Laminin, alpha 5

From Wikipedia, the free encyclopedia

Laminin, alpha 5

Identifiers

LAMA5; KIAA1907

External IDs

OMIM: 601033 MGI: 105382 HomoloGene: 4060

Gene ontology
Molecular Function:	• receptor binding • structural molecule activity • protein binding
Cellular Component:	• proteinaceous extracellular matrix • basal lamina • laminin-1 complex • membrane • integral to membrane
Biological Process:	• cell adhesion • regulation of cell adhesion • regulation of cell migration • regulation of embryonic development

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005560 (mRNA)
NP_005551 (protein)

XM_203796 (mRNA)
XP_203796 (protein)

Location

Chr 20: 60.32 - 60.38 Mb

Chr 2: 180.11 - 180.16 Mb

Pubmed search

[1]

[2]

Laminin, alpha 5, also known as LAMA5, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: LAMA5 laminin, alpha 5.

[edit] Further reading

Utani A, Nomizu M, Yamada Y (1997). "Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences.". J. Biol. Chem. 272 (5): 2814–20. PMID 9006922.
Rousselle P, Keene DR, Ruggiero F, et al. (1997). "Laminin 5 binds the NC-1 domain of type VII collagen.". J. Cell Biol. 138 (3): 719–28. PMID 9245798.
Durkin ME, Loechel F, Mattei MG, et al. (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. PMID 9271224.
Tiger CF, Champliaud MF, Pedrosa-Domellof F, et al. (1997). "Presence of laminin alpha5 chain and lack of laminin alpha1 chain during human muscle development and in muscular dystrophies.". J. Biol. Chem. 272 (45): 28590–5. PMID 9353324.
Mrowiec T, Melchar C, Górski A (1998). "HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium.". Arch. Immunol. Ther. Exp. (Warsz.) 45 (2-3): 255–9. PMID 9597096.
Nagase T, Ishikawa K, Miyajima N, et al. (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 Res. 5 (1): 31–9. PMID 9628581.
Shimizu H, Hosokawa H, Ninomiya H, et al. (1999). "Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan.". J. Biol. Chem. 274 (17): 11995–2000. PMID 10207021.
Son YJ, Scranton TW, Sunderland WJ, et al. (2000). "The synaptic vesicle protein SV2 is complexed with an alpha5-containing laminin on the nerve terminal surface.". J. Biol. Chem. 275 (1): 451–60. PMID 10617638.
Köhler D, Kruse M, Stöcker W, Sterchi EE (2000). "Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro.". FEBS Lett. 465 (1): 2–7. PMID 10620696.
Kikkawa Y, Sanzen N, Fujiwara H, et al. (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.". J. Cell. Sci. 113 ( Pt 5): 869–76. PMID 10671376.
Champliaud MF, Virtanen I, Tiger CF, et al. (2000). "Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta.". Exp. Cell Res. 259 (2): 326–35. doi:10.1006/excr.2000.4980. PMID 10964500.
Libby RT, Champliaud MF, Claudepierre T, et al. (2000). "Laminin expression in adult and developing retinae: evidence of two novel CNS laminins.". J. Neurosci. 20 (17): 6517–28. PMID 10964957.
Pierce RA, Griffin GL, Miner JH, Senior RM (2001). "Expression patterns of laminin alpha1 and alpha5 in human lung during development.". Am. J. Respir. Cell Mol. Biol. 23 (6): 742–7. PMID 11104726.
Parsons SF, Lee G, Spring FA, et al. (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. PMID 11133776.
Saghizadeh M, Brown DJ, Castellon R, et al. (2001). "Overexpression of matrix metalloproteinase-10 and matrix metalloproteinase-3 in human diabetic corneas: a possible mechanism of basement membrane and integrin alterations.". Am. J. Pathol. 158 (2): 723–34. PMID 11159210.
McArthur CP, Wang Y, Heruth D, Gustafson S (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.". Arch. Oral Biol. 46 (6): 545–55. PMID 11311202.
Gagnoux-Palacios L, Allegra M, Spirito F, et al. (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.". J. Cell Biol. 153 (4): 835–50. PMID 11352943.
Nagase T, Kikuno R, Ohara O (2002). "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 Res. 8 (4): 179–87. PMID 11572484.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
Doi M, Thyboll J, Kortesmaa J, et al. (2002). "Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells.". J. Biol. Chem. 277 (15): 12741–8. doi:10.1074/jbc.M111228200. PMID 11821406.