scholarly journals Glial Cells, Inflammation and Heat Shock Proteins in Cerebral Ischemia

10.5772/33987 ◽  
2012 ◽  
Author(s):  
Vivianne L. ◽  
Robin E. ◽  
Rona Giffar
Keyword(s):  
Cerebral Ischemia ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Glial Cells ◽  
Shock Proteins

Differential expression of heat shock proteins by human glial cells

1992 ◽  
Vol 41 (2) ◽  
pp. 231-238 ◽  
Author(s):  
Mark S. Freedman ◽  
Natalie N. Buu ◽  
Theodora C.J. Ruijs ◽  
Kenneth Williams ◽  
Jack P. Antel
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Differential Expression ◽  
Glial Cells ◽  
Shock Proteins

Geldanamycin induces heat shock proteins in brain and protects against focal cerebral ischemia

2004 ◽  
Vol 81 (2) ◽  
pp. 355-364 ◽  
Author(s):  
Aigang Lu ◽  
Ruiqiong Ran ◽  
Sophie Parmentier-Batteur ◽  
Alex Nee ◽  
Frank R. Sharp
Keyword(s):  
Cerebral Ischemia ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Focal Cerebral Ischemia ◽  
Shock Proteins

scholarly journals The pharmacological suppression of spreading depolarization in ischemic neuroprotection

2020 ◽  
Author(s):  
Írisz Szabó
Keyword(s):  
Cerebral Cortex ◽  
Cerebral Ischemia ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Receptor Antagonist ◽  
Experimental Model ◽  
Ischemic Injury ◽  
Fp Receptor ◽  
Cerebral Ischemic ◽  
Shock Proteins

Background: Spontaneous, recurrent spreading depolarizations (SD) are increasingly more appreciated as a pathomechanism behind ischemic brain injuries. Hence, the pharmacological inhibition of SDs is the subject of growing interest. Here, we set out to explore the SD suppressive potential of three distinct pharmacological agents. First we evaluated the action of LA1011, a novel of dihydropyridine derivative, which acts as a co inducer of heat shock proteins, but is devoid of calcium channel antagonistic and vasodilator effects. Next, we applied AL-8810, a selective FP receptor antagonist to test the hypothesis that FP receptor blockade may achieve neuroprotection by the inhibition of SD, and possibly improve cerebral blood flow (CBF) in the ischemic rat cortex. Lastly, the endogenous hallucinogen and non-selective sigma 1 receptor (Sig-1R) agonist dimethyltryptamine (DMT) was used. DMT exerts tissue protective effects against hypoxia, but it was to be explored whether DMT was effective to reduce cerebral ischemic injury. Methods: Rats were treated with LA1011 either by chronic, systemic, or acute, local administration. In the latter treatment group, global forebrain ischemia was induced in half of the animals by bilateral common carotid artery occlusion under isoflurane anaesthesia. Functional hyperemia in the somatosensory cortex was created by mechanical stimulation of the contralateral whisker pad under α‐chloralose anaesthesia. SD events were elicited subsequently by 1 M KCl. Local field potential and CBF in the parietal somatosensory cortex were monitored by electrophysiology and laser Doppler flowmetry. AL-8810 or its vehicle were intravenously administered to anesthetized rats with acute cerebral ischemia/reperfusion exacerbated with recurrent SD induction. In this set of experiments, CBF was monitored with laser speckle contrast imaging. Finally, in a similar experimental model of ischemia/hypoxia/reperfusion, DMT, or the selective Sig 1R agonist PRE 084, or the Sig 1R antagonist NE 100, or the wide range serotonin receptor antagonist asenapine were administered alone or in combination intravenously. Results: LA1011 did not alter CBF, but intensified SD, presumably indicating the co‐induction of heat shock proteins, and, perhaps an anti inflammatory effect. The antagonism of FP receptors suppressed SD in the ischemic rat cerebral cortex and reduced the duration of recurrent SDs by facilitating repolarization. In parallel, FP receptor antagonism improved perfusion in the ischemic cerebral cortex, and attenuated hypoemic CBF responses associated with SD. Further, FP receptor antagonism appeared to restrain apoptotic cell death related to SD recurrence. Both DMT and PRE 084 reduced SD amplitude, the rate of depolarization, and the cumulative duration of SDs, which were suppressed by the addition of NE-100. Further, DMT attenuated SD when co-administered with asenapine, compared to asenapine alone. DMT administration reduced the number of apoptotic and ferroptotic cells and supported astrocyte survival, but had no effect on microglia. Sig-1Rs were associated with the perinuclear cytoplasm of neurons, astrocytes and microglia, and with glial processes. Conclusions: LA1011 seemed not to have any discernible cerebrovascular effects as was expected. Although, LA1011 had been proven neuroprotective in another experimental model of neurodegerative diseases, the treatment with LA1011 was inefficient in experimetal ischemic injury. Further investigation is needed to understand the mechanism of action of LA1011. Conversely, the antagonism of FP receptors (located at the neuro-vascular unit, neurons, astrocytes and microglia) has emerged as a promising approach to inhibit the evolution of SDs in cerebral ischemia. At last, the administration of DMT, alone or in combination with a Sig 1R antagonist suggested that DMT attenuated SD, at least in part, through Sig-1R activation, and achieved neuroprotection in the acute phase of cerebral ischemia. These data suggest that DMT may applicable as an adjuvant pharmacological therapy in the management of acute cerebral ischemic injury.

