Laminin, alpha 5

Laminin, alpha 5
Identifiers
Symbols	LAMA5 ; KIAA1907
External IDs	OMIM: 601033 MGI: 105382 HomoloGene: 4060 GeneCards: LAMA5 Gene
Gene ontology Molecular function • integrin binding • structural molecule activity Cellular component • extracellular region • basement membrane • basal lamina • laminin-5 complex • extracellular space • nucleus • extracellular matrix • laminin-10 complex • laminin-11 complex • extracellular exosome Biological process • angiogenesis • branching involved in ureteric bud morphogenesis • morphogenesis of a polarized epithelium • neural crest cell migration • hair follicle development • cytoskeleton organization • integrin-mediated signaling pathway • muscle organ development • cell recognition • cell proliferation • embryo development • morphogenesis of embryonic epithelium • cell migration • extracellular matrix disassembly • cell differentiation • regulation of cell adhesion • extracellular matrix organization • lung development • regulation of cell migration • substrate adhesion-dependent cell spreading • regulation of cell proliferation • cilium assembly • odontogenesis of dentin-containing tooth • endothelial cell differentiation • regulation of embryonic development • focal adhesion assembly • branching involved in salivary gland morphogenesis • establishment of protein localization to plasma membrane Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
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: 62.31 – 62.37 Mb	Chr 2: 180.18 – 180.23 Mb
PubMed search

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

Function

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]

Interactions

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

References

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. "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

• 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 2141627. 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 2924637. 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 1850323. 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 2192378. 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.