Ignet

Gene Information

Gene symbol: CLDN7

Gene name: claudin 7

HGNC ID: 2049

Synonyms: Hs.84359

Related Genes

#	Gene Symbol	Number of hits
1	ACTN4	1 hits
2	CCL2	1 hits
3	CD44	1 hits
4	CLDN1	1 hits
5	CLDN2	1 hits
6	CORO1A	1 hits
7	ELAVL1	1 hits
8	HES1	1 hits
9	IL17A	1 hits
10	JAG1	1 hits
11	MKI67	1 hits
12	MMP9	1 hits
13	NES	1 hits
14	NOTCH1	1 hits
15	NPHS1	1 hits
16	NPHS2	1 hits
17	OCLN	1 hits
18	PAX2	1 hits
19	PAX8	1 hits
20	SIRT1	1 hits
21	SYNPO	1 hits
22	TJP1	1 hits
23	WT1	1 hits

Related Sentences

#	PMID	Sentence
1	18596122	One clone, designated mouse PEC (mPEC), was extensively characterized. mPEC exhibited a compact cell body with typical epithelial morphology when grown in permissive conditions, but the cell shape changed to polygonal after 14 d in growth-restrictive conditions. mPEC but not podocytes used as a negative control expressed claudin-1, claudin-2, and protein gene product 9.5, which are proteins specific to PEC in vivo, and did not express the podocyte-specific proteins synaptopodin and nephrin.
2	18596122	The junctional proteins zonula occludens-1 and beta-catenin stained positively in both mPEC and podocytes, but the staining pattern at cell-cell contacts was intermittent in mPEC and linear in podocytes.
3	19794110	The TJ proteins claudin-1, zonula occludens-1, and occludin stained positive in PECs; however, staining decreased in anti-GBM disease.
4	20007346	Double immunostaining was performed with antibodies to podocyte-specific proteins (synaptopodin and Wilms' tumor 1) and antibodies to PEC specific proteins (paired box gene 8 and claudin-1).
5	22129965	Single and double immunostaining were performed with antibodies to the PEC protein paired box gene 2 (PAX2) and tight junction protein claudin-1, the podocyte-specific protein Wilms' tumor 1 (WT-1), and the proliferating cell protein (Ki-67).
6	22129965	The increase in PEC number was due to proliferation (increase in PAX2/Ki-67 double-positive cells).
7	22129965	Aging was accompanied by a progressive increase in the number of glomerular cells double staining for PAX2 and WT-1.
8	23447065	Hyperplastic epithelium was negative for genetic podocyte tags, but positive for the parietal epithelial cell marker claudin-1, and expressed Notch1, Jagged1, and Hes1 mRNA and protein.
9	23447065	Enhanced Notch mRNA expression induced by transforming growth factor-β1 in cultured parietal epithelial cells was associated with mesenchymal markers (α-smooth muscle actin, vimentin, and Snail1).
10	23769837	A subset of cells lining Bowman's capsule activated expression of the glomerular parietal epithelial cell markers paired box protein PAX2 and claudin-1.
11	23769837	A subset of labeled cells within the glomerular tuft expressed the podocyte markers Wilms tumor protein 1, nephrin, podocin, and synaptopodin.
12	24154691	Using a podocyte-specific injury model of FSGS carrying a genetic podocyte tag combined with double immunostaining by different sets of podocytes and parietal epithelial cell (PEC) markers [nestin/Pax8, Wilms' tumor-1 (WT1)/claudin1, and podocalyxin/Pax2], we investigated the direction of epithelial phenotypic transition and its role in FSGS.
13	24154691	In addition, the average numbers of double-positive cells for X-gal/Pax8, nestin/Pax8 and podocalyxin/Pax2 staining in the FSGS mice were comparable, whereas those of WT1/claudin1 were significantly increased.
14	24154691	Using a podocyte-specific injury model of FSGS carrying a genetic podocyte tag combined with double immunostaining by different sets of podocytes and parietal epithelial cell (PEC) markers [nestin/Pax8, Wilms' tumor-1 (WT1)/claudin1, and podocalyxin/Pax2], we investigated the direction of epithelial phenotypic transition and its role in FSGS.
