Laminin, an extracellular matrix protein, is a major component of the basement membrane. It is thought to mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. It is composed of three subunits, alpha, beta, and gamma, which are bound to each other by disulfide bonds into a cross-shaped molecule. This gene encodes the alpha 2 chain, which constitutes one of the subunits of laminin 2 (merosin) and laminin 4 (s-merosin). Mutations in this gene have been identified as the cause of congenital merosin-deficient muscular dystrophy. Two transcript variants encoding different proteins have been found for this gene.[7]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000196569 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000019899 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Ehrig K, Leivo I, Argraves WS, Ruoslahti E, Engvall E (Jun 1990). "Merosin, a tissue-specific basement membrane protein, is a laminin-like protein". Proc Natl Acad Sci U S A. 87 (9): 3264–8. Bibcode:1990PNAS...87.3264E. doi:10.1073/pnas.87.9.3264. PMC53880. PMID 2185464.
^Vuolteenaho R, Nissinen M, Sainio K, Byers M, Eddy R, Hirvonen H, Shows TB, Sariola H, Engvall E, Tryggvason K (Feb 1994). "Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues". J Cell Biol. 124 (3): 381–94. doi:10.1083/jcb.124.3.381. PMC2119934. PMID 8294519.
Timpl R (1997). "Macromolecular organization of basement membranes". Curr. Opin. Cell Biol. 8 (5): 618–24. doi:10.1016/S0955-0674(96)80102-5. PMID 8939648.
Belkin AM, Stepp MA (2000). "Integrins as receptors for laminins". Microsc. Res. Tech. 51 (3): 280–301. doi:10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O. PMID 11054877. S2CID 45941383.
Jones KJ, Morgan G, Johnston H, et al. (2002). "The expanding phenotype of laminin α2 chain (merosin) abnormalities: case series and review". J. Med. Genet. 38 (10): 649–57. doi:10.1136/jmg.38.10.649. PMC1734735. PMID 11584042.
Helbling-Leclerc A, Zhang X, Topaloglu H, et al. (1995). "Mutations in the laminin alpha 2-chain gene (LAMA2) cause merosin-deficient congenital muscular dystrophy". Nat. Genet. 11 (2): 216–8. doi:10.1038/ng1095-216. PMID 7550355. S2CID 34969060.
Yamada H, Shimizu T, Tanaka T, et al. (1994). "Dystroglycan is a binding protein of laminin and merosin in peripheral nerve". FEBS Lett. 352 (1): 49–53. doi:10.1016/0014-5793(94)00917-1. PMID 7925941. S2CID 17529055.
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.
Zhang X, Vuolteenaho R, Tryggvason K (1996). "Structure of the human laminin alpha2-chain gene (LAMA2), which is affected in congenital muscular dystrophy". J. Biol. Chem. 271 (44): 27664–9. doi:10.1074/jbc.271.44.27664. PMID 8910357.
Squarzoni S, Villanova M, Sabatelli P, et al. (1997). "Intracellular detection of laminin alpha 2 chain in skin by electron microscopy immunocytochemistry: comparison between normal and laminin alpha 2 chain deficient subjects". Neuromuscul. Disord. 7 (2): 91–8. doi:10.1016/S0960-8966(96)00420-8. PMID 9131649. S2CID 140209385.
Allamand V, Sunada Y, Salih MA, et al. (1997). "Mild congenital muscular dystrophy in two patients with an internally deleted laminin alpha2-chain". Hum. Mol. Genet. 6 (5): 747–52. doi:10.1093/hmg/6.5.747. PMID 9158149.
Durkin ME, Loechel F, Mattei MG, et al. (1997). "Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation". FEBS Lett. 411 (2–3): 296–300. doi:10.1016/S0014-5793(97)00686-8. PMID 9271224. S2CID 45286880.
Mrowiec T, Melchar C, Górski A (1998). "HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium". Arch. Immunol. Ther. Exp. (Warsz.). 45 (2–3): 255–9. PMID 9597096.
Koch M, Olson PF, Albus A, et al. (1999). "Characterization and Expression of the Laminin γ3 Chain: A Novel, Non-Basement Membrane–associated, Laminin Chain". J. Cell Biol. 145 (3): 605–18. doi:10.1083/jcb.145.3.605. PMC2185082. PMID 10225960.
