Laminin, alpha 5

Available structures
PDBOrtholog search: PDBe RCSB
Aliases LAMA5, Laminin, alpha 5
External IDs MGI: 105382 HomoloGene: 4060 GeneCards: LAMA5
Genetically Related Diseases
colorectal cancer[1]
RNA expression pattern
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]
View/Edit HumanView/Edit Mouse

Laminin subunit alpha-5 is a protein that in humans is encoded by the LAMA5 gene.[4][5]


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.[5]


Laminin, alpha 5 has been shown to interact with BCAM.[6][7]


  1. "Diseases that are genetically associated with LAMA5 view/edit references on wikidata".
  2. "Human PubMed Reference:".
  3. "Mouse PubMed Reference:".
  4. 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.
  5. 1 2 "Entrez Gene: LAMA5 laminin, alpha 5".
  6. 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.
  7. 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.

Further reading

  • 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. 
  • 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 2141627Freely accessible. PMID 9245798. 
  • Tiger CF, Champliaud MF, Pedrosa-Domellof F, Thornell LE, Ekblom P, Gullberg D (Nov 1997). "Presence of laminin alpha5 chain and lack of laminin alpha1 chain during human muscle development and in muscular dystrophies". The Journal of Biological Chemistry. 272 (45): 28590–5. doi:10.1074/jbc.272.45.28590. PMID 9353324. 
  • 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): 255–9. PMID 9597096. 
  • Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Feb 1998). "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Research. 5 (1): 31–9. doi:10.1093/dnares/5.1.31. PMID 9628581. 
  • Shimizu H, Hosokawa H, Ninomiya H, Miner JH, Masaki T (Apr 1999). "Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan". The Journal of Biological Chemistry. 274 (17): 11995–2000. doi:10.1074/jbc.274.17.11995. PMID 10207021. 
  • Son YJ, Scranton TW, Sunderland WJ, Baek SJ, Miner JH, Sanes JR, Carlson SS (Jan 2000). "The synaptic vesicle protein SV2 is complexed with an alpha5-containing laminin on the nerve terminal surface". The Journal of Biological Chemistry. 275 (1): 451–60. doi:10.1074/jbc.275.1.451. PMID 10617638. 
  • Köhler D, Kruse M, Stöcker W, Sterchi EE (Jan 2000). "Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro". FEBS Letters. 465 (1): 2–7. doi:10.1016/S0014-5793(99)01712-3. PMID 10620696. 
  • Kikkawa Y, Sanzen N, Fujiwara H, Sonnenberg A, Sekiguchi K (Mar 2000). "Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins". Journal of Cell Science. 113 ( Pt 5) (5): 869–76. PMID 10671376. 
  • Champliaud MF, Virtanen I, Tiger CF, Korhonen M, Burgeson R, Gullberg D (Sep 2000). "Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta". Experimental Cell Research. 259 (2): 326–35. doi:10.1006/excr.2000.4980. PMID 10964500. 
  • Libby RT, Champliaud MF, Claudepierre T, Xu Y, Gibbons EP, Koch M, Burgeson RE, Hunter DD, Brunken WJ (Sep 2000). "Laminin expression in adult and developing retinae: evidence of two novel CNS laminins". The Journal of Neuroscience. 20 (17): 6517–28. PMC 2924637Freely accessible. PMID 10964957. 
  • Pierce RA, Griffin GL, Miner JH, Senior RM (Dec 2000). "Expression patterns of laminin alpha1 and alpha5 in human lung during development". American Journal of Respiratory Cell and Molecular Biology. 23 (6): 742–7. doi:10.1165/ajrcmb.23.6.4202. PMID 11104726. 
  • 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. 
  • Saghizadeh M, Brown DJ, Castellon R, Chwa M, Huang GH, Ljubimova JY, Rosenberg S, Spirin KS, Stolitenko RB, Adachi W, Kinoshita S, Murphy G, Windsor LJ, Kenney MC, Ljubimov AV (Feb 2001). "Overexpression of matrix metalloproteinase-10 and matrix metalloproteinase-3 in human diabetic corneas: a possible mechanism of basement membrane and integrin alterations". The American Journal of Pathology. 158 (2): 723–34. doi:10.1016/S0002-9440(10)64015-1. PMC 1850323Freely accessible. PMID 11159210. 
  • McArthur CP, Wang Y, Heruth D, Gustafson S (Jun 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): 545–55. doi:10.1016/S0003-9969(01)00014-0. PMID 11311202. 
  • Gagnoux-Palacios L, Allegra M, Spirito F, Pommeret O, Romero C, Ortonne JP, Meneguzzi G (May 2001). "The short arm of the laminin gamma2 chain plays a pivotal role in the incorporation of laminin 5 into the extracellular matrix and in cell adhesion". The Journal of Cell Biology. 153 (4): 835–50. doi:10.1083/jcb.153.4.835. PMC 2192378Freely accessible. PMID 11352943. 
  • Nagase T, Kikuno R, Ohara O (Aug 2001). "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins". DNA Research. 8 (4): 179–87. doi:10.1093/dnares/8.4.179. PMID 11572484. 
  • Doi M, Thyboll J, Kortesmaa J, Jansson K, Iivanainen A, Parvardeh M, Timpl R, Hedin U, Swedenborg J, Tryggvason K (Apr 2002). "Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells". The Journal of Biological Chemistry. 277 (15): 12741–8. doi:10.1074/jbc.M111228200. PMID 11821406. 

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