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 gene, a member of the claudin family, is an integral membrane protein and a component of tight junction strands. Loss of function mutations result in neonatal ichthyosis-sclerosing cholangitis syndrome.
Swisshelm K, Machl A, Planitzer S, Robertson R, Kubbies M, Hosier S (1999). "SEMP1, a senescence-associated cDNA isolated from human mammary epithelial cells, is a member of an epithelial membrane protein superfamily". Gene. 226 (2): 285–95. doi:10.1016/S0378-1119(98)00553-8. PMID9931503.
Krämer F, White K, Kubbies M, Swisshelm K, Weber BH (2000). "Genomic organization of claudin-1 and its assessment in hereditary and sporadic breast cancer". Hum. Genet. 107 (3): 249–56. doi:10.1007/s004390000375. PMID11071387.
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.
Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita S (2002). "Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule". J. Biol. Chem. 277 (1): 455–61. doi:10.1074/jbc.M109005200. PMID11689568.