Kuang W, Xu H, Vilquin JT, Engvall E (2000). "Activation of the lama2 gene in muscle regeneration: abortive regeneration in laminin alpha2-deficiency". Lab. Invest. 79 (12): 1601–13. PMID 10616210.
Pegoraro E, Fanin M, Trevisan CP, et al. (2000). "A novel laminin alpha2 isoform in severe laminin alpha2 deficient congenital muscular dystrophy". Neurology. 55 (8): 1128–34. doi:10.1212/wnl.55.8.1128. PMID 11071490. S2CID 80274277.
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.
External linksedit
GeneReviews/NCBI/NIH/UW entry on Congenital Muscular Dystrophy Overview
laminin, subunit, alpha, protein, that, humans, encoded, lama2, gene, lama2available, structurespdbortholog, search, pdbe, rcsblist, codes4yep, 4yeqidentifiersaliaseslama2, lamm, laminin, alpha, laminin, subunit, alpha, mdc1aexternal, idsomim, 156225, 99912, h. Laminin subunit alpha 2 is a protein that in humans is encoded by the LAMA2 gene 5 6 7 LAMA2Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes4YEP 4YEQIdentifiersAliasesLAMA2 LAMM Laminin alpha 2 laminin subunit alpha 2 MDC1AExternal IDsOMIM 156225 MGI 99912 HomoloGene 37306 GeneCards LAMA2Gene location Human Chr Chromosome 6 human 1 Band6q22 33Start128 883 138 bp 1 End129 516 566 bp 1 Gene location Mouse Chr Chromosome 10 mouse 2 Band10 A4 10 14 23 cMStart26 856 032 bp 2 End27 495 754 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed ingastric mucosaAchilles tendonright lungatriumpericardiumplacentaleft uterine tuberight ventricletibial nerveleft coronary arteryTop expressed insciatic nerveutricleascending aortavas deferensaortic valveright ventricleplantaris musclesecondary oocyteankleinterventricular septumMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionstructural molecule activity signaling receptor binding extracellular matrix structural constituentCellular componentextracellular region dendritic spine sarcolemma basement membrane extracellular matrix neuromuscular junction synaptic cleft collagen containing extracellular matrixBiological processmuscle organ development regulation of cell migration positive regulation of synaptic transmission cholinergic regulation of embryonic development regulation of cell adhesion axon guidance cell adhesion Schwann cell differentiation extracellular matrix organization animal organ morphogenesis tissue developmentSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez390816773EnsemblENSG00000196569ENSMUSG00000019899UniProtP24043Q60675RefSeq mRNA NM 000426NM 001079823NM 008481RefSeq protein NP 000417NP 001073291NP 032507Location UCSC Chr 6 128 88 129 52 MbChr 10 26 86 27 5 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 References 3 Further reading 4 External linksFunction editLaminin an extracellular matrix protein is a major component of the basement membrane It is thought to mediate the attachment migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components It is composed of three subunits alpha beta and gamma which are bound to each other by disulfide bonds into a cross shaped molecule This gene encodes the alpha 2 chain which constitutes one of the subunits of laminin 2 merosin and laminin 4 s merosin Mutations in this gene have been identified as the cause of congenital merosin deficient muscular dystrophy Two transcript variants encoding different proteins have been found for this gene 7 References edit a b c GRCh38 Ensembl release 89 ENSG00000196569 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000019899 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Ehrig K Leivo I Argraves WS Ruoslahti E Engvall E Jun 1990 Merosin a tissue specific basement membrane protein is a laminin like protein Proc Natl Acad Sci U S A 87 9 3264 8 Bibcode 1990PNAS 87 3264E doi 10 1073 pnas 87 9 3264 PMC 53880 PMID 2185464 Vuolteenaho R Nissinen M Sainio K Byers M Eddy R Hirvonen