scholarly journals Antibodies to the atherosclerotic plaque components beta2-glycoprotein I and heat-shock proteins as risk factors for acute cerebral ischemia

2003 ◽  
Vol 61 (3B) ◽  
pp. 757-763 ◽  
Author(s):  
Henrique Luiz Staub ◽  
Gary Lewis Norman ◽  
Tiffany Crowther ◽  
Viviane Roseli da Cunha ◽  
Aline Polanczyk ◽  
...  
Keyword(s):  
Risk Factors ◽  
Ischemic Stroke ◽  
Cerebral Ischemia ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Humoral Response ◽  
Igg Antibodies ◽  
Stroke Patients ◽  
Increased Risk ◽  
Shock Proteins

One third of cases of cerebral ischemia have no clear etiology. A humoral response to the atherosclerotic plaques components beta2-glycoprotein l (beta2-gpl) and heat-shock proteins (Hsp) might be involved in the pathogenesis of stroke. This case-control study includes a complete profile of anti-beta2-gpl antibodies and testing of IgG antibodies to the 60/65 kilodaltons (kDa) Hsp in stroke patients. Ninety-three patients with acute ischemic stroke and 93 controls were evaluated for age, sex, race, hypertension, smoking, previous cardiopathy, diabetes mellitus, hypercholesterolemia and previous history of cerebral ischemia. lgG/lgM/lgA anticardiolipin (aCL) and anti-beta2-gpl antibodies, as well as lgG antibodies to human 60 kDa Hsp and to Mycobacterium bovis 65 kDa Hsp, were detected by immunoassay. Adjusted odds ratios (OR) were calculated by logistic regression. The adjusted OR for IgA anti-beta2-gpl antibodies was 4.6 (90%Cl 1.5 to 14.3; p = 0.025). The non-adjusted OR for IgG antibodies to Hsp 60 was 26.1. The adjusted OR for IgG antibodies to Hsp 65 was 3.2 (90%Cl 1.2 to 8.3; p = 0.044). The adjusted OR for lgG to any Hsp (60 or 65) was 4.8 (90%Cl 1.9 to 12.1; p = 0.006). This study demonstrates that elevated IgA anti-beta2-gpl and lgG anti-Hsp 60/65 antibodies are associated with increased risk of ischemic stroke. The association occurred independently of other risk factors. This humoral response might link autoimmunity, thrombophilia and atherosclerosis in stroke patients.

Scutellaria barbata flavonoids improve the composited Aβ-induced abnormal changes of glial cells in rats’ brain

2020 ◽  
Vol 23 ◽  
Author(s):  
Jian-Jun Cheng ◽  
Qing Guo ◽  
Xiao-Guang Wu ◽  
Shuai Ma ◽  
Yang Gao ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Expression ◽  
Mrna Expression ◽  
Glial Cells ◽  
Model Group ◽  
Hsp70 Protein ◽  
Shock Proteins ◽  
Apoe Mrna ◽  
The Brain

