laminin subunit beta 3
Last updated 3 Apr 2025
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The LAMB3 gene provides instructions for making one part (subunit) of a protein called laminin 332 (formerly known as laminin 5). This protein is made up of three subunits, called alpha, beta, and gamma. The LAMB3 gene carries instructions for the beta subunit; the alpha and gamma subunits are produced from other genes.
Normal function
The LAMB3 gene provides instructions for making one part (subunit) of a protein called laminin 332 (formerly known as laminin 5). This protein is made up of three subunits, called alpha, beta, and gamma. The LAMB3 gene carries instructions for the beta subunit; the alpha and gamma subunits are produced from other genes.
Laminins are a group of proteins that regulate cell growth, cell movement (motility), and the attachment of cells to one another (adhesion). They are also involved in the formation and organisation of basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. Laminin 332 has a particularly important role in the basement membrane that underlies the top layer of skin (the epidermis). This membrane gives strength and resiliency to the skin and creates an additional barrier between the body and its surrounding environment. Laminin 332 is a major component of fibers called anchoring filaments, which connect the two layers of the basement membrane and help hold the skin together.
Studies suggest that laminin 332 also has several other functions. This protein appears to be important for wound healing. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel.
Conditions referring to this gene or chromosome
Other names
BM600-125KDA
FLJ99565
kalinin B1 chain
kalinin-140kDa
LAM5, beta-3 subunit
LAMB3_HUMAN
laminin 5, beta-3 subunit
laminin B1k chain
laminin B3
laminin S B3 chain
laminin, beta 3
laminin, beta 3 precursor
laminin, beta-3
LAMNB1
nicein-125kDa
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Further reading and references
- laminin subunit beta 3; MedlinePlus, National Library of Medicine.
- Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, Engel J, Engvall E, Hohenester E, Jones JC, Kleinman HK, Marinkovich MP, Martin GR, Mayer U, Meneguzzi G, Miner JH, Miyazaki K, Patarroyo M, Paulsson M, Quaranta V, Sanes JR, Sasaki T, Sekiguchi K, Sorokin LM, Talts JF, Tryggvason K, Uitto J, Virtanen I, von der Mark K, Wewer UM, Yamada Y, Yurchenco PD. A simplified laminin nomenclature. Matrix Biol. 2005 Aug;24(5):326-32. doi: 10.1016/j.matbio.2005.05.006.
- Hartwig B, Borm B, Schneider H, Arin MJ, Kirfel G, Herzog V. Laminin-5-deficient human keratinocytes: defective adhesion results in a saltatory and inefficient mode of migration. Exp Cell Res. 2007 May 1;313(8):1575-87. doi: 10.1016/j.yexcr.2007.02.003. Epub 2007 Feb 9.
- Muhle C, Jiang QJ, Charlesworth A, Bruckner-Tuderman L, Meneguzzi G, Schneider H. Novel and recurrent mutations in the laminin-5 genes causing lethal junctional epidermolysis bullosa: molecular basis and clinical course of Herlitz disease. Hum Genet. 2005 Jan;116(1-2):33-42. doi: 10.1007/s00439-004-1210-y. Epub 2004 Nov 5.
- Nakano A, Chao SC, Pulkkinen L, Murrell D, Bruckner-Tuderman L, Pfendner E, Uitto J. Laminin 5 mutations in junctional epidermolysis bullosa: molecular basis of Herlitz vs. non-Herlitz phenotypes. Hum Genet. 2002 Jan;110(1):41-51. doi: 10.1007/s00439-001-0630-1. Epub 2001 Nov 13.
- Nakano A, Pfendner E, Hashimoto I, Uitto J. Herlitz junctional epidermolysis bullosa: novel and recurrent mutations in the LAMB3 gene and the population carrier frequency. J Invest Dermatol. 2000 Sep;115(3):493-8. doi: 10.1046/j.1523-1747.2000.00086.x.
- Pulkkinen L, Gerecke DR, Christiano AM, Wagman DW, Burgeson RE, Uitto J. Cloning of the beta 3 chain gene (LAMB3) of human laminin 5, a candidate gene in junctional epidermolysis bullosa. Genomics. 1995 Jan 1;25(1):192-8. doi: 10.1016/0888-7543(95)80125-6.
- Pulkkinen L, Uitto J. Mutation analysis and molecular genetics of epidermolysis bullosa. Matrix Biol. 1999 Feb;18(1):29-42. doi: 10.1016/s0945-053x(98)00005-5.
- Schneider H, Muhle C, Pacho F. Biological function of laminin-5 and pathogenic impact of its deficiency. Eur J Cell Biol. 2007 Dec;86(11-12):701-17. doi: 10.1016/j.ejcb.2006.07.004. Epub 2006 Sep 26.
- Varki R, Sadowski S, Pfendner E, Uitto J. Epidermolysis bullosa. I. Molecular genetics of the junctional and hemidesmosomal variants. J Med Genet. 2006 Aug;43(8):641-52. doi: 10.1136/jmg.2005.039685. Epub 2006 Feb 10.
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