 (1): 221–8. PMID 1985895.
• Hunter DD, Shah V, Merlie JP, Sanes JR (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.
• Pikkarainen T, Kallunki T, Tryggvason K (1988). "Human laminin B2 chain. Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains.". J. Biol. Chem. 263 (14): 6751–8. PMID 3360804.
• Mattei MG, Weil D, Pribula-Conway D, et al. (1988). "cDNA cloning, expression and mapping of human laminin B2 gene to chromosome 1q31.". Hum. Genet. 79 (3): 235–41. doi:10.1007/BF00366243. PMID 3402995.
• Davis JM, Narachi MA, Alton NK, Arakawa T (1987). "Structure of human tumor necrosis factor alpha derived from recombinant DNA.". Biochemistry 26 (5): 1322–6. doi:10.1021/bi00379a018. PMID 3552045.
• 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.
• 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.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• 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.
• Kohfeldt E, Sasaki T, Göhring W, Timpl R (1998). "Nidogen-2: a new basement membrane protein with diverse binding properties.". J. Mol. Biol. 282 (1): 99–109. doi:10.1006/jmbi.1998.2004. PMID 9733643.
• Suzuki H, Denisenko ON, Suzuki Y, et al. (1998). "Inducible transcriptional activity of bcn-1 element from laminin gamma1-chain gene promoter in renal and nonrenal cells.". Am. J. Physiol. 275 (4 Pt 2): F518–26. PMID 9755123.
• Smyth N, Vatansever HS, Murray P, et al. (1999). "Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation.". J. Cell Biol. 144 (1): 151–60. doi:10.1083/jcb.144.1.151. PMC 2148127. PMID 9885251.
• 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.
• 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.
• Parsons SF, Lee G, Spring FA, et al. (2001). "Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity.". Blood 97 (1): 312–20. doi:10.1182/blood.V97.1.312. PMID 11133776.
• 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.