Adenine nucleotide and calpain inhibitor I protect against atractyloside-induced toxicity in rat renal cortical slices in vitro

2001 ◽  
Vol 75 (8) ◽  
pp. 487-496 ◽  
Author(s):  
David Obatomi ◽  
Richard Blackburn ◽  
Peter Bach
Keyword(s):  
Adenine Nucleotide ◽  
Calpain Inhibitor ◽  
Rat Renal Cortical Slices ◽  
Cortical Slices

Effects of lactate and glutamine on palmitate metabolism in rat kindey cortex

1976 ◽  
Vol 231 (1) ◽  
pp. 14-19 ◽  
Author(s):  
M Barac-Nieto
Keyword(s):  
Renal Cortex ◽  
Palmitate Oxidation ◽  
The Media ◽  
High Concentrations ◽  
Rat Renal Cortical Slices ◽  
Very High ◽  
Cortical Slices ◽  
Palmitate Metabolism ◽  
Low Rate

Rat renal cortical slices were incubated with [1-(14)C]palmitate bound to 2.5% albumin. The following effects were found: a)1 mM palmitate utilization or oxidation to CO(2) varied according to the concentration of lactate in the media, it increased at 0.8 and 3.2 mM, was unchanged at 8 mM, and decreased at 16 mM. Esterification was stimulated at 3.2 mM lactate. b) Addition of glutamine (0.1 mM) instead of lactate stimulated incomplete and complete oxidation of palmitate (1 mM), whereas high medium glutamine (10 mM) inhibited palmitate (1 mM) utilization, esterification, and oxidation to CO(2) but increased its incomplete oxidation. The low rate of exogenous palmitate oxidation observed in this study and the finding that exogenous palmitate oxidation is only partially inhibited at very high concentrations of exogenous lactate or glutamine are consistent with the view that these exogenous substrates contribute little to the oxidative metabolism of rat renal cortex in vitro, which probably depends on the supply of substrates endogenous to the tissue.

Amelioration of Cisplatin Toxicity in Rat Renal Cortical Slices by Dithiothreitol In vitro

1994 ◽  
Vol 13 (2) ◽  
pp. 89-93 ◽  
Author(s):  
J.G. Zhang ◽  
L.F. Zhong ◽  
M. Zhang ◽  
X.L. Ma ◽  
Y.X. Xia ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Protective Effect ◽  
Protective Mechanism ◽  
Protective Effects ◽  
Metal Chelator ◽  
Rat Renal Cortical Slices ◽  
Antioxidative Action ◽  
Cortical Slices ◽  
Related Increase

1 The protective effects of dithiothreitol (DTT) on cisplatin-induced nephrotoxicity were investigated with rat renal cortical slices. 2 The nephrotoxic effects of cisplatin (2 mmol l-1) were manifested in several ways: the Na+ and water content were increased while K+ was decreased. The malondiadehyde (MDA) concentration in the slices and the lactate dehydrogenase (LDH) released into the medium were increased. The uptake of p-aminohippurate (PAH), the synthesis of glucose and the glutathione (GSH) concentration in the slices were all decreased. 3 Despite a DTT-related increase in platinum (Pt) uptake by the slices, DTT (0.5-2 mmol I-1 ) ameliorated all these toxic effects of cisplatin in a concentration related manner. 4 The results suggest that the protective mechanism of DTT is its antioxidative action, DTT is also a metal chelator, however, and so a protective effect via chelation of Pt by DTT cannot be excluded.

Rat renal cortical slices: Maintenance of viability and use in in vitro nephrotoxicity testing

1997 ◽  
Vol 11 (5) ◽  
pp. 723-729 ◽  
Author(s):  
M. Blackmore ◽  
J.C. Richardson ◽  
S.A. Rhodes ◽  
L. Patterson ◽  
A.J. Spencer ◽  
...  
Keyword(s):  
Rat Renal Cortical Slices ◽  
Cortical Slices

Importance of calcium in renal renin release

1986 ◽  
Vol 251 (1) ◽  
pp. E98-E103 ◽  
Author(s):  
W. L. Henrich ◽  
W. B. Campbell
Keyword(s):  
Calcium Ionophore ◽  
Calcium Ionophore A23187 ◽  
Adenyl Cyclase ◽  
Renin Release ◽  
Ionophore A23187 ◽  
The Media ◽  
Rat Renal Cortical Slices ◽  
Camp Levels ◽  
Cortical Slices

