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Laminin subunit alpha-2

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LAMA2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesLAMA2, LAMM, Laminin, alpha 2, laminin subunit alpha 2, MDC1A
External IDsOMIM: 156225; MGI: 99912; HomoloGene: 37306; GeneCards: LAMA2; OMA:LAMA2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

3908

16773

Ensembl

ENSG00000196569

ENSMUSG00000019899

UniProt

P24043

Q60675

RefSeq (mRNA)

NM_000426
NM_001079823

NM_008481

RefSeq (protein)

NP_000417
NP_001073291

NP_032507

Location (UCSC)Chr 6: 128.88 – 129.52 MbChr 10: 26.86 – 27.5 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Laminin subunit alpha-2 is a protein that in humans is encoded by the LAMA2 gene.[5][6][7]

Function

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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]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196569 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019899 – 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. ^ 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 2185464.3264-8&rft.date=1990-06&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC53880#id-name=PMC&rft_id=info:pmid/2185464&rft_id=info:doi/10.1073/pnas.87.9.3264&rft_id=info:bibcode/1990PNAS...87.3264E&rft.aulast=Ehrig&rft.aufirst=K&rft.au=Leivo, I&rft.au=Argraves, WS&rft.au=Ruoslahti, E&rft.au=Engvall, E&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC53880&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  6. ^ 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 8294519.381-94&rft.date=1994-02&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119934#id-name=PMC&rft_id=info:pmid/8294519&rft_id=info:doi/10.1083/jcb.124.3.381&rft.aulast=Vuolteenaho&rft.aufirst=R&rft.au=Nissinen, M&rft.au=Sainio, K&rft.au=Byers, M&rft.au=Eddy, R&rft.au=Hirvonen, H&rft.au=Shows, TB&rft.au=Sariola, H&rft.au=Engvall, E&rft.au=Tryggvason, K&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119934&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  7. ^ a b "Entrez Gene: LAMA2 laminin, alpha 2 (merosin, congenital muscular dystrophy)".

Further reading

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  • 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 8939648.618-24&rft.date=1997&rft_id=info:doi/10.1016/S0955-0674(96)80102-5&rft_id=info:pmid/8939648&rft.au=Timpl R&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 48631383.280-301&rft.date=2000&rft_id=https://api.semanticscholar.org/CorpusID:48631383#id-name=S2CID&rft_id=info:pmid/11054877&rft_id=info:doi/10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O&rft.aulast=Belkin&rft.aufirst=AM&rft.au=Stepp, MA&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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. PMC 1734735. PMID 11584042.649-57&rft.date=2002&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1734735#id-name=PMC&rft_id=info:pmid/11584042&rft_id=info:doi/10.1136/jmg.38.10.649&rft.aulast=Jones&rft.aufirst=KJ&rft.au=Morgan, G&rft.au=Johnston, H&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1734735&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 7535762.1212-9&rft.date=1995&rft_id=info:doi/10.1093/oxfordjournals.jbchem.a124666&rft_id=info:pmid/7535762&rft.aulast=Hori&rft.aufirst=H&rft.au=Kanamori, T&rft.au=Mizuta, T&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 34969060.216-8&rft.date=1995&rft_id=https://api.semanticscholar.org/CorpusID:34969060#id-name=S2CID&rft_id=info:pmid/7550355&rft_id=info:doi/10.1038/ng1095-216&rft.aulast=Helbling-Leclerc&rft.aufirst=A&rft.au=Zhang, X&rft.au=Topaloglu, H&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 7928631. S2CID 17529055.49-53&rft.date=1994&rft_id=https://api.semanticscholar.org/CorpusID:17529055#id-name=S2CID&rft_id=info:pmid/7928631&rft_id=info:doi/10.1016/0014-5793(94)00917-1&rft.aulast=Yamada&rft.aufirst=H&rft.au=Shimizu, T&rft.au=Tanaka, T&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 8889548.791-806&rft.date=1997&rft_id=info:doi/10.1101/gr.6.9.791&rft_id=info:pmid/8889548&rft.aulast=Bonaldo&rft.aufirst=MF&rft.au=Lennon, G&rft.au=Soares, MB&rft_id=https://doi.org/10.1101%2Fgr.6.9.791&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 8910357.27664-9&rft.date=1996&rft_id=info:doi/10.1074/jbc.271.44.27664&rft_id=info:pmid/8910357&rft.aulast=Zhang&rft.aufirst=X&rft.au=Vuolteenaho, R&rft.au=Tryggvason, K&rft_id=https://doi.org/10.1074%2Fjbc.271.44.27664&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 140209385.91-8&rft.date=1997&rft_id=https://api.semanticscholar.org/CorpusID:140209385#id-name=S2CID&rft_id=info:pmid/9131649&rft_id=info:doi/10.1016/S0960-8966(96)00420-8&rft.aulast=Squarzoni&rft.aufirst=S&rft.au=Villanova, M&rft.au=Sabatelli, P&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 9158149.747-52&rft.date=1997&rft_id=info:doi/10.1093/hmg/6.5.747&rft_id=info:pmid/9158149&rft.aulast=Allamand&rft.aufirst=V&rft.au=Sunada, Y&rft.au=Salih, MA&rft_id=https://doi.org/10.1093%2Fhmg%2F6.5.747&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 45286880.2–3&rft.pages=296-300&rft.date=1997&rft_id=https://api.semanticscholar.org/CorpusID:45286880#id-name=S2CID&rft_id=info:pmid/9271224&rft_id=info:doi/10.1016/S0014-5793(97)00686-8&rft.aulast=Durkin&rft.aufirst=ME&rft.au=Loechel, F&rft.au=Mattei, MG&rft_id=https://doi.org/10.1016%2FS0014-5793%2897%2900686-8&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 9597096.2–3&rft.pages=255-9&rft.date=1998&rft_id=info:pmid/9597096&rft.aulast=Mrowiec&rft.aufirst=T&rft.au=Melchar, C&rft.au=Górski, A&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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. PMC 2185082. PMID 10225960.605-18&rft.date=1999&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2185082#id-name=PMC&rft_id=info:pmid/10225960&rft_id=info:doi/10.1083/jcb.145.3.605&rft.aulast=Koch&rft.aufirst=M&rft.au=Olson, PF&rft.au=Albus, A&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2185082&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 10616210.1601-13&rft.date=2000&rft_id=info:pmid/10616210&rft.aulast=Kuang&rft.aufirst=W&rft.au=Xu, H&rft.au=Vilquin, JT&rft.au=Engvall, E&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 80274277.1128-34&rft.date=2000&rft_id=https://api.semanticscholar.org/CorpusID:80274277#id-name=S2CID&rft_id=info:pmid/11071490&rft_id=info:doi/10.1212/wnl.55.8.1128&rft.aulast=Pegoraro&rft.aufirst=E&rft.au=Fanin, M&rft.au=Trevisan, CP&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
  • 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 11311202.545-55&rft.date=2001&rft_id=info:doi/10.1016/S0003-9969(01)50014-0&rft_id=info:pmid/11311202&rft.aulast=McArthur&rft.aufirst=CP&rft.au=Wang, Y&rft.au=Heruth, D&rft.au=Gustafson, S&rfr_id=info:sid/en.wikipedia.org:Laminin subunit alpha-2" class="Z3988">
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