Claudin 3, also known as CLDN3, is a protein which in humans is encoded by the CLDN3gene.[1] It is a member of the claudin protein family.
Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. These junctions are composed of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet, with complementary grooves in the inwardly facing extracytoplasmic leaflet. The protein encoded by this intron-less gene, a member of the claudin family, is an integral membrane protein and a component of tight junction strands. It is also a low-affinity receptor for Clostridium perfringens enterotoxin, and shares amino acid sequence similarity with a putative apoptosis-related protein found in rat.[1]
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Katahira J, Sugiyama H, Inoue N, Horiguchi Y, Matsuda M, Sugimoto N (1997). "Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo". J. Biol. Chem. 272 (42): 26652–8. doi:10.1074/jbc.272.42.26652. PMID9334247.
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Miyamori H, Takino T, Kobayashi Y, Tokai H, Itoh Y, Seiki M, Sato H (2001). "Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases". J. Biol. Chem. 276 (30): 28204–11. doi:10.1074/jbc.M103083200. PMID11382769.
Long H, Crean CD, Lee WH, Cummings OW, Gabig TG (2001). "Expression of Clostridium perfringens enterotoxin receptors claudin-3 and claudin-4 in prostate cancer epithelium". Cancer Res. 61 (21): 7878–81. PMID11691807.
Katoh M, Katoh M (2003). "CLDN23 gene, frequently down-regulated in intestinal-type gastric cancer, is a novel member of CLAUDIN gene family". Int. J. Mol. Med. 11 (6): 683–9. doi:10.3892/ijmm.11.6.683. PMID12736707.