The sequence of intracellular events that lead to renin release is incompletely defined. Accordingly, we examined the interrelationship of two important factors in the process: renin release coupled to cAMP and renin release related to a decrease in intracellular calcium activity (Cai). Rat renal cortical slices were used to study these relationships in vitro. In the initial studies, cAMP-coupled renin release was established for isoproterenol (10(-5) M), prostacyclin (PGI2; 10(-6) M), and forskolin (10(-5) M). Each agent caused an increase in renin release and tissue cAMP levels, which were inhibited by the addition of the adenyl cyclase inhibitor 2',5'-dideoxyadenosine (DDA, 10(-5) M) to the media. Diltiazem (10(-4) M) and 8-(N,N-diethylamino)octyl-3,4,5-trimethoxybenzoate (TMB-8; 0.6 X 10(-4) M) are believed to decrease Cai by different mechanisms; each of these agents caused a significant increase in renin release. Renin release stimulated by diltiazem, and TMB-8 was not inhibited by either DDA or indomethacin. The calcium ionophore A23187 (17 X 10(-6) M) and vanadate (10(-3) M) were next added to produce an increase in Cai. Both of these agents blunted renin release produced by isoproterenol, PGI2, and forskolin. These results provide strong indirect support for an inverse relationship between Cai and renin release in the juxtaglomerular cell. The results also imply that changes in Cai occupy a step that is distal to cAMP-coupled events in the sequence of intracellular events which culminate in renin release.

Modification of glycosylation of renin in sodium-depleted and captopril-treated rats

1989 ◽  
Vol 256 (6) ◽  
pp. E798-E804 ◽  
Author(s):  
S. Kim ◽  
M. Hosoi ◽  
M. Hiruma ◽  
F. Ikemoto ◽  
K. Yamamoto
Keyword(s):  
Half Life ◽  
Blood Circulation ◽  
Relative Proportion ◽  
Plasma Renin ◽  
Rat Plasma ◽  
Con A ◽  
Plasma Renin Concentration ◽  
Rat Renal Cortical Slices ◽  
Cortical Slices

Concanavalin A (con A) chromatography of rat plasma revealed the presence of three differently glycosylated forms of renin, including the con A unbound form (renin C), the loosely bound form (renin A), and the tightly bound form (renin B). Rat renal cortical slices in vitro secreted all these forms. They had a different half-life in the plasma after ligation of both renal artery and vein (half-life of 21 +/- 1, 14 +/- 3, and 35 +/- 4 min for renin A, B, and C, respectively). Thus differently glycosylated forms of renin are released from the kidney into the blood circulation and disappear, with a different half-life. Rats were sodium-depleted and captopril-treated (40-60 mg.kg-1.day-1) for 2 wk, and the effects of these treatments on relative proportions of renin A, B, and C were investigated. These treatments elevated plasma renin concentration approximately 60-fold (from 24 +/- 3 to 1,406 +/- 128 ng angiotensin I.h-1.ml-1; P less than 0.01), in association with an increase in the relative percent of renin C in the plasma from 22 +/- 2 to 39 +/- 3% (P less than 0.01). Moreover, the relative proportion of renin C released from the renal cortical slices was significantly higher in the treated than in the control rats (42 +/- 9 vs. 16 +/- 3% of secreted renin, respectively; P less than 0.02). These results show that the predominant release of renin C, with the longest half-life (35 min) in the plasma, contributes to the increased plasma renin concentration in sodium-depleted and captopril-treated rats.

scholarly journals PAR-4/Ca2+-calpain pathway activation stimulates platelet-derived microparticles in hyperglycemic type 2 diabetes

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Alessandra Giannella ◽  
Giulio Ceolotto ◽  
Claudia Maria Radu ◽  
Arianna Cattelan ◽  
Elisabetta Iori ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Normal Glucose Tolerance ◽  
Calpain Inhibitor ◽  
Pathway Activation ◽  
Normal Glucose ◽  
Circulating Levels ◽  
Dependent Mechanism

