Cytochemical and cytopathological observations in robins (Turdus migratorius) infected with Leucocytozoon dubreuili

Pathological alterations in hepatocytes and proximal renal tubular cells of the American robin (Turdus migratorius) harbouring schizonts of Leucocytozoon dubreuili consisted primarily of nuclear hypertrophy and the reduction and disruption of cytoplasmic organelles such as endoplasmic reticulum and mitochondria. Other changes included the accumulation of lipofuscin-like bodies and the reduction and disorganization of microvilli.Neither glycogen nor acid or alkaline phosphatase activities were detected in the parasite while these occurred in the parasitized cells and adjacent uninfected cells. The significance of these observations is discussed in relation to studies on other malaria-like parasites.

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Naproxen-induced Ca2+ movement and death in MDCK canine renal tubular cells

Human & Experimental Toxicology ◽

10.1177/0960327115569810 ◽

2015 ◽

Vol 34 (11) ◽

pp. 1096-1105

Author(s):

H-H Cheng ◽

C-T Chou ◽

T-K Sun ◽

W-Z Liang ◽

J-S Cheng ◽

...

Keyword(s):

Endoplasmic Reticulum ◽

Annexin V ◽

Dependent Manner ◽

Acetoxymethyl Ester ◽

Concentration Dependent Manner ◽

Tubular Cells ◽

Renal Tubular Cells ◽

Renal Tubular ◽

Induced Apoptosis ◽

Darby Canine Kidney

Naproxen is an anti-inflammatory drug that affects cellular calcium ion (Ca2+) homeostasis and viability in different cells. This study explored the effect of naproxen on [Ca2+]i and viability in Madin-Darby canine kidney cells (MDCK) canine renal tubular cells. At concentrations between 50 μM and 300 μM, naproxen induced [Ca2+]i rises in a concentration-dependent manner. This Ca2+ signal was reduced partly when extracellular Ca2+ was removed. The Ca2+ signal was inhibited by a Ca2+ channel blocker nifedipine but not by store-operated Ca2+ channel inhibitors (econazole and SKF96365), a protein kinase C (PKC) activator phorbol 12-myristate 13-acetate, and a PKC inhibitor GF109203X. In Ca2+-free medium, pretreatment with 2,5-di-tert-butylhydroquinone or thapsigargin, an inhibitor of endoplasmic reticulum Ca2+ pumps, partly inhibited naproxen-induced Ca2+ signal. Inhibition of phospholipase C with U73122 did not alter naproxen-evoked [Ca2+]i rises. At concentrations between 15 μM and 30 μM, naproxen killed cells in a concentration-dependent manner, which was not reversed by prechelating cytosolic Ca2+ with the acetoxymethyl ester of 1,2-bis(2-aminophenoxy)ethane- N, N, N′, N′-tetraacetic acid acetoxymethyl. Annexin V/propidium iodide staining data suggest that naproxen induced apoptosis. Together, in MDCK renal tubular cells, naproxen induced [Ca2+]i rises by inducing Ca2+ release from multiple stores that included the endoplasmic reticulum and Ca2+ entry via nifedipine-sensitive Ca2+ channels. Naproxen induced cell death that involved apoptosis.

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Resveratrol decreases high glucose‑induced apoptosis in renal tubular cells via suppressing endoplasmic reticulum stress

Molecular Medicine Reports ◽

10.3892/mmr.2020.11511 ◽

2020 ◽

Author(s):

Jing Zhang ◽

Xiong‑Jun Dong ◽

Meng‑Ru Ding ◽

Chun‑Yu You ◽

Xin Lin ◽

...

Keyword(s):

Endoplasmic Reticulum ◽

Endoplasmic Reticulum Stress ◽

High Glucose ◽

Tubular Cells ◽

Renal Tubular Cells ◽

Renal Tubular ◽

Induced Apoptosis

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Effects of targeted Bcl-2 expression in mitochondria or endoplasmic reticulum on renal tubular cell apoptosis

AJP Renal Physiology ◽

10.1152/ajprenal.00415.2007 ◽

2008 ◽

Vol 294 (3) ◽

pp. F499-F507 ◽

Cited By ~ 31

Author(s):

Kirti Bhatt ◽

Leping Feng ◽

Navjotsingh Pabla ◽

Kebin Liu ◽

Sylvia Smith ◽

...

Keyword(s):

Endoplasmic Reticulum ◽

Cytochrome C ◽

Cell Apoptosis ◽

Atp Depletion ◽

Tubular Cell ◽

Renal Tubular Cell ◽

Wild Type ◽

Tubular Cells ◽

Renal Tubular Cells ◽

Renal Tubular

Bcl-2 family proteins are central regulators of apoptosis. As the prototypic member, Bcl-2 protects various types of cells against apoptotic insults. In mammalian cells, Bcl-2 has a dual subcellular localization, in mitochondria and endoplasmic reticulum (ER). The respective roles played by mitochondrial and ER-localized Bcl-2 in apoptotic inhibition are unclear. Using Bcl-2 constructs for targeted subcellular expression, we have now determined the contributions of mitochondrial and ER-localized Bcl-2 to the antiapoptotic effects of Bcl-2 in renal tubular cells. Wild-type Bcl-2, when expressed in renal proximal tubular cells, showed partial colocalizations with both cytochrome c and disulfide isomerase, indicating dual localizations of Bcl-2 in mitochondria and ER. In contrast, Bcl-2 constructs with mitochondria-targeting or ER-targeting sequences led to relatively restricted Bcl-2 expression in mitochondria and ER, respectively. Expression of wild-type and mitochondrial Bcl-2 showed significant inhibitory effects on tubular cell apoptosis that was induced by cisplatin or ATP depletion; however, ER-Bcl-2 was much less effective. During ATP depletion, cytochrome c was released from mitochondria into the cytosol. This release was suppressed by wild-type and mitochondrial Bcl-2, but not by ER-Bcl-2. Consistently, wild-type and mitochondrial Bcl-2, but not ER-Bcl-2, blocked Bax activation during ATP depletion, a critical event for mitochondrial outer membrane permeabilization and cytochrome c release. In contrast, ER-Bcl-2 protected against apoptosis during tunicamycin-induced ER stress. Collectively, the results suggest that the cytoprotective effects of Bcl-2 in different renal injury models are largely determined by its subcellular localizations.

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