Induction of stress protein HSP70 in nerve cells after status epilepticus in the rat

Vass, Karl; Berger, Michael L.; Nowak, Thaddeus S.; Welch, William J.; Lassmann, Hans

doi:10.1016/0304-3940(89)90695-2

Cited by 171 publications

(73 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Some staining, confined mostly to neu ronal cell bodies in the centers of infarctions, was observed when second antibody was not preab sorbed with rat serum. As noted previously by Vass et al (1989), some injured neurons appear to take up immunoglobulins (and other proteins), and prob ably because of cross-reactivity of rodent immuno globulins, incubation with anti-mouse second antisera (which have not been preabsorbed) can produce nonspecific cellular staining of immuno globulins in injured neurons and other cells. This nonspecific effect generally produced staining of cell bodies.…”

Section: Resultsmentioning

confidence: 61%

Heat Shock Protein hsp72 Induction in Cortical and Striatal Astrocytes and Neurons following Infarction

Sharp

Lowenstein

Simon

et al. 1991

J Cereb Blood Flow Metab

128

View full text Add to dashboard Cite

Summary: Transient global and transient focal ischemia induced the 72 kDa heat shock protein (hsp72) in neurons in cortex, striatum, and other regions known to be injured during transient ischemia. A novel finding was the induc tion of hsp72 in islands (cylinders in three dimensions) of cells composed of astrocytes around the perimeter and neurons in the interior. Since histology showed pale stain ing in these regions, it is proposed that these islands rep-

show abstract

Section: Resultsmentioning

confidence: 61%

Heat Shock Protein hsp72 Induction in Cortical and Striatal Astrocytes and Neurons following Infarction

Sharp

Lowenstein

Simon

et al. 1991

J Cereb Blood Flow Metab

128

View full text Add to dashboard Cite

show abstract

“…Vass et al (1989) in CA3, CA4, and dentate granule cell neurons known to survive, whereas HSP70 was minimally induced in CAl pyramidal neurons, which die. Sim ilarly, Simon et al (1991) found that short durations of global ischemia induced HSP70 in neurons that did not die, as assessed by acid fuchsin stains.…”

Section: This Induction In the Endothelial Cells In Infarcted Brain Rmentioning

confidence: 94%

“…Though many studies show that HSP70 expres sion is extremely useful for assessing injury (Vass et al, 1988(Vass et al, , 1989Brown et al , 1989;Dwyer et al , 1989;Gonzalez et al, 1989Gonzalez et al, , 1991F erriero et al , 1990;Lowenstein et al, 1990;Sharp et al , 1991a,b), it is unclear whether cells expressing HSP will live or die. Vass et al (1989) in CA3, CA4, and dentate granule cell neurons known to survive, whereas HSP70 was minimally induced in CAl pyramidal neurons, which die.…”

Section: This Induction In the Endothelial Cells In Infarcted Brain Rmentioning

confidence: 99%

Induction of 70-kDa Heat Shock Protein and hsp70 mRNA following Transient Focal Cerebral Ischemia in the Rat

