Induction of Differential Heat Shock Gene Expression in Heart, Lung, Liver, Brain and Kidney by a Sympathomimetic Drug, Amphetamine

Lu, Danhong; Das, Debashis

doi:10.1006/bbrc.1993.1486

Cited by 28 publications

(11 citation statements)

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“…1A). In agreement with a previous report (Lu & Das 1993), Hsp27 mRNA was detected in heart tissue, but very low expression was detected in liver tissue under our assay conditions. Our experiments demonstrated that Hsp27 mRNA expression significantly increased during late pregnancy (one-way ANOVA, P , 0.0001; n ¼ 4).…”

Section: Analysis Of Hsp27 Expressionsupporting

confidence: 93%

Small heat shock protein 27 (Hsp27) expression is highly induced in rat myometrium during late pregnancy and labour

White¹,

Williams²,

Highmore³

et al. 2005

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The underlying mechanisms that regulate uterine contractions during labour are still poorly understood. A candidate regulatory protein is heat shock protein 27 (Hsp27). It belongs to the small heat shock protein family and can regulate actin cytoskeleton dynamics, act as a chaperone, and may regulate contractile protein activation. As a result, we hypothesized that Hsp27 expression would be highly induced during late pregnancy and labour. Hsp27 mRNA expression was significantly elevated (P < 0.05) on days 17 to 22 of gestation. In addition, immunoblot analysis demonstrated that detection of total Hsp27 increased (P < 0.05) between day 21 and 1 day post-partum (PP) inclusive. Since phosphorylation of Hsp27 has been reported to be a prerequisite for smooth muscle contraction, we examined the temporal and spatial expression of Ser-15 phosphorylated Hsp27. Immunoblot analysis showed that the detection of Ser-15 phosphorylated Hsp27 significantly increased (P < 0.05) between days 19 and 23 (active labour) inclusive, in parallel with detection of total Hsp27. Immunocytochemical analysis of Ser-15 phosphorylated Hsp27 expression in situ demonstrated that phosphorylated Hsp27 in circular muscle became detectable in peri-nuclear and membrane regions on days 19 to 22, but was primarily restricted to the cytoplasm on days 23 to PP. In contrast, phosphorylated Hsp27 in longitudinal muscle was primarily detected in myocyte membranes on days 15 to 22, and then also became detectable in the cytoplasm of myocytes on days 23 and PP. Our results demonstrate that Hsp27 expression is highly upregulated during late pregnancy and labour and suggest that Hsp27 is a potential candidate contraction-associated protein.

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Section: Analysis Of Hsp27 Expressionsupporting

confidence: 93%

Small heat shock protein 27 (Hsp27) expression is highly induced in rat myometrium during late pregnancy and labour

White¹,

Williams²,

Highmore³

et al. 2005

Reproduction

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“…Carpenter and Hofmann (2000) demonstrated a similar result, showing a higher constitutive Hsp70 expression in brain tissue as compared with white muscle tissue in several different notothenid fish species. Several other studies also showed tissue-specific differences in Hsp72 induction following hyperthermia; however, these studies did not examine the constitutive levels of Hsp73 and basal levels of Hsp72 in relation to the induction response (Flanagan et al, 1995;Hotchkiss et al, 1993;Lu and Das, 1993). In addition, it was shown that when Hsp73 was directly injected into Xenopus oocytes prior to an increase in temperature that would normally result in Hsp72 induction, an attenuation of the stress response was observed (Mifflin and Cohen, 1994).…”

Section: Correlation Between Hsp73 and Hsp72 Expressionmentioning

confidence: 99%

Tissue-specific expression of inducible and constitutive Hsp70 isoforms in the western painted turtle

Scott

Locke

Buck

2003

Journal of Experimental Biology

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Expression of Hsp73 and Hsp72 in four tissues of the naturally anoxia-tolerant western painted turtle (Chrysemys picta) was investigated in response to a 24 h forced dive and following 1 h recovery. Of the tissues examined, brain and liver displayed approximately threefold and sevenfold higher basal Hsp73 expression than heart and skeletal muscle. Basal Hsp72 expression was relatively low in all tissues examined. After the 24 h forced dive and 1 h recovery, Hsp73 expression did not differ significantly from basal expression with the exception of liver, where expression decreased significantly after 1 h recovery. Hsp72 expression was unchanged in liver following a 24 h dive; however, it increased twofold in brain and threefold in heart and skeletal muscle. Dive-induced Hsp72 expression was found to correlate inversely with basal Hsp73 expression. Following 1 h recovery, Hsp72 expression was significantly elevated in all tissues above levels in dived animals. These data indicate a tissue-specific pattern of Hsp73 and Hsp72 expression in the western painted turtle during both unstressed and stressed conditions.

