Laminin, alpha 3

Laminin, alpha 3
Identifiers
Symbols	LAMA3 ; E170; LAMNA; LOCS; lama3a
External IDs	Template:OMIM5 Template:MGI HomoloGene: 18279
Gene ontology Molecular function Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE LAMA3 203726 s at tn.png
File:PBB GE LAMA3 gnf1h02350 at tn.png
File:PBB GE LAMA3 gnf1h02351 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Laminin, alpha 3, also known as LAMA3, is a human gene.

Laminins are basement membrane components thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. The protein encoded by this gene is the alpha-3 chain of laminin 5, which is a complex glycoprotein composed of three subunits (alpha, beta, and gamma). Laminin 5 is thought to be involved in cell adhesion, signal transduction and differentiation of keratinocytes. Mutations in this gene have been identified as the cause of Herlitz type junctional epidermolysis bullosa. Alternatively spliced transcript variants encoding different isoforms have been identified.

Further reading

• Timpl R (1997). "Macromolecular organization of basement membranes". Curr. Opin. Cell Biol. 8 (5): 618–24. PMID 8939648.
• Kivirikko S, McGrath JA, Baudoin C; et al. (1995). "A homozygous nonsense mutation in the alpha 3 chain gene of laminin 5 (LAMA3) in lethal (Herlitz) junctional epidermolysis bullosa". Hum. Mol. Genet. 4 (5): 959–62. PMID 7633458.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Rousselle P, Golbik R, van der Rest M, Aumailley M (1995). "Structural requirement for cell adhesion to kalinin (laminin-5)". J. Biol. Chem. 270 (23): 13766–70. PMID 7775432.CS1 maint: Multiple names: authors list (link)
• Burgeson RE, Chiquet M, Deutzmann R; et al. (1994). "A new nomenclature for the laminins". Matrix Biol. 14 (3): 209–11. PMID 7921537.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• Vidal F, Baudoin C, Miquel C; et al. (1996). "Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with Herlitz junctional epidermolysis bullosa". Genomics. 30 (2): 273–80. doi:10.1006/geno.1995.9877. PMID 8586427.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• McGrath JA, Kivirikko S, Ciatti S; et al. (1996). "A recurrent homozygous nonsense mutation within the LAMA3 gene as a cause of Herlitz junctional epidermolysis bullosa in patients of Pakistani ancestry: evidence for a founder effect". J. Invest. Dermatol. 106 (4): 781–4. PMID 8618022.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mizushima H, Miyagi Y, Kikkawa Y; et al. (1997). "Differential expression of laminin-5/ladsin subunits in human tissues and cancer cell lines and their induction by tumor promoter and growth factors". J. Biochem. 120 (6): 1196–202. PMID 9010770.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Miner JH, Patton BL, Lentz SI; et al. (1997). "The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform". J. Cell Biol. 137 (3): 685–701. PMID 9151674.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Doliana R, Bellina I, Bucciotti F; et al. (1998). "The human alpha3b is a 'full-sized' laminin chain variant with a more widespread tissue expression than the truncated alpha3a". FEBS Lett. 417 (1): 65–70. PMID 9395076.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• Pulkkinen L, Cserhalmi-Friedman PB, Tang M; et al. (1998). "Molecular analysis of the human laminin alpha3a chain gene (LAMA3a): a strategy for mutation identification and DNA-based prenatal diagnosis in Herlitz junctional epidermolysis bullosa". Lab. Invest. 78 (9): 1067–76. PMID 9759651.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gonzales M, Haan K, Baker SE; et al. (1999). "A cell signal pathway involving laminin-5, alpha3beta1 integrin, and mitogen-activated protein kinase can regulate epithelial cell proliferation". Mol. Biol. Cell. 10 (2): 259–70. PMID 9950675.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hirosaki T, Mizushima H, Tsubota Y; et al. (2000). "Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5". J. Biol. Chem. 275 (29): 22495–502. doi:10.1074/jbc.M001326200. PMID 10801807.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Amano S, Scott IC, Takahara K; et al. (2000). "Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain". J. Biol. Chem. 275 (30): 22728–35. doi:10.1074/jbc.M002345200. PMID 10806203.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Goldfinger LE, Jiang L, Hopkinson SB; et al. (2001). "Spatial regulation and activity modulation of plasmin by high affinity binding to the G domain of the alpha 3 subunit of laminin-5". J. Biol. Chem. 275 (45): 34887–93. doi:10.1074/jbc.M006652200. PMID 10956663.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fujiwara H, Kikkawa Y, Sanzen N, Sekiguchi K (2001). "Purification and characterization of human laminin-8. Laminin-8 stimulates cell adhesion and migration through alpha3beta1 and alpha6beta1 integrins". J. Biol. Chem. 276 (20): 17550–8. doi:10.1074/jbc.M010155200. PMID 11278628.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• Utani A, Nomizu M, Matsuura H; et al. (2001). "A unique sequence of the laminin alpha 3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4". J. Biol. Chem. 276 (31): 28779–88. doi:10.1074/jbc.M101420200. PMID 11373281.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)