15	24154691	In addition, the average numbers of double-positive cells for X-gal/Pax8, nestin/Pax8 and podocalyxin/Pax2 staining in the FSGS mice were comparable, whereas those of WT1/claudin1 were significantly increased.
16	24856573	Some glomeruli were accompanied by sclerotic lesions surrounded by proliferating cells; immunofluorescence staining revealed a majority of these proliferating cells to be positive for claudin-1 (a parietal cell marker) but negative for synaptopodin.
17	24868462	Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis.
18	24868462	Some animal studies demonstrated that parietal epithelial cells of Bowman's capsule (PECs) were the main component of proliferating cells and PEC-specific tight junction protein claudin-1 was expressed in crescentic lesions.
19	24868462	We investigated the expression of claudin-1 in human GN.
20	24868462	Immunohistochemistry for claudin-1 was performed on 17 kidney biopsy samples with crescent formation.
21	24868462	Colocalization of claudin-1 with intracellular tight junction protein ZO-1 was also evaluated by immunofluorescence double staining.
22	24868462	Small numbers of crescent forming cells showed extrajunctional localization of claudin-1.
23	24868462	Colocalization of claudin-1 with ZO-1 was found at cell to cell contact sites of adjacent proliferating cells.
24	24868462	In control samples, staining of claudin-1 was positive in PECs, but not in podocytes.
25	24868462	Our findings suggest that claudin-1 contributes to crescent formation as a component of the tight junction protein complex that includes ZO-1.
26	24868462	Co-localization of claudin-1 with ZO-1 implies the formation of functional tight junction complexes in crescentic lesions to prevent the interstitial damage caused by penetration of filtered molecules from Bowman's space.
27	24868462	Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis.
28	24868462	Some animal studies demonstrated that parietal epithelial cells of Bowman's capsule (PECs) were the main component of proliferating cells and PEC-specific tight junction protein claudin-1 was expressed in crescentic lesions.
29	24868462	We investigated the expression of claudin-1 in human GN.
30	24868462	Immunohistochemistry for claudin-1 was performed on 17 kidney biopsy samples with crescent formation.
31	24868462	Colocalization of claudin-1 with intracellular tight junction protein ZO-1 was also evaluated by immunofluorescence double staining.
32	24868462	Small numbers of crescent forming cells showed extrajunctional localization of claudin-1.
33	24868462	Colocalization of claudin-1 with ZO-1 was found at cell to cell contact sites of adjacent proliferating cells.
34	24868462	In control samples, staining of claudin-1 was positive in PECs, but not in podocytes.
35	24868462	Our findings suggest that claudin-1 contributes to crescent formation as a component of the tight junction protein complex that includes ZO-1.
36	24868462	Co-localization of claudin-1 with ZO-1 implies the formation of functional tight junction complexes in crescentic lesions to prevent the interstitial damage caused by penetration of filtered molecules from Bowman's space.
37	24868462	Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis.
38	24868462	Some animal studies demonstrated that parietal epithelial cells of Bowman's capsule (PECs) were the main component of proliferating cells and PEC-specific tight junction protein claudin-1 was expressed in crescentic lesions.
39	24868462	We investigated the expression of claudin-1 in human GN.
40	24868462	Immunohistochemistry for claudin-1 was performed on 17 kidney biopsy samples with crescent formation.
41	24868462	Colocalization of claudin-1 with intracellular tight junction protein ZO-1 was also evaluated by immunofluorescence double staining.
42	24868462	Small numbers of crescent forming cells showed extrajunctional localization of claudin-1.
43	24868462	Colocalization of claudin-1 with ZO-1 was found at cell to cell contact sites of adjacent proliferating cells.
44	24868462	In control samples, staining of claudin-1 was positive in PECs, but not in podocytes.
45	24868462	Our findings suggest that claudin-1 contributes to crescent formation as a component of the tight junction protein complex that includes ZO-1.