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“…was administered and hsp25 are increased dramatically. [8][9] to naive, phenobarbital (PB)-induced or b-naphthofla-A number of observations suggest that stress induction vone (bNF)-induced mice, and the level of hsps in the of hsp synthesis is mediated by the presence of non-native liver analyzed 3, 6, and 24 hours after the cocaine dose.proteins. For example, overexpression of mammalian proAs measured by Western blotting, hsp70i levels were inteins unable to fold properly causes activation of hsp genes in creased at all time points, and hsp25 levels at the 6-and bacteria, 10 and the injection of chemically-denatured proteins 24-hour time points.…”

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Heat shock protein induction in murine liver after acute treatment with cocaine

et al. 1997

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the liver of naive mice, for example, hsp90, hsc70, and hsp60 The effect of cocaine on heat shock protein (hsp) inare expressed constitutively at appreciable levels. Levels of duction in murine liver was examined using Western hsp70i are relatively low, and hsp25 is virtually undetectblotting and immunohistochemistry. A single dose of coable. [5][6][7] In animals subjected to heat stress, levels of hsp70i caine (50 mg/kg, intraperitoneal [i.p.]) was administered and hsp25 are increased dramatically. [8][9] to naive, phenobarbital (PB)-induced or b-naphthofla-A number of observations suggest that stress induction vone (bNF)-induced mice, and the level of hsps in the of hsp synthesis is mediated by the presence of non-native liver analyzed 3, 6, and 24 hours after the cocaine dose.proteins. For example, overexpression of mammalian proAs measured by Western blotting, hsp70i levels were inteins unable to fold properly causes activation of hsp genes in creased at all time points, and hsp25 levels at the 6-and bacteria, 10 and the injection of chemically-denatured proteins 24-hour time points. Levels of hsp60, hsc70, and hsp90 into vertebrate cells increases stress protein synthesis, remained unchanged. Pretreatment of mice with the cywhereas injection of the corresponding native protein does tochrome P-450 inhibitor SKF-525A eliminated both conot. 11 Proteins of the hsp70 family are known to be capable of caine hepatotoxicity and the induced accumulation of binding non-native proteins [12][13] and are thought to chaperone hsp25 and hsp70i. Immunohistochemical localization of their refolding or elimination. During this binding, the heat hsp25 and hsp70i in the liver showed that concentrashock transcription factor normally bound to hsp70 is retions of both hsps were elevated only in cells with alleased, whereupon it rapidly oligomerizes to become trantered morphology. As has been observed previously, hescriptionally active. 14-16patic enzyme induction with PB or bNF shifted the Many hepatotoxicants are bioactivated to reactive intermelocation of the necrotic lesion within the lobule from diates that bind cellular macromolecules including prozone 2, as observed in naive mice of this strain, toward teins. [17][18] It is conceivable that adducted proteins resulting zone 1 (PB) or zone 3 (bNF), respectively. Localization from reactive metabolite binding are physiologically equivaof induced accumulation of hsp25 and hsp70i was found lent to proteins unfolded as a consequence of exposure to to shift within the lobule in parallel with the necrotic classical inducers of the heat stress response (e.g., heat, lesion in these animals. Immunostaining of cocaine reacheavy metals, and so on), thereby activating hsp gene exprestive metabolites bound to proteins was superimposable sion. Limited studies have suggested that hepatotoxicants on the areas with hsp accumulation and cells with alforming reactive metabolites may increase the expression of tered morphology. Our observations indicate a strong hsps, 19 but there has been little ...

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Induction of Differential Heat Shock Gene Expression in Heart, Lung, Liver, Brain and Kidney by a Sympathomimetic Drug, Amphetamine

Cited by 28 publications

References 0 publications

Small heat shock protein 27 (Hsp27) expression is highly induced in rat myometrium during late pregnancy and labour

Small heat shock protein 27 (Hsp27) expression is highly induced in rat myometrium during late pregnancy and labour

Tissue-specific expression of inducible and constitutive Hsp70 isoforms in the western painted turtle

Heat shock protein induction in murine liver after acute treatment with cocaine

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