LAMC2 Antibody

Background:

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 processesincluding cell adhesion, differentiation, migration, signaling,neurite outgrowth and metastasis. Laminins are composed of 3 nonidentical chains: laminin alpha, beta and gamma (formerly A, B1,and B2, respectively) and they form a cruciform structureconsisting of 3 short arms, each formed by a different chain, and along arm composed of all 3 chains. Each laminin chain is amultidomain protein encoded by a distinct gene. Several isoformsof each chain have been described. Different alpha, beta and gammachain isomers combine to give rise to different heterotrimericlaminin isoforms which are designated by Arabic numerals in theorder of their discovery, i.e. alpha1beta1gamma1 heterotrimer islaminin 1. The biological functions of the different chains andtrimer molecules are largely unknown, but some of the chains havebeen shown to differ with respect to their tissue distribution,presumably reflecting diverse functions in vivo. This gene encodesthe gamma chain isoform laminin, gamma 2. The gamma 2 chain,formerly thought to be a truncated version of beta chain (B2t), ishighly homologous to the gamma 1 chain; however, it lacks domainVI, and domains V, IV and III are shorter. It is expressed inseveral fetal tissues but differently from gamma 1, and isspecifically localized to epithelial cells in skin, lung andkidney. The gamma 2 chain together with alpha 3 and beta 3 chainsconstitute laminin 5 (earlier known as kalinin), which is anintegral part of the anchoring filaments that connect epithelialcells to the underlying basement membrane. The epithelium-specificexpression of the gamma 2 chain implied its role as an epitheliumattachment molecule, and mutations in this gene have beenassociated with junctional epidermolysis bullosa, a skin diseasecharacterized by blisters due to disruption of the epidermal-dermaljunction. Two transcript variants resulting from alternativesplicing of the 3' terminal exon, and encoding different isoformsof gamma 2 chain, have been described. The two variants aredifferentially expressed in embryonic tissues, however, thebiological significance of the two forms is not known. Transcriptvariants utilizing alternative polyA_signal have also been noted inliterature.