scholarly journals Long-term thyroxine administration increases heat stress protein-70 mRNA expression and attenuates p38 MAP kinase activity in response to ischaemia

2001 ◽  
Vol 170 (1) ◽  
pp. 207-215 ◽  
Author(s):  
CI Pantos ◽  
VA Malliopoulou ◽  
IS Mourouzis ◽  
EP Karamanoli ◽  
SM Tzeis ◽  
...  
Keyword(s):  
Protein Expression ◽  
Mrna Expression ◽  
P38 Mapk ◽  
Stress Protein ◽  
P38 Map Kinase ◽  
Hsp70 Mrna ◽  
Mrna Induction ◽  
Rat Hearts ◽  
Heat Stress Protein

The present study was undertaken to investigate heat stress protein (HSP)-70 mRNA induction and p38 MAP kinase (MAPK) activity in response to ischaemic stress in the hyperthyroid rat heart. L-Thyroxine (T(4)) (25 microg/100 g body weight) was administered to Wistar rats for 2 days (THYRacute) or 14 days (THYR), while animals treated similarly with normal saline served as controls (NORMacute and NORM). In addition, abdominal aortic banding was performed in another group of rats to produce constriction-induced hypertrophy (HYP), while sham-operated (SOP) animals served as controls. Isolated rat hearts were perfused in a Langendorff mode. Hearts from NORMacute (n=6), THYRacute animals (n=8), NORM (n=6), THYR (n=6), SOP (n=5) and HYP (n=7) animals were subjected to 20 min of zero-flow global ischaemia followed by 45 min of reperfusion. HSP70 mRNA expression and phosphorylated p38 MAPK protein expression were detected in response to ischaemia and protein kinase C-epsilon (PKCepsilon) protein expression was detected at baseline. Thyroid hormones were measured in plasma. Long-term T(4) administration and aortic constriction resulted in the development of cardiac hypertrophy. Thyroid hormones were increased in both THYR and THYRacute as compared with normal groups (P<0.05). HSP70 mRNA induction was increased 2.3-fold in THYR as compared with NORM hearts (P<0.05), whereas there was not any difference between THYRacute and NORMacute hearts (P>0.05). Phosphorylated p38 MAPK protein expression was 2.2-fold more in NORM than in THYR hearts (P<0.05), but it was not different between NORMacute and THYRacute hearts (P>0.05). HSP70 mRNA induction was 1.8-fold greater in HYP than in SOP hearts (P<0.05), whereas phosphorylated p38 MAPK protein expression was similar between the two groups (P>0.05). PKCepsilon protein expression at baseline was 1.7-fold more in NORM than in THYR hearts (P<0.05), and not different between NORMacute and THYRacute hearts (P>0.05) as well as HYP and SOP hearts (P>0.05). This study shows that HSP70 mRNA expression is increased, whereas p38 MAPK activation is attenuated in response to ischaemia in long-term T(4)-treated rat hearts as compared with normal and acute hyperthyroid hearts.

A new method of long-term preventive cardioprotection usingLactobacillus

2000 ◽  
Vol 278 (5) ◽  
pp. H1717-H1724 ◽  
Author(s):  
Tatyana Oxman ◽  
Michal Shapira ◽  
Adriana Diver ◽  
Rodica Klein ◽  
Natalie Avazov ◽  
...  
Keyword(s):  
Ischemia Reperfusion ◽  
Stress Protein ◽  
Beneficial Effects ◽  
Cellular Defense ◽  
Heat Stress Protein ◽  
Protective Proteins ◽  
Perfused Hearts ◽  
Related Compounds ◽  
Stop Flow

Potential long-term cardioprotection was investigated in an extensive experimental study. Lactobacillus cultivation components (LCC) were administered intravenously in anesthetized rats 1, 7, and 21 days before global ischemia (GI). GI was produced by full stop flow in isolated Langendorff-perfused hearts for 20 min and was followed by reperfusion. Control animals were injected with saline. LCC reduced reperfusion tachyarrhythmia significantly and improved functional recovery of the ischemized rat heart. These beneficial effects were associated with reduction of release of norepinephrine (NE) and prostacyclin at the first minute of reperfusion, activation of myocardial catalase, and overexpression of 70-kDa heat stress protein (HSP-70) at ischemia and reperfusion ( P < 0.05). This cardioprotection was documented up to 21 days after a single injection of LCC. Thus Lactobacillus cultivation components are new nontoxic materials that produce marked long-term cardioprotection against ischemia-reperfusion damage. This effect is attributed to an activation of the cellular defense system, manifested by activation of the antioxidant pathway and by expression of protective proteins. NE is involved in this process, and the data also suggest a role for prostacyclin in this model of cardioprotection. The potential of LCC and related compounds working through similar mechanisms in the prevention and therapy of various ischemic heart syndromes should be explored.