46	24868462	Co-localization of claudin-1 with ZO-1 implies the formation of functional tight junction complexes in crescentic lesions to prevent the interstitial damage caused by penetration of filtered molecules from Bowman's space.
47	24868462	Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis.
48	24868462	Some animal studies demonstrated that parietal epithelial cells of Bowman's capsule (PECs) were the main component of proliferating cells and PEC-specific tight junction protein claudin-1 was expressed in crescentic lesions.
49	24868462	We investigated the expression of claudin-1 in human GN.
50	24868462	Immunohistochemistry for claudin-1 was performed on 17 kidney biopsy samples with crescent formation.
51	24868462	Colocalization of claudin-1 with intracellular tight junction protein ZO-1 was also evaluated by immunofluorescence double staining.
52	24868462	Small numbers of crescent forming cells showed extrajunctional localization of claudin-1.
53	24868462	Colocalization of claudin-1 with ZO-1 was found at cell to cell contact sites of adjacent proliferating cells.
54	24868462	In control samples, staining of claudin-1 was positive in PECs, but not in podocytes.
55	24868462	Our findings suggest that claudin-1 contributes to crescent formation as a component of the tight junction protein complex that includes ZO-1.
56	24868462	Co-localization of claudin-1 with ZO-1 implies the formation of functional tight junction complexes in crescentic lesions to prevent the interstitial damage caused by penetration of filtered molecules from Bowman's space.
57	24868462	Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis.
58	24868462	Some animal studies demonstrated that parietal epithelial cells of Bowman's capsule (PECs) were the main component of proliferating cells and PEC-specific tight junction protein claudin-1 was expressed in crescentic lesions.
59	24868462	We investigated the expression of claudin-1 in human GN.
60	24868462	Immunohistochemistry for claudin-1 was performed on 17 kidney biopsy samples with crescent formation.
61	24868462	Colocalization of claudin-1 with intracellular tight junction protein ZO-1 was also evaluated by immunofluorescence double staining.
62	24868462	Small numbers of crescent forming cells showed extrajunctional localization of claudin-1.
63	24868462	Colocalization of claudin-1 with ZO-1 was found at cell to cell contact sites of adjacent proliferating cells.
64	24868462	In control samples, staining of claudin-1 was positive in PECs, but not in podocytes.
65	24868462	Our findings suggest that claudin-1 contributes to crescent formation as a component of the tight junction protein complex that includes ZO-1.
66	24868462	Co-localization of claudin-1 with ZO-1 implies the formation of functional tight junction complexes in crescentic lesions to prevent the interstitial damage caused by penetration of filtered molecules from Bowman's space.
67	24868462	Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis.
68	24868462	Some animal studies demonstrated that parietal epithelial cells of Bowman's capsule (PECs) were the main component of proliferating cells and PEC-specific tight junction protein claudin-1 was expressed in crescentic lesions.
69	24868462	We investigated the expression of claudin-1 in human GN.
70	24868462	Immunohistochemistry for claudin-1 was performed on 17 kidney biopsy samples with crescent formation.
71	24868462	Colocalization of claudin-1 with intracellular tight junction protein ZO-1 was also evaluated by immunofluorescence double staining.
72	24868462	Small numbers of crescent forming cells showed extrajunctional localization of claudin-1.
73	24868462	Colocalization of claudin-1 with ZO-1 was found at cell to cell contact sites of adjacent proliferating cells.
74	24868462	In control samples, staining of claudin-1 was positive in PECs, but not in podocytes.
75	24868462	Our findings suggest that claudin-1 contributes to crescent formation as a component of the tight junction protein complex that includes ZO-1.
76	24868462	Co-localization of claudin-1 with ZO-1 implies the formation of functional tight junction complexes in crescentic lesions to prevent the interstitial damage caused by penetration of filtered molecules from Bowman's space.
77	24868462	Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis.
78	24868462	Some animal studies demonstrated that parietal epithelial cells of Bowman's capsule (PECs) were the main component of proliferating cells and PEC-specific tight junction protein claudin-1 was expressed in crescentic lesions.
79	24868462	We investigated the expression of claudin-1 in human GN.
