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Junctional proteins

Musil LS et al. 1990. Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines. J Cell Biol 111 2077-2088. [Pg.307]

Nakamuta S, Endo H, Higashi Y, Kousaka A, Yamada H, Yano M, Kido H (2008) Human immunodeficiency virus type 1 gpl20-mediated disruption of tight junction proteins by induction of proteasome-mediated degradation of zonula occludens-1 and -2 in human brain microvascular endothelial cells. J Neurovirol 14 186-195... [Pg.247]

HABERMANN H, RAY V, HABERMANN w and PRiNS G s (2001) Alterations in gap junction protein expression in human benign prostatic hyperplasia and prostate cancer. J Urol 166(6) 2267-72. [Pg.125]

Connexin 43 is one of the cell membrane gap junction proteins that allow for cell to cell communication. Cancer cell transformation is correlated with the loss of Connexin 43 expression (Hussain et al. 1989, Zhang et al. 1992). Lycopene increased Connexin 43 expression in fetal skin fibroblasts (Stahl et al. 2000), oral cancer KB-1 cells grown in organotypic rafts (Livny et al. 2003) and breast cancer cell lines (Chalabi et al. 2007). [Pg.453]

Hirakawa, H., Okajima, S., Nagaoka, T., Takamatsu, T. and Oyamada, M. Loss and recovery of the blood-nerve barrier in the rat sciatic nerve after crush injury are associated with expression of intercellular junctional proteins. Exp. Cell Res. 284 196-210,2003. [Pg.626]

Figure 11.2 Morphological differences between human alveolar epithelial cells in primary culture (A and C) and the A549 cell line (B and D). Cells are visualised by light microscopy (A and B) and immunofluorescence microscopy (C and D) using an antibody against a tight junctional protein, occludin. Figure 11.2 Morphological differences between human alveolar epithelial cells in primary culture (A and C) and the A549 cell line (B and D). Cells are visualised by light microscopy (A and B) and immunofluorescence microscopy (C and D) using an antibody against a tight junctional protein, occludin.
Evans SM, Blyth DI, Wong T, Sanjar S, West MR (2002) Decreased distribution of lung epithelial junction proteins after intratracheal antigen or lipopolysaccharide challenge correlation with neutrophil influx and levels of BALF sE-cadherin. Am J Respir Cell Mol Biol 27(4) 446-454... [Pg.277]

Suzuki K, Tanaka T, Enoki M, Nishida T. Coordinated reassembly of the basement membrane and junctional proteins during cornea epithelial wound healing. Invest Ophthalmol Vis Sci 41 2495-2500 (2000). [Pg.301]

Gonzalez-Mariscal L, Betanzos A, Nava P, and Jaramillo BE [2003] Tight junction proteins. Prog Biophys Mol Biol 81 1 14... [Pg.362]

Nusrat A, Brown GT, Tom J, Drake A, Bui TTT, Quan C, and Mrsny RJ [2005] Multiple protein interactions involving proposed extracellular loop domains of the tight junction protein occludin. Mol Biol Cell 16 1725-1734... [Pg.362]

Yoo J, Nichols A, Mammen J, Calvo I, Song JC, Worrell RT, Matlin K, and Matthews JB [2003] Bryostatin-1 enhances barrier function in T84 epithelia through PKC-dependent regulation of tight junction proteins. Am J Physiol 285 C300-C309... [Pg.365]

Freshly isolated or subcultured brain microvascular endothelial cells offer a notable in vitro tool to study drug transport across the blood-brain barrier. Cells can be grown to monolayers on culture plates or permeable membrane supports. The cells retain the major characteristics of brain endothelial cells in vivo, such as the morphology, specific biochemical markers of the blood-brain barrier, and the intercellular tight junctional network. Examples of these markers are y-glutamyl transpeptidase, alkaline phosphatase, von-Willebrandt factor-related antigen, and ZO-1 tight junctional protein. The methods of... [Pg.406]

Paul, A., Cevc, G. and Bachhawat, B. K., Transdermal immunisation with an integral membrane component, gap junction protein, by means of ultradeformable drug carriers, transfersomes. Vaccine, 16, 188-95, 1998. [Pg.16]

Anisotropy and nonuniformity are at least in part due to inhomogeneities in the distribution of gap junctions and the biophysical properties of the tissue are in fact influenced by the intercellular coupling. At least four features have to be considered. (1) Cardiac cells express different gap junction proteins (so-called connexins in the heart, connexin 40, connexin 43 and connexin 45 are most abundantly found for details see chapters 2 and 3). Channels formed by these connexins are different with regard to their biophysical properties. In various parts of the heart the content of each of these isoforms is different. [Pg.6]

Cx43 is the gap junction protein most abundantly found in the hearts of various species including human, dog, chicken and rat. The molecular weight as determined by SDS-PAGE ranges from 42 to 45 kD. Besides in the heart, Cx43 has been found in uterine muscle, granulosa cells, smooth muscle cells, kidney, eye (cornea and lens), epithelium [Beyer et al., 1987,1989 Risek et al.,... [Pg.22]


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