Biology:Laminin, alpha 5
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
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]
References
- ↑ "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. Jul 1997. doi:10.1016/S0014-5793(97)00686-8. PMID 9271224.
- ↑ 2.0 2.1 "Entrez Gene: LAMA5 laminin, alpha 5". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3911.
- ↑ "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. Jan 2001. doi:10.1182/blood.V97.1.312. PMID 11133776.
- ↑ "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. Nov 2002. doi:10.1074/jbc.M208731200. PMID 12244066.
Further reading
- "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. Jan 1997. doi:10.1074/jbc.272.5.2814. PMID 9006922.
- "Laminin 5 binds the NC-1 domain of type VII collagen". The Journal of Cell Biology 138 (3): 719–28. Aug 1997. doi:10.1083/jcb.138.3.719. PMID 9245798.
- "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. Nov 1997. doi:10.1074/jbc.272.45.28590. PMID 9353324.
- "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. 1998. PMID 9597096.
- "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. Feb 1998. doi:10.1093/dnares/5.1.31. PMID 9628581.
- "Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan". The Journal of Biological Chemistry 274 (17): 11995–2000. Apr 1999. doi:10.1074/jbc.274.17.11995. PMID 10207021.
- "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. Jan 2000. doi:10.1074/jbc.275.1.451. PMID 10617638.
- "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. Jan 2000. doi:10.1016/S0014-5793(99)01712-3. PMID 10620696.
- "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. Mar 2000. doi:10.1242/jcs.113.5.869. PMID 10671376.
- "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. Sep 2000. doi:10.1006/excr.2000.4980. PMID 10964500.
- "Laminin expression in adult and developing retinae: evidence of two novel CNS laminins". The Journal of Neuroscience 20 (17): 6517–28. Sep 2000. doi:10.1523/JNEUROSCI.20-17-06517.2000. PMID 10964957.
- "Expression patterns of laminin alpha1 and alpha5 in human lung during development". American Journal of Respiratory Cell and Molecular Biology 23 (6): 742–7. Dec 2000. doi:10.1165/ajrcmb.23.6.4202. PMID 11104726.
- "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. Jan 2001. doi:10.1182/blood.V97.1.312. PMID 11133776.
- "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. Feb 2001. doi:10.1016/S0002-9440(10)64015-1. PMID 11159210.
- "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. Jun 2001. doi:10.1016/S0003-9969(01)00014-0. PMID 11311202.
- "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. May 2001. doi:10.1083/jcb.153.4.835. PMID 11352943.
- "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. Aug 2001. doi:10.1093/dnares/8.4.179. PMID 11572484.
- "Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells". The Journal of Biological Chemistry 277 (15): 12741–8. Apr 2002. doi:10.1074/jbc.M111228200. PMID 11821406.
 |