80	24868462	Immunohistochemistry for claudin-1 was performed on 17 kidney biopsy samples with crescent formation.
81	24868462	Colocalization of claudin-1 with intracellular tight junction protein ZO-1 was also evaluated by immunofluorescence double staining.
82	24868462	Small numbers of crescent forming cells showed extrajunctional localization of claudin-1.
83	24868462	Colocalization of claudin-1 with ZO-1 was found at cell to cell contact sites of adjacent proliferating cells.
84	24868462	In control samples, staining of claudin-1 was positive in PECs, but not in podocytes.
85	24868462	Our findings suggest that claudin-1 contributes to crescent formation as a component of the tight junction protein complex that includes ZO-1.
86	24868462	Co-localization of claudin-1 with ZO-1 implies the formation of functional tight junction complexes in crescentic lesions to prevent the interstitial damage caused by penetration of filtered molecules from Bowman's space.
87	24868462	Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis.
88	24868462	Some animal studies demonstrated that parietal epithelial cells of Bowman's capsule (PECs) were the main component of proliferating cells and PEC-specific tight junction protein claudin-1 was expressed in crescentic lesions.
89	24868462	We investigated the expression of claudin-1 in human GN.
90	24868462	Immunohistochemistry for claudin-1 was performed on 17 kidney biopsy samples with crescent formation.
91	24868462	Colocalization of claudin-1 with intracellular tight junction protein ZO-1 was also evaluated by immunofluorescence double staining.
92	24868462	Small numbers of crescent forming cells showed extrajunctional localization of claudin-1.
93	24868462	Colocalization of claudin-1 with ZO-1 was found at cell to cell contact sites of adjacent proliferating cells.
94	24868462	In control samples, staining of claudin-1 was positive in PECs, but not in podocytes.
95	24868462	Our findings suggest that claudin-1 contributes to crescent formation as a component of the tight junction protein complex that includes ZO-1.
96	24868462	Co-localization of claudin-1 with ZO-1 implies the formation of functional tight junction complexes in crescentic lesions to prevent the interstitial damage caused by penetration of filtered molecules from Bowman's space.
97	24868462	Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis.
98	24868462	Some animal studies demonstrated that parietal epithelial cells of Bowman's capsule (PECs) were the main component of proliferating cells and PEC-specific tight junction protein claudin-1 was expressed in crescentic lesions.
99	24868462	We investigated the expression of claudin-1 in human GN.
100	24868462	Immunohistochemistry for claudin-1 was performed on 17 kidney biopsy samples with crescent formation.
101	24868462	Colocalization of claudin-1 with intracellular tight junction protein ZO-1 was also evaluated by immunofluorescence double staining.
102	24868462	Small numbers of crescent forming cells showed extrajunctional localization of claudin-1.
103	24868462	Colocalization of claudin-1 with ZO-1 was found at cell to cell contact sites of adjacent proliferating cells.
104	24868462	In control samples, staining of claudin-1 was positive in PECs, but not in podocytes.
105	24868462	Our findings suggest that claudin-1 contributes to crescent formation as a component of the tight junction protein complex that includes ZO-1.
106	24868462	Co-localization of claudin-1 with ZO-1 implies the formation of functional tight junction complexes in crescentic lesions to prevent the interstitial damage caused by penetration of filtered molecules from Bowman's space.
107	24868462	Expression of tight junction protein claudin-1 in human crescentic glomerulonephritis.
108	24868462	Some animal studies demonstrated that parietal epithelial cells of Bowman's capsule (PECs) were the main component of proliferating cells and PEC-specific tight junction protein claudin-1 was expressed in crescentic lesions.
109	24868462	We investigated the expression of claudin-1 in human GN.
110	24868462	Immunohistochemistry for claudin-1 was performed on 17 kidney biopsy samples with crescent formation.
111	24868462	Colocalization of claudin-1 with intracellular tight junction protein ZO-1 was also evaluated by immunofluorescence double staining.
112	24868462	Small numbers of crescent forming cells showed extrajunctional localization of claudin-1.
113	24868462	Colocalization of claudin-1 with ZO-1 was found at cell to cell contact sites of adjacent proliferating cells.
