Laminin, alpha 5

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Laminin, alpha 5
Symbols LAMA5 ; KIAA1907
External IDs OMIM601033 MGI105382 HomoloGene4060 GeneCards: LAMA5 Gene
RNA expression pattern
PBB GE LAMA5 210150 s at tn.png
More reference expression data
Species Human Mouse
Entrez 3911 16776
Ensembl ENSG00000130702 ENSMUSG00000015647
UniProt O15230 Q61001
RefSeq (mRNA) NM_005560 NM_001081171
RefSeq (protein) NP_005551 NP_001074640
Location (UCSC) Chr 20:
60.88 – 60.94 Mb
Chr 2:
180.18 – 180.23 Mb
PubMed search [1] [2]

Laminin subunit alpha-5 is a protein that in humans is encoded by the LAMA5 gene.[1][2]

Components of the extracellular matrix exert myriad effects on tissues throughout the body. In particular, the laminins, a family of heterotrimeric extracellular glycoproteins, affect tissue development and integrity in such diverse organs as the kidney, lung, skin, and nervous system. It is thought that laminins mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Laminins function as heterotrimeric complexes of alpha, beta, and gamma chains, with each chain type representing a different subfamily of proteins. The protein encoded by this gene belongs to the alpha subfamily of laminin chains and is a major component of basement membranes. Two transcript variants encoding different isoforms have been found for this gene, but the full-length nature of one of them has not been determined.[2]


Laminin, alpha 5 has been shown to interact with BCAM,[3][4] FBLN2[5] and Collagen, type VII, alpha 1.[6]


  1. ^ Durkin ME, Loechel F, Mattei MG, Gilpin BJ, Albrechtsen R, Wewer UM (Sep 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. 
  2. ^ a b "Entrez Gene: LAMA5 laminin, alpha 5". 
  3. ^ Parsons, S F; Lee G; Spring F A; Willig T N; Peters L L; Gimm J A; Tanner M J; Mohandas N; Anstee D J; Chasis J A (Jan 2001). "Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity". Blood (UNITED STATES) 97 (1): 312–20. doi:10.1182/blood.V97.1.312. ISSN 0006-4971. PMID 11133776. 
  4. ^ Kikkawa, Yamato; Moulson Casey L; Virtanen Ismo; Miner Jeffrey H (Nov 2002). "Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo". J. Biol. Chem. (United States) 277 (47): 44864–9. doi:10.1074/jbc.M208731200. ISSN 0021-9258. PMID 12244066. 
  5. ^ Utani, A; Nomizu M; Yamada Y (Jan 1997). "Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences". J. Biol. Chem. (UNITED STATES) 272 (5): 2814–20. doi:10.1074/jbc.272.5.2814. ISSN 0021-9258. PMID 9006922. 
  6. ^ Rousselle, P; Keene D R; Ruggiero F; Champliaud M F; Rest M; Burgeson R E (Aug 1997). "Laminin 5 Binds the NC-1 Domain of Type VII Collagen". J. Cell Biol. (UNITED STATES) 138 (3): 719–28. doi:10.1083/jcb.138.3.719. ISSN 0021-9525. PMC 2141627. PMID 9245798. 

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