H Shows TB Sariola H Engvall E Tryggvason K Feb 1994 Human laminin M chain merosin complete primary structure chromosomal assignment and expression of the M and A chain in human fetal tissues J Cell Biol 124 3 381 94 doi 10 1083 jcb 124 3 381 PMC 2119934 PMID 8294519 a b Entrez Gene LAMA2 laminin alpha 2 merosin congenital muscular dystrophy Further reading editTimpl R 1997 Macromolecular organization of basement membranes Curr Opin Cell Biol 8 5 618 24 doi 10 1016 S0955 0674 96 80102 5 PMID 8939648 Belkin AM Stepp MA 2000 Integrins as receptors for laminins Microsc Res Tech 51 3 280 301 doi 10 1002 1097 0029 20001101 51 3 lt 280 AID JEMT7 gt 3 0 CO 2 O PMID 11054877 S2CID 45941383 Jones KJ Morgan G Johnston H et al 2002 The expanding phenotype of laminin a2 chain merosin abnormalities case series and review J Med Genet 38 10 649 57 doi 10 1136 jmg 38 10 649 PMC 1734735 PMID 11584042 Hori H Kanamori T Mizuta T et al 1995 Human laminin M chain epitope analysis of its monoclonal antibodies by immunoscreening of cDNA clones and tissue expression J Biochem 116 6 1212 9 doi 10 1093 oxfordjournals jbchem a124666 PMID 7535762 Helbling Leclerc A Zhang X Topaloglu H et al 1995 Mutations in the laminin alpha 2 chain gene LAMA2 cause merosin deficient congenital muscular dystrophy Nat Genet 11 2 216 8 doi 10 1038 ng1095 216 PMID 7550355 S2CID 34969060 Yamada H Shimizu T Tanaka T et al 1994 Dystroglycan is a binding protein of laminin and merosin in peripheral nerve FEBS Lett 352 1 49 53 doi 10 1016 0014 5793 94 00917 1 PMID 7925941 S2CID 17529055 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 Zhang X Vuolteenaho R Tryggvason K 1996 Structure of the human laminin alpha2 chain gene LAMA2 which is affected in congenital muscular dystrophy J Biol Chem 271 44 27664 9 doi 10 1074 jbc 271 44 27664 PMID 8910357 Squarzoni S Villanova M Sabatelli P et al 1997 Intracellular detection of laminin alpha 2 chain in skin by electron microscopy immunocytochemistry comparison between normal and laminin alpha 2 chain deficient subjects Neuromuscul Disord 7 2 91 8 doi 10 1016 S0960 8966 96 00420 8 PMID 9131649 S2CID 140209385 Allamand V Sunada Y Salih MA et al 1997 Mild congenital muscular dystrophy in two patients with an internally deleted laminin alpha2 chain Hum Mol Genet 6 5 747 52 doi 10 1093 hmg 6 5 747 PMID 9158149 Durkin ME Loechel F Mattei MG et al 1997 Tissue specific expression of the human laminin alpha5 chain and mapping of the gene to human chromosome 20q13 2 13 3 and to distal mouse chromosome 2 near the locus for the ragged Ra mutation FEBS Lett 411 2 3 296 300 doi 10 1016 S0014 5793 97 00686 8 PMID 9271224 S2CID 45286880 Mrowiec T Melchar C Gorski A 1998 HIV protein mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium Arch Immunol Ther Exp Warsz 45 2 3 255 9 PMID 9597096 Koch M Olson PF Albus A et al 1999 Characterization and Expression of the Laminin g3 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 Kuang W Xu H Vilquin JT Engvall E 2000 Activation of the lama2 gene in muscle regeneration abortive regeneration in laminin alpha2 deficiency Lab Invest 79 12 1601 13 PMID 10616210 Pegoraro E Fanin M Trevisan CP et al 2000 A novel laminin alpha2 isoform in severe laminin alpha2 deficient congenital muscular dystrophy Neurology 55 8 1128 34 doi 10 1212 wnl 55 8 1128 PMID 11071490 S2CID 80274277 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 External links editGeneReviews NCBI NIH UW entry on Congenital Muscular Dystrophy Overview LOVD mutation database LAMA2 Overview of all the structural information available in the PDB for UniProt P24043 Laminin subunit alpha 2 at the PDBe KB nbsp This article on a gene on human chromosome 6 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Laminin subunit alpha 2 amp oldid 1142706864, wikipedia, wiki, book, books, library,
