Laminin, alpha 4
| Laminin, alpha 4 | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | LAMA4; LAMA3; LAMA4*-1 | ||||||||||||
| External IDs | OMIM: 600133 MGI: 109321 HomoloGene: 37604 GeneCards: LAMA4 Gene | ||||||||||||
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| Species | Human | Mouse | |||||||||||
| Entrez | 3910 | 16775 | |||||||||||
| Ensembl | ENSG00000112769 | ENSMUSG00000019846 | |||||||||||
| UniProt | Q16363 | P97927 | |||||||||||
| RefSeq (mRNA) | NM_001105206 | NM_010681 | |||||||||||
| RefSeq (protein) | NP_001098676 | NP_034811 | |||||||||||
| Location (UCSC) | Chr 6: 112.43 – 112.58 Mb | Chr 10: 38.97 – 39.11 Mb | |||||||||||
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Laminin subunit alpha-4 is a protein that in humans is encoded by the LAMA4 gene.[1][2]
Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the alpha chain isoform laminin, alpha 4. The domain structure of alpha 4 is similar to that of alpha 3, both of which resemble truncated versions of alpha 1 and alpha 2, in that approximately 1,200 residues at the N-terminus (domains IV, V and VI) have been lost. Laminin, alpha 4 contains the C-terminal G domain which distinguishes all alpha chains from the beta and gamma chains. The RNA analysis from adult and fetal tissues revealed developmental regulation of expression, however, the exact function of laminin, alpha 4 is not known. Tissue-specific utilization of alternative polyA-signal has been described in literature. Also, alternative splicing involving the first intron in the 5' UTR, and laminin alpha 4 like isoforms have been noted, however, the full-length nature of these products is not known.[2]
References
- ↑ Richards AJ, al-Imara L, Carter NP, Lloyd JC, Leversha MA, Pope FM (Dec 1994). "Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a partial cDNA encoding a variant laminin A chain". Genomics 22 (1): 237–9. doi:10.1006/geno.1994.1372. PMID 7959779.
- ↑ 2.0 2.1 "Entrez Gene: LAMA4 laminin, alpha 4".
Further reading
- Ljubimova JY, Fujita M, Khazenzon NM, et al. (2006). "Changes in laminin isoforms associated with brain tumor invasion and angiogenesis.". Front. Biosci. 11 (1): 81–8. doi:10.2741/1781. PMID 16146715.
- Iivanainen A, Sainio K, Sariola H, Tryggvason K (1995). "Primary structure and expression of a novel human laminin alpha 4 chain.". FEBS Lett. 365 (2-3): 183–8. doi:10.1016/0014-5793(95)00462-I. PMID 7781776.
- Burgeson RE, Chiquet M, Deutzmann R, et al. (1994). "A new nomenclature for the laminins.". Matrix Biol. 14 (3): 209–11. doi:10.1016/0945-053X(94)90184-8. PMID 7921537.
- Ryan MC, Tizard R, VanDevanter DR, Carter WG (1994). "Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair.". J. Biol. Chem. 269 (36): 22779–87. PMID 8077230.
- Richards A, Al-Imara L, Pope FM (1996). "The complete cDNA sequence of laminin alpha 4 and its relationship to the other human laminin alpha chains.". Eur. J. Biochem. 238 (3): 813–21. doi:10.1111/j.1432-1033.1996.0813w.x. PMID 8706685.
- Xiao S, Lux ML, Reeves R, et al. (1997). "HMGI(Y) activation by chromosome 6p21 rearrangements in multilineage mesenchymal cells from pulmonary hamartoma.". Am. J. Pathol. 150 (3): 901–10. PMC 1857887. PMID 9060828.
- 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. doi:10.1016/S0014-5793(97)00686-8. PMID 9271224.
- Richards A, Luccarini C, Pope FM (1997). "The structural organisation of LAMA4, the gene encoding laminin alpha4.". Eur. J. Biochem. 248 (1): 15–23. doi:10.1111/j.1432-1033.1997.t01-1-00015.x. PMID 9310354.
- 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.
- Talts JF, Sasaki T, Miosge N, et al. (2001). "Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues.". J. Biol. Chem. 275 (45): 35192–9. doi:10.1074/jbc.M003261200. PMID 10934193.
- Fleischmajer R, Kuroda K, Utani A, et al. (2001). "Differential expression of laminin alpha chains during proliferative and differentiation stages in a model for skin morphogenesis.". Matrix Biol. 19 (7): 637–47. doi:10.1016/S0945-053X(00)00092-5. PMID 11102753.
- 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. doi:10.1016/S0003-9969(01)00014-0. PMID 11311202.
- Petäjäniemi N, Korhonen M, Kortesmaa J, et al. (2002). "Localization of laminin alpha4-chain in developing and adult human tissues.". J. Histochem. Cytochem. 50 (8): 1113–30. PMID 12133914.
- Gu YC, Kortesmaa J, Tryggvason K, et al. (2003). "Laminin isoform-specific promotion of adhesion and migration of human bone marrow progenitor cells.". Blood 101 (3): 877–85. doi:10.1182/blood-2002-03-0796. PMID 12393739.
- Hayashi Y, Kim KH, Fujiwara H, et al. (2003). "Identification and recombinant production of human laminin alpha4 subunit splice variants.". Biochem. Biophys. Res. Commun. 299 (3): 498–504. doi:10.1016/S0006-291X(02)02642-6. PMID 12445830.
- Gonzalez AM, Gonzales M, Herron GS, et al. (2003). "Complex interactions between the laminin alpha 4 subunit and integrins regulate endothelial cell behavior in vitro and angiogenesis in vivo.". Proc. Natl. Acad. Sci. U.S.A. 99 (25): 16075–80. doi:10.1073/pnas.252649399. PMC 138567. PMID 12454288.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
- DeHahn KC, Gonzales M, Gonzalez AM, et al. (2004). "The alpha4 laminin subunit regulates endothelial cell survival.". Exp. Cell Res. 294 (1): 281–9. doi:10.1016/j.yexcr.2003.11.006. PMID 14980521.
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