Kinouchi

Sharp

Hill

et al. 1993

J Cereb Blood Flow Metab

185

View full text Add to dashboard Cite

Summary: Induction of the 70-kDa heat shock protein (HSP70) was demonstrated immunocytochemically in adult rats 4 h to 7 days following temporary middle cere bral artery (MeA) occlusions lasting 30, 60, or 90 min. Maximal HSP70 induction occurred �24 h following ischemia. Thirty minutes of ischemia induced HSP70 in neurons throughout the cortex in the MeA distribution, whereas 90 min of ischemia induced HSP70 in neurons in the penumbra. HSP70 protein was induced in endothelial cells in infarcted neocortex following 60-90 min of MeA occlusion, and HSP70 was induced in endothelial cells in infarcted regions of lateral striatum following 30-90 min Normal rat brain cells do not express the 70-kDa heat shock protein (HSP70) (Vass et aI. , 1988; Brown et aI. , 1989; Gonzalez et aI. , 1989; Sharp et aI. , 1991a,b), which is a product of the hsp70 gene (Hunt and Morimoto, 1985). HSP70 is induced in brain in response to hyperthermia (Brown, 1983;Sprang and Brown, 1987; Barbe et aI. , 1988), epi lepsy (Gonzalez et aI. , 1989; Vass et aI. , 1989; Lo wenstein et aI., 1990), hypoxia-ischemia (Nowak, 1985 Kiessling et aI. , 1986; Vass et aI. , 1988; Dwy er et aI. , 1989; Gonzalez et aI., 1989; Ferriero et aI. , 1990), injection of excitotoxins (Uney et aI. , 1988; Gonzalez et aI. , 1989) 105of MeA occlusion. hsp70 mRNA was induced in the MeA distribution in cortex and to a lesser extent in stri atum at 2 h to 3 days following 60 min of ischemia. It is proposed that brief ischemia induces hsp70 mRNA and HSP70 protein in the cells most vulnerable to ischemia the neurons. HSP70 protein is not induced in most neu rons and glia following 60-90 min of ischemia in areas destined to infarct, whereas it is induced in vascular en dothelial cells. Key Words: Focal brain-hsp70 mRNA Middle cerebral artery-Stress and heat shock protein Stroke.1981; Brown et aI. , 1989). Gonzalez et al. (1989) emphasized the potential value of using HSP70 im munostaining as a sensitive marker of brain cell in jury.HSPs are a family of proteins that perform many functions. Some 60-to 80-kDa HSPs appear to chaperone protein movements across membranes and mediate important protein-protein interactions in normal and stressed cells (Chapell et aI. , 1986;Ellis, 1987; Chirico et aI. , 1988; Cheng et aI. , 1989; Chiang et aI. , 1989; Deshaies et aI. , 1989; Beck mann et aI. , 1990). Some 90-kDa HSPs regulate ste roid receptor availability.Once HSPs are induced, they may prevent pro teins from being denatured (Pelham, 1986) and pro tect cells from subsequent injury (Schlesinger et aI. , 1982;Johnston and Kucey, 1988; Riabowol et aI., 1988). Barbe et al. (1988) provided the first direct evidence for this protective role in the CNS by showing that preinduction in the rabbit retina via systemic hyperthermia is associated with a de crease in light-induced retinal injury. Moreover, mild global cerebral ischemia, sufficient to induce 106 H. KINOUCHI ET AL.HSP70 in the hippocampus, attenuates the hippo campal injury associated with a subsequent severe ischemic...

show abstract

“…Polyclonal rabbit primary antisera were used in dilutions of 1:300. Bound antibody was visualized with an alkaline-phosphatase/anti-alkaline phosphatase technique [12]. As controls the primary antiserum was…”

Section: Methodsmentioning

confidence: 99%

A high ratio of chromogranin A to synaptin/synaptophysin is a common feature of brains in Alzheimer and Pick disease

et al. 1990

Self Cite

View full text Add to dashboard Cite

Chromogranin A and synaptin/synaptophysin were characterized by immunological methods in human autopsy brain tissue from patients with Alzheimer's and Pick's disease. In immunoblots there was no qualitative difference between the antigens in control and diseased brain, but significant quantitative differences were found. In all Alzheimer cases there was a significantly lower level of synaptin/synaptophysin, whereas chromogranin A was higher in 4 out of 5 cases and in all cases relative to synaptin/synaptophysin. An analogous findingwas obtained for Pick's disease. Immunohistologically a consistent staining of neuritic plaques for chromogranin A, but not for secretogranin II was found in Alzheimer cases. In Pick's disease the characteristic Pick bodies showed an analogous specific immunostaining.

show abstract

Induction of stress protein HSP70 in nerve cells after status epilepticus in the rat

Cited by 171 publications

References 13 publications

Heat Shock Protein hsp72 Induction in Cortical and Striatal Astrocytes and Neurons following Infarction

Heat Shock Protein hsp72 Induction in Cortical and Striatal Astrocytes and Neurons following Infarction

Induction of 70-kDa Heat Shock Protein and hsp70 mRNA following Transient Focal Cerebral Ischemia in the Rat

A high ratio of chromogranin A to synaptin/synaptophysin is a common feature of brains in Alzheimer and Pick disease

Contact Info

Product

Resources

About