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1 involving increased inflammation and loss of claudin-3.
2 udin-19 mRNA was 25 times more abundant than claudin-3.
3 site at amino acid 192 in the C terminus of claudin-3.
4 nd diminished junctional immunoreactivity of claudin-3.
5 d downregulated expression of genes encoding claudin 3, 4, and 7 and the luminal marker, cytokeratin
7 regimen, a novel and tissue-specific role of claudin-3, a tight junction integral protein, in inhibit
10 EB1, S100A8, amyloid beta precursor protein, claudin 3 and cadherin 1 (downregulated in MDA-MB-231) w
11 whereas the expression of 194 genes, such as claudin 3 and cell adhesion molecule 1, is significantly
12 d decreased intestinal barrier marker genes (claudin 3 and claudin 15) expression, and rescued increa
14 junction (TJ) proteins in the ileum revealed claudin 3 and occludin expression to be increased overal
17 presence of the high-affinity CPE receptors claudin-3 and -4 in both organs of rabbits, consistent w
18 present surface or secreted proteins such as claudin-3 and -4, HE4, mucin-1, epithelial cellular adhe
19 ptors on intestinal epithelial cells include claudin-3 and -4, members of a large family of tight jun
20 or role for dynamin-dependent endocytosis of claudin-3 and 4 during nutrient stress in intestinal epi
22 ity association of the PDZ domain of nNOS to claudin-3 and claudin-14, two tight junction tetraspan m
25 nterfering RNA (siRNA)-mediated knockdown of claudin-3 and claudin-4 expression in ovarian cancer cel
27 current ovarian tumors were found to express claudin-3 and claudin-4 genes at significantly higher le
28 profiling, we and others have recently found claudin-3 and claudin-4 genes to be highly expressed in
29 (CNS) revealed low or undetectable levels of claudin-3 and claudin-4 in all regions tested by Western
30 tudy was designed to study the expression of claudin-3 and claudin-4 in human prostate tissue as pote
33 issue Northern blot analysis, mRNAs for both claudin-3 and claudin-4 were expressed at high levels in
39 ession of TJ proteins ZO-1, JAM-2, Occludin, Claudin-3 and Claudin-5, using in vitro cultures of the
40 y we investigated the level of expression of claudin-3 and/or claudin-4 in chemotherapy-naive and che
44 e tight-junction molecules zona occludens-1, claudin 3, and claudin 5 and other pathways critically i
46 pression of TJ proteins, ZO-1, Occludin, and Claudin-3, and exacerbated the bacterial endotoxin lipop
47 blots revealed that expression of Claudin-7, Claudin-3, and Occludin, critical proteins that regulate
49 helial cells, in which zonal occludens-1 and claudin-3, apical tight-junction proteins, are mislocali
53 ts were unexplained by effects on claudin-2, claudin-3, claudin-19, occludin, and ZO-1, but changes i
54 audins expressed by the alveolar epithelium, claudin-3, claudin-4, and claudin-18 are the most promin
55 hrough immunohistochemical analysis of ApoJ, claudin-3, claudin-4, and epithelial cellular adhesion m
56 pression of other tight junctional proteins (claudin-3, claudin-4, claudin-5, occludin, and ZO-1) and
60 , which were heterotypically compatible with claudin-3, did not heterotypically bind to claudin-4.
61 tercellular junctional proteins (e.g., ZO-1, claudin-3, E-cadherin) and the subapical cytoskeletal/mi
65 e findings however contrasted an upregulated claudin-3 expression in other cancer types and implicate
68 tes that introduction of these residues from claudin-3 into claudin-4 significantly enhances polymeri
69 from periportal to pericentral hepatocytes, claudin 3 is uniformly expressed, claudin 4 is absent, a
70 nstructs demonstrated that the C terminus of claudin-3 is an excellent substrate for cAMP-dependent p
73 c and pharmacological studies confirmed that claudin-3 loss induces Wnt/beta-catenin activation, whic
76 nding normal glandular tissue, expression of claudin-3 mRNA remained high in the epithelium of prosta
78 e blood-testis barrier to biotin, suggesting claudin 3 regulates the movement of small molecules acro
79 ed tight junction proteins (ZO-1, Claudin-1, Claudin-3), RPE disorganization, barrier leakage, and im
80 stinal tight junction proteins, occludin and claudin-3, showed decreases in the distribution of occlu
82 on in the first extracellular loop domain of claudin-3 to convert Asn(44) to the corresponding amino
83 In normal prostate tissue, expression of claudin-3 was localized exclusively within acinar epithe
84 icated by loss of the tight junction protein claudin-3 was not observed during acute infection despit
86 e first EL domain or the second EL domain of claudin-3 were able to heterotypically bind to claudin-1
88 n Sertoli cells, regulates the expression of claudin 3, which encodes a transient component of newly
89 caused a loss of the tight junction protein claudin-3, which was ameliorated by genetic ablation of