114	24868462	In control samples, staining of claudin-1 was positive in PECs, but not in podocytes.
115	24868462	Our findings suggest that claudin-1 contributes to crescent formation as a component of the tight junction protein complex that includes ZO-1.
116	24868462	Co-localization of claudin-1 with ZO-1 implies the formation of functional tight junction complexes in crescentic lesions to prevent the interstitial damage caused by penetration of filtered molecules from Bowman's space.
117	25307344	Ninety-five renal biopsies were stained for claudin-1 (PEC marker), CD44 (activated PECs), and LKIV69 (PEC matrix); 38 had been diagnosed as early primary FSGS and 57 as minimal change disease.
118	25307344	Two novel PEC markers A-kinase anchor protein 12 and annexin A3 exhibited similar sensitivity.
119	25849723	Matrix metalloproteinase-9 expression is enhanced in renal parietal epithelial cells of zucker diabetic Fatty rats and is induced by albumin in in vitro primary parietal cell culture.
120	25849723	As a subfamily of matrix metalloproteinases (MMPs), gelatinases including MMP-2 and MMP-9 play an important role in remodeling and homeostasis of the extracellular matrix.
121	25849723	This study investigated whether and how MMP-9 expression and activity were changed in glomerular epithelial cells upon albumin overload.
122	25849723	Increased glomerular MMP-9 staining was mainly observed in hyperplastic parietal epithelial cells (PECs) expressing claudin-1 in the diabetic kidneys.
123	25849723	Interestingly, increased parietal MMP-9 was often accompanied by decreased staining for podocyte markers (nephrin and podocalyxin) in the sclerotic area of affected glomeruli in diabetic rats.
124	25849723	Additionally, urinary excretion of podocyte marker proteins was significantly increased in association with the levels of MMP-9 and albumin in the urine of diabetic animals.
125	25849723	To evaluate the direct effect of albumin on expression and activity of MMP-9, primary cultured rat glomerular PECs were incubated with rat serum albumin (0.25 - 1 mg/ml) for 24 - 48 hrs.
126	25849723	MMP-9 mRNA levels were significantly increased following albumin treatment.
127	25849723	Meanwhile, albumin administration resulted in a dose-dependent increase in MMP-9 protein and activity in culture supernatants of PECs.
128	25849723	Moreover, albumin activated p44/42 mitogen-activated protein kinase (MAPK) in PECs.
129	25849723	Inhibition of p44/42 MAPK suppressed albumin-induced MMP-9 secretion from glomerular PECs.
130	25849723	Albumin overload may induce MMP-9 expression and secretion by PECs via the activation of p44/42 MAPK pathway.
131	26083654	This further decreases expression of Sirt1 in glomerular podocytes and increases expression of a tight junction protein, claudin-1, which results in albuminuria.
132	26376129	Markers of podocytes (WT-1, p57), parietal epithelial cells (PECs) (claudin-1), and cell proliferation (Ki-67) were identified by immunohistochemistry.
133	27076646	On FSGS day 7, immunostaining for the podocyte markers p57, synaptopodin, and podocin were markedly decreased by 44%, and this was accompanied by a decrease in ZsGreen fluorescence.
134	27076646	Staining for p57, synaptopodin, podocin, and DAPI increased at FSGS day 28 and was augmented by the ACE inhibitor enalapril, which is consistent with a partial replenishment of podocytes.
135	27076646	Moreover, more than half of the migrated podocytes coexpressed the parietal epithelial cell (PEC) proteins claudin-1, SSeCKS, and PAX8.
136	27151920	In diabetic nephropathy, the gene expression of claudins, in particular claudin-1, is markedly upregulated in the podocyte, accompanied by a tighter filtration slit and the appearance of TJ-like structures between the foot processes.
137	27151920	However, there is no definitive evidence to show slit diaphragm (SD) to TJ transition in vivo Here, we report the generation of a claudin-1 transgenic mouse model with doxycycline-inducible transgene expression specifically in the glomerular podocyte.
