Laminin, alpha 5

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Available structures
PDB Ortholog search: PDBe RCSB
Aliases LAMA5, Laminin, alpha 5
External IDs MGI: 105382 HomoloGene: 4060 GeneCards: 3911
Genetically Related Diseases
Disease Name References
colorectal cancer
RNA expression pattern
PBB GE LAMA5 210150 s at tn.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 20: 62.31 – 62.37 Mb Chr 2: 180.18 – 180.23 Mb
PubMed search [2] [3]
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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 (Jul 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. 
  2. ^ a b "Entrez Gene: LAMA5 laminin, alpha 5". 
  3. ^ Parsons SF, Lee G, Spring FA, Willig TN, Peters LL, Gimm JA, Tanner MJ, Mohandas N, Anstee DJ, Chasis JA (Jan 2001). "Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity". Blood 97 (1): 312–20. doi:10.1182/blood.V97.1.312. PMID 11133776. 
  4. ^ Kikkawa Y, Moulson CL, Virtanen I, Miner JH (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". The Journal of Biological Chemistry 277 (47): 44864–9. doi:10.1074/jbc.M208731200. 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". The Journal of Biological Chemistry 272 (5): 2814–20. doi:10.1074/jbc.272.5.2814. PMID 9006922. 
  6. ^ Rousselle P, Keene DR, Ruggiero F, Champliaud MF, Rest M, Burgeson RE (Aug 1997). "Laminin 5 binds the NC-1 domain of type VII collagen". The Journal of Cell Biology 138 (3): 719–28. doi:10.1083/jcb.138.3.719. PMC 2141627. PMID 9245798. 

Further reading[edit]