scholarly journals Effect of Plastrum Testudinis Extracts on the Proliferation and Osteogenic Differentiation of rBMSCs by Regulating p38 MAPK-Related Genes

2019 ◽  
Vol 2019 ◽  
pp. 1-10 ◽  
Author(s):  
Qi Shang ◽  
Xiang Yu ◽  
Hui Ren ◽  
Gengyang Shen ◽  
Wenhua Zhao ◽  
...  
Keyword(s):  
Protein Expression ◽  
Osteogenic Differentiation ◽  
Mrna Expression ◽  
P38 Mapk ◽  
Bone Diseases ◽  
Treatment Of Osteoporosis ◽  
Osteogenic Induction ◽  
Rat Bone

Extracts from plastrum testudinis (PTE) are active compounds that have been used to treat bone diseases in traditional Chinese medicine for thousands of years. In previous studies, we demonstrated their effects on glucocorticoid-induced osteoporosis both in vivo and in vitro. However, the mechanisms by which PTE regulates the osteogenic differentiation of rat bone marrow-derived mesenchymal stem cells (rBMSCs) in vitro remain poorly understood. In this study, rBMSCs were treated with medium (CON), PTE, osteogenic induction (OI), and a combination of PTE and OI (PTE+OI) over a 21-day period. We found that PTE significantly promoted rBMSCs osteogenic differentiation and mineralisation after 21 days of culturing. Moreover, PTE+OI further enhanced the differentiation and mineralisation process. PTE upregulated STE20, IGF1R, and p38 MAPK mRNA expression and downregulated TRAF6 mRNA expression. The extracts inhibited TRAF6 protein expression and promoted STE20, IGF1R, and phosphorylated p38 MAPK protein expression. Our results imply that PTE promotes the proliferation and osteogenic differentiation of rBMSCs by upregulating p38 MAPK, STE20, and IGF1R and downregulating TRAF6 expression, which may provide experimental evidence of the potential of PTE in the treatment of osteoporosis.

Activation of pancreatic acinar cells on isolation from tissue: cytokine upregulation via p38 MAP kinase

2000 ◽  
Vol 279 (6) ◽  
pp. C1993-C2003 ◽  
Author(s):  
Thane A. Blinman ◽  
Ilya Gukovsky ◽  
Michelle Mouria ◽  
Vjekoslav Zaninovic ◽  
Edward Livingston ◽  
...  
Keyword(s):  
Mrna Expression ◽  
P38 Mapk ◽  
Acinar Cells ◽  
Inflammatory Cells ◽  
Cytokine Expression ◽  
P38 Map Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Pancreatic Acinar Cells ◽  
Rat Pancreas ◽  
Sb 203580

Cytokines produced by pancreatic acinar cells may mediate cell death and recruitment of inflammatory cells into pancreas in pancreatitis and other disorders. Here, we demonstrate mRNA expression for a number of cytokines in acini isolated from rat pancreas. Using RNA from microscopically selected individual cells, we confirmed the acinar cell as a source for cytokine expression. Competitive RT-PCR, Western blot analysis, and immunocytochemistry showed large amounts of monocyte chemotactic protein-1 and interleukin-6 compared with other cytokines. Cytokine expression was inhibited by either inhibitors of p38 mitogen-activated protein kinase (MAPK), SB-202190 and SB-203580, or (less strongly) by the transcription factor nuclear factor (NF)-κB inhibitor MG-132. A combination of SB-203580 and MG-132 inhibited mRNA expression of all cytokines by >90%. The results suggest a major role for p38 MAPK and involvement of NF-κB in cytokine expression in pancreatic acinar cells. In contrast to isolated acini, we detected no or very low cytokine expression in normal rat pancreas. Our results indicate that activation of p38 MAPK, transcription factors, and cytokines occurs during removal of the pancreas from the animal and isolation of acini.