138	27151920	We found that induction of claudin-1 gene expression in mature podocytes caused profound proteinuria, and with deep-etching freeze-fracture electron microscopy, we resolved the ultrastructural change in the claudin-1-induced SD-TJ transition.
139	27151920	Notably, immunolabeling of kidney proteins revealed that claudin-1 induction destabilized the SD protein complex in podocytes, with significantly reduced expression and altered localization of nephrin and podocin proteins.
140	27151920	Mechanistically, claudin-1 interacted with both nephrin and podocin through cis- and trans-associations in cultured cells.
141	27151920	Furthermore, the rat puromycin aminonucleoside nephrosis model, previously suspected of undergoing SD-TJ transition, exhibited upregulated expression levels of claudin-1 mRNA and protein in podocytes.
142	27151920	In diabetic nephropathy, the gene expression of claudins, in particular claudin-1, is markedly upregulated in the podocyte, accompanied by a tighter filtration slit and the appearance of TJ-like structures between the foot processes.
143	27151920	However, there is no definitive evidence to show slit diaphragm (SD) to TJ transition in vivo Here, we report the generation of a claudin-1 transgenic mouse model with doxycycline-inducible transgene expression specifically in the glomerular podocyte.
144	27151920	We found that induction of claudin-1 gene expression in mature podocytes caused profound proteinuria, and with deep-etching freeze-fracture electron microscopy, we resolved the ultrastructural change in the claudin-1-induced SD-TJ transition.
145	27151920	Notably, immunolabeling of kidney proteins revealed that claudin-1 induction destabilized the SD protein complex in podocytes, with significantly reduced expression and altered localization of nephrin and podocin proteins.
146	27151920	Mechanistically, claudin-1 interacted with both nephrin and podocin through cis- and trans-associations in cultured cells.
147	27151920	Furthermore, the rat puromycin aminonucleoside nephrosis model, previously suspected of undergoing SD-TJ transition, exhibited upregulated expression levels of claudin-1 mRNA and protein in podocytes.
148	27151920	In diabetic nephropathy, the gene expression of claudins, in particular claudin-1, is markedly upregulated in the podocyte, accompanied by a tighter filtration slit and the appearance of TJ-like structures between the foot processes.
149	27151920	However, there is no definitive evidence to show slit diaphragm (SD) to TJ transition in vivo Here, we report the generation of a claudin-1 transgenic mouse model with doxycycline-inducible transgene expression specifically in the glomerular podocyte.
150	27151920	We found that induction of claudin-1 gene expression in mature podocytes caused profound proteinuria, and with deep-etching freeze-fracture electron microscopy, we resolved the ultrastructural change in the claudin-1-induced SD-TJ transition.
151	27151920	Notably, immunolabeling of kidney proteins revealed that claudin-1 induction destabilized the SD protein complex in podocytes, with significantly reduced expression and altered localization of nephrin and podocin proteins.
152	27151920	Mechanistically, claudin-1 interacted with both nephrin and podocin through cis- and trans-associations in cultured cells.
153	27151920	Furthermore, the rat puromycin aminonucleoside nephrosis model, previously suspected of undergoing SD-TJ transition, exhibited upregulated expression levels of claudin-1 mRNA and protein in podocytes.
154	27151920	In diabetic nephropathy, the gene expression of claudins, in particular claudin-1, is markedly upregulated in the podocyte, accompanied by a tighter filtration slit and the appearance of TJ-like structures between the foot processes.
155	27151920	However, there is no definitive evidence to show slit diaphragm (SD) to TJ transition in vivo Here, we report the generation of a claudin-1 transgenic mouse model with doxycycline-inducible transgene expression specifically in the glomerular podocyte.
156	27151920	We found that induction of claudin-1 gene expression in mature podocytes caused profound proteinuria, and with deep-etching freeze-fracture electron microscopy, we resolved the ultrastructural change in the claudin-1-induced SD-TJ transition.
157	27151920	Notably, immunolabeling of kidney proteins revealed that claudin-1 induction destabilized the SD protein complex in podocytes, with significantly reduced expression and altered localization of nephrin and podocin proteins.