Abstract Background Patients with type 2 diabetes (T2DM) have a prothrombotic state that needs to be fully clarified; microparticles (MPs) have emerged as mediators and markers of this condition. Thus, we investigate, in vivo, in T2DM either with good (HbA1c ≤ 7.0%; GGC) or poor (HbA1c > 7.0%; PGC) glycemic control, the circulating levels of MPs, and in vitro, the molecular pathways involved in the release of MPs from platelets (PMP) and tested their pro-inflammatory effects on THP-1 transformed macrophages. Methods In 59 T2DM, and 23 control subjects with normal glucose tolerance (NGT), circulating levels of CD62E+, CD62P+, CD142+, CD45+ MPs were determined by flow cytometry, while plasma levels of ICAM-1, VCAM-1, IL-6 by ELISA. In vitro, PMP release and activation of isolated platelets from GGC and PGC were investigated, along with their effect on IL-6 secretion in THP-1 transformed macrophages. Results We found that MPs CD62P+ (PMP) and CD142+ (tissue factor-bearing MP) were significantly higher in PGC T2DM than GGC T2DM and NGT. Among MPs, PMP were also correlated with HbA1c and IL-6. In vitro, we showed that acute thrombin exposure stimulated a significantly higher PMP release in PGC T2DM than GGC T2DM through a more robust activation of PAR-4 receptor than PAR-1 receptor. Treatment with PAR-4 agonist induced an increased release of PMP in PGC with a Ca2+-calpain dependent mechanism since this effect was blunted by calpain inhibitor. Finally, the uptake of PMP derived from PAR-4 treated PGC platelets into THP-1 transformed macrophages promoted a marked increase of IL-6 release compared to PMP derived from GGC through the activation of the NF-kB pathway. Conclusions These results identify PAR-4 as a mediator of platelet activation, microparticle release, and inflammation, in poorly controlled T2DM.

The novel calpain inhibitor A-705253 prevents stress-induced tau hyperphosphorylation in vitro and in vivo

2012 ◽  
Vol 63 (4) ◽  
pp. 606-612 ◽  
Author(s):  
Arthur L. Nikkel ◽  
Brenda Martino ◽  
Stella Markosyan ◽  
Jill-Desiree Brederson ◽  
Rodrigo Medeiros ◽  
...  
Keyword(s):  
Calpain Inhibitor ◽  
Tau Hyperphosphorylation ◽  
The Novel

scholarly journals Effects of calpain and Rho-kinase inhibitors on the acrosome reaction and motility of fowl spermatozoa in vitro

Reproduction ◽  
2006 ◽  
Vol 131 (1) ◽  
pp. 71-79 ◽  
Author(s):  
K Ashizawa ◽  
G J Wishart ◽  
S Katayama ◽  
D Takano ◽  
M Maeda ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Acrosome Reaction ◽  
Kinase Inhibitors ◽  
Rho Kinase ◽  
Specific Inhibitor ◽  
Immunoblot Analysis ◽  
Calpain Inhibitor ◽  
Cytoplasmic Matrix ◽  
Sperm Extract

At the avian body temperature of 40 °C, intact fowl spermatozoa require Ca2+for the initiation of motility and a combination of both Ca2+and homogenized inner perivitelline layer (IPVL) together to induce the acrosome reaction. Within the range of 1–100 μmol/l, neither PD 150606 (a Ca2+-dependent calpain inhibitor) nor Y-27632 (an inhibitor of Ca2+-dependent Rho-kinase) were able to inhibit the acrosome reaction induced by the presence of Ca2+and IPVL. However, PD 150606, although not Y-27632, was able to inhibit sperm motility initiated by Ca2+, as well as motility initiated by calyculin A – a specific inhibitor of protein phosphatases, which also initiates sperm motility at 40 °C. The addition of PD 150606 did not reduce the ATP concentrations of intact spermatozoa, nor the motility of demembranated spermatozoa. Immunoblot analysis of sperm extract using a polyclonal antibody against calpain 12 revealed a cross-reacting protein of approximately 80 kDa. These results suggest that Rho-kinase is not involved in the regulation of the acrosome reaction or of motility in fowl spermatozoa. In contrast, calpain appears to be involved in the regulation of flagellar movement, but not izn that of the acrosome reaction. Furthermore, it seems that endogenous calpain is present in the cytoplasmic matrix and/or the plasma membrane, but not retained in the axoneme and/or accessory cytoskeletal components.

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