Differential long-term regulation of MEK and of p42 MAPK in rat glomerular mesangial cells

1996 ◽  
Vol 270 (1) ◽  
pp. C40-C48 ◽  
Author(s):  
H. Schramek ◽  
A. Sorokin ◽  
R. D. Watson ◽  
M. J. Dunn
Keyword(s):  
Mrna Expression ◽  
Receptor Agonist ◽  
Mesangial Cells ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Mitogen Activated Protein Kinase ◽  
Early Gene ◽  
Glomerular Mesangial Cells ◽  
Mrna Induction

Constitutive stimulation of the mitogen-activated protein kinase (MAPK) activator MAPK/ERK kinase (MEK) is sufficient to promote long-term events such as cell differentiation, proliferation, and transformation. To evaluate a possible mechanism for the chronic regulation of MEK and p42 MAPK, we studied the long-term effects of fetal bovine serum (FBS), the G protein-coupled receptor agonist endothelin-1 (ET-1), and the protein tyrosine kinase-coupled receptor agonist platelet-derived growth factor BB (PDGF BB) on MEK and p42 MAPK in glomerular mesangial cells (GMC). FBS, ET-1, and PDGF BB led to a time-dependent increase in MEK-1 mRNA and protein expression without altering p42 MAPK mRNA and protein levels. FBS also induced MEK-1 mRNA expression in diverse cell types, including NIH/3T3 fibroblasts, A7r5 vascular smooth muscle cells, and Chinese hamster ovary cells. In GMC, cycloheximide inhibited MEK-1 mRNA induction but stimulated p42 MAPK mRNA expression in the absence and presence of FBS, ET-1, or PDGF. The FBS-induced increase in MEK-1 mRNA was accompanied by a sustained enhancement of MEK activity, as assessed by the ability of immunoprecipitated p45 MEK to activate recombinant p42 MAPK and hence phosphorylate myelin basic protein, and p42 MAPK activity. We conclude that, in GMC, MEK-1 acts like a delayed-early gene and that it can be chronically induced at the mRNA and protein level.

scholarly journals Decreased expression of carbonic anhydrase isozyme II, rather than of isozyme VI, in submandibular glands in long-term zinc-deficient rats

2008 ◽  
Vol 99 (2) ◽  
pp. 248-253 ◽  
Author(s):  
Tomoko Goto ◽  
Hitoshi Shirakawa ◽  
Yuji Furukawa ◽  
Michio Komai
Keyword(s):  
Carbonic Anhydrase ◽  
Protein Expression ◽  
Mrna Expression ◽  
Submandibular Gland ◽  
Blot Analysis ◽  
Salivary Secretion ◽  
Zn Deficiency ◽  
Sprague Dawley ◽  
Carbonic Anhydrase Isozyme

We previously reported that in rats, long-term Zn deficiency significantly reduced taste sensitivity and total carbonic anhydrase (CA) activity in the submandibular gland. We therefore investigated the effects of Zn deficiency on salivary secretion and the expressions of CA isozymes (II and VI) in the rat submandibular gland, since those isozymes are thought to be related to taste sensation and salivary secretion. Male Sprague–Dawley rats, age 4 weeks, were divided into three groups (Zn-def, low-Zn and pair-fed, that were fed a diet containing 2·2, 4·1 or 33·7 mg Zn/kg, respectively, for 42 d). Northern blot analysis indicated that Zn deficiency reduced CA II mRNA expression in the submandibular gland without reducing CA VI mRNA expression. In Western blot analysis, Zn deficiency significantly reduced CA II (erythrocyte CA) protein expression in the submandibular gland without reducing CA VI protein expression. Salivary secretion was lower in the Zn-def group than in the pair-fed group. These results suggest that decreased CA isozyme II expression underlies the decreased CA activity previously reported in the submandibular gland in Zn-def rats, and this may reduce regular salivary secretion.

scholarly journals Localization of 70 kDa Stress Protein mRNA Induction in Gerbil Brain after Ischemia

1991 ◽  
Vol 11 (3) ◽  
pp. 432-439 ◽  
Author(s):  
Thaddeus S. Nowak
Keyword(s):  
Hippocampal Neurons ◽  
Granule Cells ◽  
Stress Protein ◽  
Transcriptional Level ◽  
Drug Induced ◽  
Hsp70 Mrna ◽  
Ca1 Neurons ◽  
Mrna Induction ◽  
Gerbil Brain ◽  
Pre Treatment

