{{Short description|Protein-coding gene in the species Homo sapiens}} {{cs1 config|name-list-style=vanc|display-authors=6}} {{Infobox_gene}} '''Laminin subunit alpha-2''' is a protein that in humans is encoded by the ''LAMA2'' gene.<ref name="pmid2185464">{{cite journal | vauthors = Ehrig K, Leivo I, Argraves WS, Ruoslahti E, Engvall E | date = June 1990 | title = Merosin, a tissue-specific basement membrane protein, is a laminin-like protein | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 87 | issue = 9 | pages = 3264–3268 | doi = 10.1073/pnas.87.9.3264 | doi-access = free | pmc = 53880 | pmid = 2185464 | bibcode = 1990PNAS...87.3264E }}</ref><ref name="pmid8294519">{{cite journal | vauthors = Vuolteenaho R, Nissinen M, Sainio K, Byers M, Eddy R, Hirvonen H, Shows TB, Sariola H, Engvall E, Tryggvason K | date = February 1994 | title = Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues | journal = The Journal of Cell Biology | volume = 124 | issue = 3 | pages = 381–394 | doi = 10.1083/jcb.124.3.381 | pmc = 2119934 | pmid = 8294519 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LAMA2 laminin, alpha 2 (merosin, congenital muscular dystrophy)| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=3908}}</ref>
== Function ==
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.<ref name="entrez" />
Upregulation of ''LAMA1'' holds potential for treating LAMA2-related muscular dystrophy.<ref>{{cite journal | vauthors = Kemaladewi DU, Bassi PS, Erwood S, Al-Basha D, Gawlik KI, Lindsay K, Hyatt E, Kember R, Place KM, Marks RM, Durbeej M, Prescott SA, Ivakine EA, Cohn RD | date = August 2019 | title = A mutation-independent approach for muscular dystrophy via upregulation of a modifier gene | journal = Nature | volume = 572 | issue = 7767 | pages = 125–130 | doi = 10.1038/s41586-019-1430-x | pmid = 31341277 }}</ref><ref>{{cite journal | vauthors = Liu Y, Tan D, Ma K, Luo H, Mao J, Luo J, Shen Q, Xu L, Yang S, Ge L, Guo Y, Zhang H, Xiong H | title = Lama1 upregulation prolongs the lifespan of the dy<sup>H</sup>/dy<sup>H</sup> mouse model of LAMA2-related congenital muscular dystrophy | journal = Journal of Genetics and Genomics = Yi Chuan Xue Bao | volume = 51 | issue = 10 | pages = 1066–1078 | date = October 2024 | pmid = 38777118 | doi = 10.1016/j.jgg.2024.05.005 | language = en-US }}</ref>
== References == {{reflist}}
== Further reading == {{refbegin | 2}} * {{cite journal | vauthors = Timpl R | title = Macromolecular organization of basement membranes | journal = Current Opinion in Cell Biology | volume = 8 | issue = 5 | pages = 618–624 | date = October 1996 | pmid = 8939648 | doi = 10.1016/S0955-0674(96)80102-5 }} * {{cite journal |vauthors=Belkin AM, Stepp MA |title=Integrins as receptors for laminins |journal=Microscopy Research and Technique |volume=51 |issue= 3 |pages= 280–301 |year= 2000 |pmid= 11054877 |doi= 10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O |s2cid=45941383 }} * {{cite journal | vauthors = Jones KJ, Morgan G, Johnston H, Tobias V, Ouvrier RA, Wilkinson I, North KN | title = The expanding phenotype of laminin alpha2 chain (merosin) abnormalities: case series and review | journal = Journal of Medical Genetics | volume = 38 | issue = 10 | pages = 649–657 | date = October 2001 | pmid = 11584042 | doi = 10.1136/jmg.38.10.649 | pmc = 1734735 }} * {{cite journal | vauthors = Hori H, Kanamori T, Mizuta T, Yamaguchi N, Liu Y, Nagai Y | title = Human laminin M chain: epitope analysis of its monoclonal antibodies by immunoscreening of cDNA clones and tissue expression | journal = Journal of Biochemistry | volume = 116 | issue = 6 | pages = 1212–1219 | date = December 1994 | pmid = 7535762 | doi = 10.1093/oxfordjournals.jbchem.a124666 | doi-access = free | title-link = immunoscreening }} * {{cite journal | vauthors = Helbling-Leclerc A, Zhang X, Topaloglu H, Cruaud C, Tesson F, Weissenbach J, Tomé FM, Schwartz K, Fardeau M, Tryggvason K | title = Mutations in the laminin alpha 2-chain gene (LAMA2) cause merosin-deficient congenital muscular dystrophy | journal = Nature Genetics | volume = 11 | issue = 2 | pages = 216–218 | date = October 1995 | pmid = 