Laminin subunit alpha-2

LAMA2
Identifiers
Aliases	LAMA2, LAMM, Laminin, alpha 2, laminin subunit alpha 2, MDC1A
External IDs	OMIM: 156225; MGI: 99912; GeneCards: LAMA2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4YEP, 4YEQ
Gene location (Human) Chr. Chromosome 6 (human) Band 6q22.33 Start 128,883,138 bp End 129,516,566 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10 A4|10 14.23 cM Start 26,856,032 bp End 27,495,754 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastric mucosa Achilles tendon right ovary left ovary right lung atrium right auricle of heart myocardium of left ventricle cardiac muscle tissue of right atrium pericardium Top expressed in sciatic nerve epithelium of lens efferent ductule utricle vestibular sensory epithelium ascending aorta vas deferens aortic valve right ventricle plantaris muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function structural molecule activity signaling receptor binding extracellular matrix structural constituent Cellular component extracellular region dendritic spine sarcolemma basement membrane extracellular matrix neuromuscular junction synaptic cleft collagen-containing extracellular matrix Biological process muscle 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 development Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse 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 Mb Chr 10: 26.86 – 27.5 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Laminin subunit alpha-2 is a protein that in humans is encoded by the LAMA2 gene.

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.

Upregulation of LAMA1 holds potential for treating LAMA2-related muscular dystrophy.

Further reading

• Timpl R (October 1996). "Macromolecular organization of basement membranes". Current Opinion in Cell Biology. 8 (5): 618–624. doi:10.1016/S0955-0674(96)80102-5. PMID 8939648.
• Belkin AM, Stepp MA (2000). "Integrins as receptors for laminins". Microscopy Research and Technique. 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, Tobias V, Ouvrier RA, Wilkinson I, et al. (October 2001). "The expanding phenotype of laminin alpha2 chain (merosin) abnormalities: case series and review". Journal of Medical Genetics. 38 (10): 649–657. doi:10.1136/jmg.38.10.649. PMC 1734735. PMID 11584042.
• Hori H, Kanamori T, Mizuta T, Yamaguchi N, Liu Y, Nagai Y (December 1994). "Human laminin M chain: epitope analysis of its monoclonal antibodies by immunoscreening of cDNA clones and tissue expression". Journal of Biochemistry. 116 (6): 1212–1219. doi:10.1093/oxfordjournals.jbchem.a124666. PMID 7535762.
• Helbling-Leclerc A, Zhang X, Topaloglu H, Cruaud C, Tesson F, Weissenbach J, et al. (October 1995). "Mutations in the laminin alpha 2-chain gene (LAMA2) cause merosin-deficient congenital muscular dystrophy". Nature Genetics. 11 (2): 216–218. doi:10.1038/ng1095-216. PMID 7550355. S2CID 34969060.
• Yamada H, Shimizu T, Tanaka T, Campbell KP, Matsumura K (September 1994). "Dystroglycan is a binding protein of laminin and merosin in peripheral nerve". FEBS Letters. 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 Research. 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". The Journal of Biological Chemistry. 271 (44): 27664–27669. doi:10.1074/jbc.271.44.27664. PMID 8910357.
• Squarzoni S, Villanova M, Sabatelli P, Malandrini A, Toti P, Pini A, et al. (March 1997). "Intracellular detection of laminin alpha 2 chain in skin by electron microscopy immunocytochemistry: comparison between normal and laminin alpha 2 chain deficient subjects". Neuromuscular Disorders. 7 (2): 91–98. doi:10.1016/S0960-8966(96)00420-8. PMID 9131649. S2CID 140209385.
• Allamand V, Sunada Y, Salih MA, Straub V, Ozo CO, Al-Turaiki MH, et al. (May 1997). "Mild congenital muscular dystrophy in two patients with an internally deleted laminin alpha2-chain". Human Molecular Genetics. 6 (5): 747–752. doi:10.1093/hmg/6.5.747. PMID 9158149.
• Durkin ME, Loechel F, Mattei MG, Gilpin BJ, Albrechtsen R, Wewer UM (July 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 Letters. 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". Archivum Immunologiae et Therapiae Experimentalis. 45 (2–3): 255–259. PMID 9597096.
• Koch M, Olson PF, Albus A, Jin W, Hunter DD, Brunken WJ, et al. (May 1999). "Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain". The Journal of Cell Biology. 145 (3): 605–618. 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". Laboratory Investigation; A Journal of Technical Methods and Pathology. 79 (12): 1601–1613. PMID 10616210.
• Pegoraro E, Fanin M, Trevisan CP, Angelini C, Hoffman EP (October 2000). "A novel laminin alpha2 isoform in severe laminin alpha2 deficient congenital muscular dystrophy". Neurology. 55 (8): 1128–1134. 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". Archives of Oral Biology. 46 (6): 545–555. doi:10.1016/S0003-9969(01)00014-0. PMID 11311202.

External links

• GeneReviews/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.