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]
Upregulation of LAMA1 holds potential for treating LAMA2-related muscular dystrophy.[8][9]
References
- ^ 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 (June 1990). “Merosin, a tissue-specific basement membrane protein, is a laminin-like protein”. Proceedings of the National Academy of Sciences of the United States of America. 87 (9): 3264–3268. 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, et al. (February 1994). “Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues”. The Journal of Cell Biology. 124 (3): 381–394. doi:10.1083/jcb.124.3.381. PMC 2119934. PMID 8294519.
- ^ a b “Entrez Gene: LAMA2 laminin, alpha 2 (merosin, congenital muscular dystrophy)”.
- ^ Kemaladewi DU, Bassi PS, Erwood S, Al-Basha D, Gawlik KI, Lindsay K, et al. (August 2019). “A mutation-independent approach for muscular dystrophy via upregulation of a modifier gene”. Nature. 572 (7767): 125–130. doi:10.1038/s41586-019-1430-x. PMID 31341277.
- ^ Liu Y, Tan D, Ma K, Luo H, Mao J, Luo J, et al. (October 2024). “Lama1 upregulation prolongs the lifespan of the dyH/dyH mouse model of LAMA2-related congenital muscular dystrophy”. Journal of Genetics and Genomics = Yi Chuan Xue Bao. 51 (10): 1066–1078. doi:10.1016/j.jgg.2024.05.005. PMID 38777118.
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.