Laminin subunit gamma-1

LAMC1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1KLO, 1NPE, 1TLE, 4AQT
Identifiers
Aliases	LAMC1 , LAMB2, Laminin, gamma 1, laminin subunit gamma 1
External IDs	OMIM: 150290 MGI: 99914 HomoloGene: 1724 GeneCards: LAMC1
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1q25.3 Start 183,023,420 bp [1] End 183,145,592 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1 G3|1 65.3 cM Start 153,094,668 bp [2] End 153,208,532 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium visceral pleura parietal pleura Achilles tendon sural nerve saphenous vein placenta gastric mucosa urethra synovial joint Top expressed in ascending aorta aortic valve molar left lung lobe atrium yolk sac uterus temporal muscle sternocleidomastoid muscle triceps brachii muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function extracellular matrix structural constituent extracellular matrix constituent conferring elasticity Cellular component extracellular matrix extracellular region basement membrane laminin-1 complex extracellular exosome laminin-10 complex laminin-11 complex extracellular space endoplasmic reticulum lumen collagen-containing extracellular matrix Biological process hemidesmosome assembly substrate adhesion-dependent cell spreading endoderm development cell adhesion extracellular matrix organization cell migration positive regulation of epithelial cell proliferation extracellular matrix disassembly post-translational protein modification protein-containing complex assembly animal organ morphogenesis tissue development organism system development basement membrane assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3915 226519 Ensembl ENSG00000135862 ENSMUSG00000026478 UniProt P11047 P02468 RefSeq (mRNA) NM_002293 NM_010683 RefSeq (protein) NP_002284 n/a Location (UCSC) Chr 1: 183.02 – 183.15 Mb Chr 1: 153.09 – 153.21 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Laminin subunit gamma-1 is a protein that in humans is encoded by the LAMC1 gene. ^{[5] [6]}

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. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000135862 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026478 - 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. 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.
6. "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. doi: 10.1016/S0021-9258(18)52424-8 . 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. Bibcode:1989Natur.338..229H. doi:10.1038/338229a0. PMID   2922051. S2CID   4313384.
• 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. doi: 10.1016/S0021-9258(18)68707-1 . 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. S2CID   8075171.
• 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. doi:10.1152/ajprenal.1998.275.4.F518. PMID   9755123. S2CID   4380343.
• 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) (5): 869–76. doi:10.1242/jcs.113.5.869. 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. S2CID   10715366.
• 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.