Laminin subunit alpha-2

Protein-coding gene in the species Homo sapiens
LAMA2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4YEP, 4YEQ

Identifiers
AliasesLAMA2, LAMM, Laminin, alpha 2, laminin subunit alpha 2, MDC1A
External IDsOMIM: 156225; MGI: 99912; HomoloGene: 37306; GeneCards: LAMA2; OMA:LAMA2 - orthologs
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for LAMA2
Genomic location for LAMA2
Band6q22.33Start128,883,138 bp[1]
End129,516,566 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for LAMA2
Genomic location for LAMA2
Band10 A4|10 14.23 cMStart26,856,032 bp[2]
End27,495,754 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gastric mucosa

  • Achilles tendon

  • right ovary

  • left ovary

  • right lung

  • atrium

  • right auricle

  • 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
SpeciesHumanMouse
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 MbChr 10: 26.86 – 27.5 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000196569 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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.


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