7550355 | doi = 10.1038/ng1095-216 | s2cid = 34969060 }} * {{cite journal | vauthors = Yamada H, Shimizu T, Tanaka T, Campbell KP, Matsumura K | title = Dystroglycan is a binding protein of laminin and merosin in peripheral nerve | journal = FEBS Letters | volume = 352 | issue = 1 | pages = 49–53 | date = September 1994 | pmid = 7925941 | doi = 10.1016/0014-5793(94)00917-1 | s2cid = 17529055 }} * {{cite journal |vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Research |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 |doi-access=free }} * {{cite journal | vauthors = Zhang X, Vuolteenaho R, Tryggvason K | year = 1996 | title = Structure of the human laminin alpha2-chain gene (LAMA2), which is affected in congenital muscular dystrophy | journal = The Journal of Biological Chemistry | volume = 271 | issue = 44 | pages = 27664–27669 | doi = 10.1074/jbc.271.44.27664 | doi-access = free | pmid = 8910357 }} * {{cite journal | vauthors = Squarzoni S, Villanova M, Sabatelli P, Malandrini A, Toti P, Pini A, Merlini L, Guazzi GC, Maraldi NM | title = Intracellular detection of laminin alpha 2 chain in skin by electron microscopy immunocytochemistry: comparison between normal and laminin alpha 2 chain deficient subjects | journal = Neuromuscular Disorders | volume = 7 | issue = 2 | pages = 91–98 | date = March 1997 | pmid = 9131649 | doi = 10.1016/S0960-8966(96)00420-8 | s2cid = 140209385 }} * {{cite journal | vauthors = Allamand V, Sunada Y, Salih MA, Straub V, Ozo CO, Al-Turaiki MH, Akbar M, Kolo T, Colognato H, Zhang X, Sorokin LM, Yurchenco PD, Tryggvason K, Campbell KP | title = Mild congenital muscular dystrophy in two patients with an internally deleted laminin alpha2-chain | journal = Human Molecular Genetics | volume = 6 | issue = 5 | pages = 747–752 | date = May 1997 | pmid = 9158149 | doi = 10.1093/hmg/6.5.747 | doi-access = free }} * {{cite journal | vauthors = Durkin ME, Loechel F, Mattei MG, Gilpin BJ, Albrechtsen R, Wewer UM | date = July 1997 | title = 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 | journal = FEBS Letters | volume = 411 | issue = 2–3 | pages = 296–300 | doi = 10.1016/S0014-5793(97)00686-8 | doi-access = free | pmid = 9271224 | s2cid = 45286880 }} * {{cite journal | vauthors = Mrowiec T, Melchar C, Górski A | year = 1998 | title = HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium | journal = Archivum Immunologiae et Therapiae Experimentalis | volume = 45 | issue = 2–3 | pages = 255–259 | pmid = 9597096 }} * {{cite journal | vauthors = Koch M, Olson PF, Albus A, Jin W, Hunter DD, Brunken WJ, Burgeson RE, Champliaud MF | title = Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain | journal = The Journal of Cell Biology | volume = 145 | issue = 3 | pages = 605–618 | date = May 1999 | pmid = 10225960 | doi = 10.1083/jcb.145.3.605 | pmc = 2185082 }} * {{cite journal | vauthors = Kuang W, Xu H, Vilquin JT, Engvall E | year = 2000 | title = Activation of the lama2 gene in muscle regeneration: abortive regeneration in laminin alpha2-deficiency | journal = Laboratory Investigation; A Journal of Technical Methods and Pathology | volume = 79 | issue = 12 | pages = 1601–1613 | pmid = 10616210 }} * {{cite journal | vauthors = Pegoraro E, Fanin M, Trevisan CP, Angelini C, Hoffman EP | title = A novel laminin alpha2 isoform in severe laminin alpha2 deficient congenital muscular dystrophy | journal = Neurology | volume = 55 | issue = 8 | pages = 1128–1134 | date = October 2000 | pmid = 11071490 | doi = 10.1212/wnl.55.8.1128 | s2cid = 80274277 }} * {{cite journal | vauthors = McArthur CP, Wang Y, Heruth D, Gustafson S | year = 2001 | title = 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 | journal = Archives of Oral Biology | volume = 46 | issue = 6 | pages = 545–555 | doi = 10.1016/S0003-9969(01)00014-0 | pmid = 11311202 }} {{refend}}
== External links == * [https://www.ncbi.nlm.nih.gov/books/NBK1291/ GeneReviews/NCBI/NIH/UW entry on Congenital Muscular Dystrophy Overview] * LOVD mutation database: [http://www.dmd.nl/nmdb2/?select_db=LAMA2 LAMA2] * {{PDBe-KB2|P24043|Laminin subunit alpha-2}}
{{Fibrous proteins}}
{{gene-6-stub}}
Category:Laminins