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]
↑Kemaladewi DU, Bassi PS, Erwood S, Al-Basha D, Gawlik KI, Lindsay K, etal. (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. PMID31341277.
↑Liu Y, Tan D, Ma K, Luo H, Mao J, Luo J, etal. (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. PMID38777118.
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. PMID8939648.
Helbling-Leclerc A, Zhang X, Topaloglu H, Cruaud C, Tesson F, Weissenbach J, etal. (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. PMID7550355. S2CID34969060.
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. PMID7925941. S2CID17529055.
Squarzoni S, Villanova M, Sabatelli P, Malandrini A, Toti P, Pini A, etal. (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. PMID9131649. S2CID140209385.
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. PMID9597096.
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. PMID10616210.
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. PMID11071490. S2CID80274277.
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. PMID11311202.
