Laminin subunit alpha-2

LAMA2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4YEP, 4YEQ
Identifiers
Aliases	LAMA2 , LAMM, Laminin, alpha 2, laminin subunit alpha 2, MDC1A
External IDs	OMIM: 156225; MGI: 99912; HomoloGene: 37306; GeneCards: LAMA2; OMA:LAMA2 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) [1] Band 6q22.33 Start 128,883,138 bp [1] End 129,516,566 bp [1]
Gene location (Mouse) Chr. Chromosome 10 (mouse) [2] Band 10 A4|10 14.23 cM Start 26,856,032 bp [2] End 27,495,754 bp [2]
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 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 [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000196569 – Ensembl, May 2017
2. 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.
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.
7. "Entrez Gene: LAMA2 laminin, alpha 2 (merosin, congenital muscular dystrophy)".

Further reading

• 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. 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, 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. 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

• 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 .