158	27151920	Mechanistically, claudin-1 interacted with both nephrin and podocin through cis- and trans-associations in cultured cells.
159	27151920	Furthermore, the rat puromycin aminonucleoside nephrosis model, previously suspected of undergoing SD-TJ transition, exhibited upregulated expression levels of claudin-1 mRNA and protein in podocytes.
160	27151920	In diabetic nephropathy, the gene expression of claudins, in particular claudin-1, is markedly upregulated in the podocyte, accompanied by a tighter filtration slit and the appearance of TJ-like structures between the foot processes.
161	27151920	However, there is no definitive evidence to show slit diaphragm (SD) to TJ transition in vivo Here, we report the generation of a claudin-1 transgenic mouse model with doxycycline-inducible transgene expression specifically in the glomerular podocyte.
162	27151920	We found that induction of claudin-1 gene expression in mature podocytes caused profound proteinuria, and with deep-etching freeze-fracture electron microscopy, we resolved the ultrastructural change in the claudin-1-induced SD-TJ transition.
163	27151920	Notably, immunolabeling of kidney proteins revealed that claudin-1 induction destabilized the SD protein complex in podocytes, with significantly reduced expression and altered localization of nephrin and podocin proteins.
164	27151920	Mechanistically, claudin-1 interacted with both nephrin and podocin through cis- and trans-associations in cultured cells.
165	27151920	Furthermore, the rat puromycin aminonucleoside nephrosis model, previously suspected of undergoing SD-TJ transition, exhibited upregulated expression levels of claudin-1 mRNA and protein in podocytes.
166	27151920	In diabetic nephropathy, the gene expression of claudins, in particular claudin-1, is markedly upregulated in the podocyte, accompanied by a tighter filtration slit and the appearance of TJ-like structures between the foot processes.
167	27151920	However, there is no definitive evidence to show slit diaphragm (SD) to TJ transition in vivo Here, we report the generation of a claudin-1 transgenic mouse model with doxycycline-inducible transgene expression specifically in the glomerular podocyte.
168	27151920	We found that induction of claudin-1 gene expression in mature podocytes caused profound proteinuria, and with deep-etching freeze-fracture electron microscopy, we resolved the ultrastructural change in the claudin-1-induced SD-TJ transition.
169	27151920	Notably, immunolabeling of kidney proteins revealed that claudin-1 induction destabilized the SD protein complex in podocytes, with significantly reduced expression and altered localization of nephrin and podocin proteins.
170	27151920	Mechanistically, claudin-1 interacted with both nephrin and podocin through cis- and trans-associations in cultured cells.
171	27151920	Furthermore, the rat puromycin aminonucleoside nephrosis model, previously suspected of undergoing SD-TJ transition, exhibited upregulated expression levels of claudin-1 mRNA and protein in podocytes.
172	27878608	In the glomerular podocytes, claudin-1 is an important determinant of cell junction fate.
173	27878608	More importantly, claudin-14 gene expression can be regulated by extracellular calcium levels via the calcium sensing receptor.
174	27878608	Aldosterone, WNK4, Cap1, and KLHL3 are powerful regulators of claudin and the paracellular chloride permeability.
175	28329012	Four CoRL reporters (GFP, YFP, RFP, CFP) were restricted to cells in the juxtaglomerular compartment (JGC) at baseline.
176	28329012	Following abrupt podocyte depletion in experimental FSGS, all four CoRL reporters were detected in a subset of glomeruli at day 28, where they co-expressed de novo four podocyte proteins (podocin, nephrin, WT-1 and p57) and two glomerular parietal epithelial cell (PEC) proteins (claudin-1, PAX8).
177	32487989	RNA-binding proteins (RBPs) play a pivotal role in epigenetic regulation; tristetraprolin (TTP) and human antigen R (HuR) competitively bind cytokine mRNAs, exert contrasting effects on RNA stability, and drive inflammation.
178	32487989	In DKD patients and db/db mice, TTP expression was significantly decreased and HuR expression was increased in glomerular podocytes, concurrent with podocyte injury, histological signs of DKD, and augmented glomerular expression of interleukin (IL)-17 and claudin-1, which are targets of TTP and HuR, as evidenced by RNA immunoprecipitation.