Aim: It has been reported that glial cells are involved in Alzheimer’s disease (AD). According to our previous research, Scutellaria barbata flavonoids (SBFs) can protect the neuronal disorder and memory impairment for AD-like rats, while the effect of SBFs on the glial cells disorder in AD-like rats has been less well studied. The effects of SBFs on astrocytes(ASs), microglial cells (MGs) and oligodendrocytes (Ols), as well as heat shock proteins 70 (Hsp70) and apolipoprotein E (ApoE) were investigated in the present study. Methods: The successful model rats, screened by Morris water maze, were daily orally administrated with 35, 70 and 140 mg/kg SBFs for 36 d. The numbers of brain’s astrocytes (ASs), microglial cells (MGs) and oligodendrocytes (Ols) were examined by immunohistochemistry. The cortical glial fibrillary acidic protein (GFAP), leukocyte common antigen (LCA) (CD45), Claudin 11 and heat shock proteins 70 (Hsp70) protein expression were assayed by Western blotting, and apolipoprotein E (ApoE) mRNA expression was analyzed by real-time quantitative polymerase chain reaction (qPCR). Results: Compared with the sham-operated group, the numbers of ASs and MGs in the brain were significantly increased in the model group (P<0.05, P<0.01), and accompanied with increases of GFAP, CD45 and Hsp70 protein and ApoE mRNA expression (P<0.05, P<0.01). Both Ols number and Claudin 11 protein expression decreased in the brain in the model group (P<0.05, P<<.01). However, the above abnormal changes induced by composited Aβ were differently reversed by treatment of SBFs at three doses of 35, 70 and 140 mg/kg (P<0.05, P<0.01). Conclusions: SBFs can dramatically improve the abnormal changes of glial cells in rats’ brain induced by composited Aβ, which may be a helpful treatment of neurodegenerative diseases.

Induction of heat shock proteins by hyperglycemic cerebral ischemia

2005 ◽  
Vol 139 (1) ◽  
pp. 80-87 ◽  
Author(s):  
Marianna Muranyi ◽  
Qing Ping He ◽  
Keith S.K. Fong ◽  
Ping-An Li
Keyword(s):  
Cerebral Ischemia ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins

scholarly journals Regulation of Apoptotic and Inflammatory Cell Signaling in Cerebral Ischemia

2008 ◽  
Vol 109 (2) ◽  
pp. 339-348 ◽  
Author(s):  
Rona G. Giffard ◽  
Ru-Quan Han ◽  
John F. Emery ◽  
Melissa Duan ◽  
Jean Francois Pittet
Keyword(s):  
Cerebral Ischemia ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Multiple Points ◽  
Inflammatory Cytokine Production ◽  
Response To Stress ◽  
Survival Signaling ◽  
Shock Proteins

Although heat shock proteins have been studied for decades, new intracellular and extracellular functions in a variety of diseases continue to be discovered. Heat shock proteins function within networks of interacting proteins; they can alter cellular physiology rapidly in response to stress without requiring new protein synthesis. This review focuses on the heat shock protein 70 family and considers especially the functions of the inducible member, heat shock protein 72, in the setting of cerebral ischemia. In general, inhibiting apoptotic signaling at multiple points and up-regulating survival signaling, heat shock protein 70 has a net prosurvival effect. Heat shock protein 70 has both antiinflammatory and proinflammatory effects depending on the cell type, context, and intracellular or extracellular location. Intracellular effects are often antiinflammatory with inhibition of nuclear factor-kappaB signaling. Extracellular effects can lead to inflammatory cytokine production or induction of regulatory immune cells and reduced inflammation.

Effect of Exposure to 1,800 MHz Electromagnetic Fields on Heat Shock Proteins and Glial Cells in the Brain of Developing Rats

2010 ◽  
Vol 20 (2) ◽  
pp. 109-119 ◽  
Author(s):  
Aurélie Watilliaux ◽  
Jean-Marc Edeline ◽  
Philippe Lévêque ◽  
Thérèse M. Jay ◽  
Michel Mallat
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Electromagnetic Fields ◽  
Glial Cells ◽  
Shock Proteins ◽  
The Brain

Two Novel Agents Boost Heat Shock Proteins

2005 ◽  
Vol 36 (10) ◽  
pp. 14
Author(s):  
PATRICE WENDLING
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Novel Agents ◽  
Shock Proteins

Heat shock proteins in willow (Salix viminalis)

1990 ◽  
Vol 80 (2) ◽  
pp. 301-306
Author(s):  
Tiina Vahala ◽  
Tage Eriksson ◽  
Peter Engstrom
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Salix Viminalis ◽  
Shock Proteins
Sign in / Sign up

Export Citation Format

Share Document