Induction of mRNA encoding the 70 kDa stress/heat shock protein, hsp70, was evaluated in postischemic gerbil brain by in situ hybridization using an oligonucleotide probe selective for stress-inducible members of this gene family. Expression of hsp70 sequences was most pronounced in hippocampal CA1 neurons that fail to accumulate immunoreactive hsp70 protein, and that are selectively lost following ischemia. Hybridizable RNA continued to be expressed in CA1 through at least 48 h, essentially until the onset of cell death in this model. In contrast, dentate granule cells and CA3 neurons destined to survive the insult showed transient induction of hsp70 mRNA during the first 24 h of recirculation that disappeared prior to the detection of maximal hsp70 immunoreactivity in these cell populations. Pre treatment with a single injection of MK-801 (10 mg/kg) considerably attenuated the induction of hsp70 mRNA in hippocampus at 6 h of recirculation, an effect apparently mediated by persistent drug-induced hypothermia. The drug did not prevent the later, selective appearance of hsp70 hybridization in CA1 neurons at 24 h, nor did it protect against the subsequent loss of these cells. These results demonstrate a prolonged postischemic stress response at the transcriptional level in vulnerable hippocampal neurons, and suggest its utility as a marker for neuronal pathophysiology associated with mechanisms mediating delayed neuronal death.

scholarly journals Pattern of stress protein expression in human lung cell-line A549 after short- or long-term exposure to cadmium.

2000 ◽  
Vol 108 (1) ◽  
pp. 55-60 ◽  
Author(s):  
F Croute ◽  
B Beau ◽  
C Arrabit ◽  
Y Gaubin ◽  
F Delmas ◽  
...  
Keyword(s):  
Protein Expression ◽  
Cell Line ◽  
Human Lung ◽  
Stress Protein ◽  
Human Lung Cell Line ◽  
Lung Cell Line

Membrane depolarization induces calcium-dependent upregulation of Hsp70 and Hmox-1 in skeletal muscle cells

2009 ◽  
Vol 297 (3) ◽  
pp. C581-C590 ◽  
Author(s):  
Gonzalo Jorquera ◽  
Nevenka Juretić ◽  
Enrique Jaimovich ◽  
Nora Riveros
Keyword(s):  
Skeletal Muscle ◽  
Protein Expression ◽  
Muscle Cells ◽  
Membrane Depolarization ◽  
Skeletal Muscle Cells ◽  
Heme Oxygenase 1 ◽  
Induced Expression ◽  
Hsp70 Mrna ◽  
Calcium Dependent ◽  
Mrna Induction

Heat shock proteins (HSPs) are a conserved family of cytoprotective polypeptides, synthesized by cells in response to stress. Hsp70 and heme oxygenase 1 (Hmox-1) are induced by a variety of cellular stressors in skeletal muscle, playing a role in long-term adaptations and muscle fibers regeneration. Though HSPs expression after exercise has been intensely investigated, the molecular mechanisms concerning Hsp70 and Hmox-1 induction are poorly understood. The aim of this work was to investigate the involvement of calcium in Hsp70 and Hmox-1 expression upon depolarization of skeletal muscle cells. We observed that depolarization of myotubes increased both mRNA levels and protein expression for Hsp70 and Hmox-1. Stimulation in the presence of intracellular calcium chelator BAPTA-AM resulted in a complete inhibition of Hsp70-induced expression. It is known that inositol-1,4,5-trisphophate (IP3)-mediated slow Ca2+ transients, evoked by membrane depolarization, are involved in the regulation of gene expression. Here we demonstrated that inhibition of IP3-dependent calcium signals decreased both Hsp70 mRNA induction and Hsp70 and Hmox-1 protein expression. Inhibitors of calcium-dependent protein kinase C also abolished Hsp70 mRNA induction. Our results provide evidence that membrane depolarization increases Hsp70 and Hmox-1 expression in cultured skeletal muscle cells, which the effect is critically dependent on Ca2+ released from IP3-sensitive intracellular stores and that it involves PKC as an upstream effector in Hsp70 mRNA-induced expression.

Sign in / Sign up

Export Citation Format

Share Document