179	32487989	In cultured podocytes, exposure to high ambient glucose amplified HuR expression and repressed TTP expression, upregulated IL-17 and claudin-1, and promoted podocyte injury.
180	32487989	Treatment of db/db mice with a small molecule inhibitor of GSK-3β abrogated the changes in TTP and HuR in glomeruli and mitigated the overexpression of their target genes (IL-17, claudin-1, B7-1, and MCP-1) thus also mitigating proteinuria and DKD pathology.
181	32487989	RNA-binding proteins (RBPs) play a pivotal role in epigenetic regulation; tristetraprolin (TTP) and human antigen R (HuR) competitively bind cytokine mRNAs, exert contrasting effects on RNA stability, and drive inflammation.
182	32487989	In DKD patients and db/db mice, TTP expression was significantly decreased and HuR expression was increased in glomerular podocytes, concurrent with podocyte injury, histological signs of DKD, and augmented glomerular expression of interleukin (IL)-17 and claudin-1, which are targets of TTP and HuR, as evidenced by RNA immunoprecipitation.
183	32487989	In cultured podocytes, exposure to high ambient glucose amplified HuR expression and repressed TTP expression, upregulated IL-17 and claudin-1, and promoted podocyte injury.
184	32487989	Treatment of db/db mice with a small molecule inhibitor of GSK-3β abrogated the changes in TTP and HuR in glomeruli and mitigated the overexpression of their target genes (IL-17, claudin-1, B7-1, and MCP-1) thus also mitigating proteinuria and DKD pathology.
185	32487989	RNA-binding proteins (RBPs) play a pivotal role in epigenetic regulation; tristetraprolin (TTP) and human antigen R (HuR) competitively bind cytokine mRNAs, exert contrasting effects on RNA stability, and drive inflammation.
186	32487989	In DKD patients and db/db mice, TTP expression was significantly decreased and HuR expression was increased in glomerular podocytes, concurrent with podocyte injury, histological signs of DKD, and augmented glomerular expression of interleukin (IL)-17 and claudin-1, which are targets of TTP and HuR, as evidenced by RNA immunoprecipitation.
187	32487989	In cultured podocytes, exposure to high ambient glucose amplified HuR expression and repressed TTP expression, upregulated IL-17 and claudin-1, and promoted podocyte injury.
188	32487989	Treatment of db/db mice with a small molecule inhibitor of GSK-3β abrogated the changes in TTP and HuR in glomeruli and mitigated the overexpression of their target genes (IL-17, claudin-1, B7-1, and MCP-1) thus also mitigating proteinuria and DKD pathology.
189	34411489	miR-193a as a potential mediator of WT-1/synaptopodin in the renoprotective effect of Losartan on diabetic kidney.
190	34411489	Next, immunohistochemistry and immunofluorescence were used to detect Wilms tumor protein 1 (WT-1) and synaptopodin expression, respectively.
191	34411489	Protein levels of WT-1, synaptopodin, claudin1, and Pax-2 were assessed by Western blotting and real-time PCR.
192	34411489	In addition, Losartan significantly upregulated the immunopositive cell numbers of WT-1, the expression of WT-1 and synaptopodin in renal tissue.
193	34411489	By contrast, expression of claudin1 and Pax-2 in renal tissue were decreased in db/db-losartan group.
194	34411489	miR-193a as a potential mediator of WT-1/synaptopodin in the renoprotective effect of Losartan on diabetic kidney.
195	34411489	Next, immunohistochemistry and immunofluorescence were used to detect Wilms tumor protein 1 (WT-1) and synaptopodin expression, respectively.
196	34411489	Protein levels of WT-1, synaptopodin, claudin1, and Pax-2 were assessed by Western blotting and real-time PCR.
197	34411489	In addition, Losartan significantly upregulated the immunopositive cell numbers of WT-1, the expression of WT-1 and synaptopodin in renal tissue.
198	34411489	By contrast, expression of claudin1 and Pax-2 in renal tissue were decreased in db/db-losartan group.