scholarly journals Inducible heat shock protein A1A (HSPA1A) is markedly expressed in rat myometrium by labour and secreted via myometrial cell-derived extracellular vesicles

2021 ◽  
Vol 33 (4) ◽  
pp. 279
Author(s):  
M. F. Russell ◽  
G. C. Bailey ◽  
E. I. Miskiewicz ◽  
D. J. MacPhee
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Extracellular Vesicles ◽  
Susceptibility Gene ◽  
Protein A ◽  
Circular Muscle ◽  
Late Pregnancy ◽  
Immunoblot Analysis ◽  
Interacting Protein ◽  
Myometrial Cell

The myometrium goes through physiological, cellular and molecular alterations during gestation that necessitate effective cellular proteostasis. Inducible heat shock protein A1A (HSPA1A) is a member of the 70-kDa heat shock protein A (HSPA) family, which acts as a chaperone to regulate proteostasis; however, HSPA1A also participates as a cytokine in inflammatory regulation, leading to its designation as a chaperokine. This study examined the spatiotemporal expression of HSPA1A protein in the rat myometrium throughout gestation and assessed whether it is secreted as cargo of myometrial cell-derived extracellular vesicles (EVs). Immunoblot analysis demonstrated that HSPA1A expression was markedly elevated during late pregnancy and labour and increased by uterine distension. Myometrial HSPA1A expression insitu increased in myocytes of longitudinal and circular muscle layers from Day 19 through to postpartum, specifically in the cytoplasm and nuclei of myocytes from both muscle layers, but frequently detectable just outside myocyte membranes. Scanning electron microscopy examination of samples isolated from hTERT-HM cell-conditioned culture medium, using EV isolation spin columns, confirmed the presence of EVs. EV lysates contained HSPA8, HSPA1A and the EV markers apoptosis-linked gene 2-interacting protein X (Alix), the tetraspanin cluster of differentiation 63 (CD63), tumour susceptibility gene 101 (TSG101) and HSP90, but not the endoplasmic reticulum protein calnexin. These results indicate that HSPA1A may act as a chaperokine in the myometrium during pregnancy.

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

Reproduction ◽  
2005 ◽  
Vol 129 (1) ◽  
pp. 115-126 ◽  
Author(s):  
B G White ◽  
S J Williams ◽  
K Highmore ◽  
D J MacPhee
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Regulatory Protein ◽  
Circular Muscle ◽  
Small Heat Shock Protein ◽  
Late Pregnancy ◽  
Immunoblot Analysis ◽  
Heat Shock Protein 27 ◽  
Potential Candidate ◽  
Hsp27 Expression

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 expressionin situdemonstrated 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.

The 90 000 dalton heat shock protein, a lot of smoke but no function as yet

1989 ◽  
Vol 67 (11-12) ◽  
pp. 749-750 ◽  
Author(s):  
Boyd Hardesty ◽  
Gisela Kramer
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein A

Expression of prostaglandin G/H synthase (PGHS) and heat shock protein-70 (HSP-70) in the corpus luteum (CL) of prostaglandin F2α-treated immature superovulated rats

2004 ◽  
Vol 82 (6) ◽  
pp. 363-371 ◽  
Author(s):  
R M Narayansingh ◽  
M Senchyna ◽  
M M Vijayan ◽  
J C Carlson
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Expression ◽  
Corpus Luteum ◽  
Heat Shock Protein 70 ◽  
Prostaglandin F2α ◽  
Sampling Period ◽  
Immunoblot Analysis ◽  
Hsp 70 ◽  
Prostaglandin F

In this study we examined the mechanism of corpus luteum (CL) regression by measuring changes in expression of prostaglandin G/H synthase-1 (PGHS-1) and -2 (PGHS-2) in day 4 CL and inducible heat shock protein 70 (HSP-70) in day 4 and day 9 CL of immature superovulated rats. The rats were superovulated and treated with 500 µg of prostaglandin F2α (PGF2α) on day 4 or day 9 after CL formation. Ovaries and serial blood samples were removed during the 24-hour period following treatment. Plasma progesterone was determined by radioimmunoassay while mRNA abundance and protein expression were assessed by semiquantitative RT-PCR and immunoblot analysis, respectively. One hour after PGF2α, both day 4 and day 9 rats exhibited a significant decrease in progesterone secretion; however, there was a greater decrease in day 9 rats. In ovarian samples removed on day 4, there was a significant increase in mRNA for PGHS-2 at 1 hour after PGF2α. PGHS-1 mRNA content remained unchanged. Immunoblot analyses showed an increase in PGHS-2 protein expression only at 8 h. There were no changes in PGHS-1 protein expression. In day 9 rats, ovarian HSP-70 protein levels increased by 50% after PGF2α injection; however, on day 4 there was no change in expression of this protein over the sampling period. These results suggest that expression of PGHS-2 may be involved in inhibiting progesterone production and that expression of HSP-70 may be required for complete CL regression in the rat.Key words: rat, prostaglandin F2α, corpus luteum, prostaglandin G/H synthase, heat shock protein-70.

Increased expression of collagen-binding heat shock protein 47 in murine bleomycin-induced pneumopathy

2003 ◽  
Vol 285 (4) ◽  
pp. L957-L963 ◽  
Author(s):  
Hiroshi Ishii ◽  
Hiroshi Mukae ◽  
Tomoyuki Kakugawa ◽  
Tetsuji Iwashita ◽  
Hideyuki Kaida ◽  
...  
Keyword(s):  
Heat Shock ◽  
Pulmonary Fibrosis ◽  
Heat Shock Protein ◽  
Smooth Muscle Actin ◽  
Protein A ◽  
Immunohistochemical Analysis ◽  
Rt Pcr ◽  
Heat Shock Protein 47 ◽  
Positive Type ◽  
Fibrotic Process

The 47-kDa heat shock protein 47 (HSP47) is a collagen-specific molecular chaperone that has been shown to play a major role during the processing and/or secretion of procollagen. Expression of HSP47 has been reported to increase in parallel with expression of collagens during the progression of various fibrosis models. The aim of the present study was to investigate the association between HSP47 expression and collagen accumulation in bleomycin (BLM)-induced murine fibrosis. We investigated the expression of HSP47 protein and mRNA using immunohistochemical analysis and semi-quantitative RT-PCR in murine BLM-induced pulmonary fibrosis. Immunohistochemical analysis showed that higher expression of HSP47 protein was present in BLM-induced pulmonary fibrosis compared with controls. HSP47 was localized predominantly in α-smooth muscle actin-positive myofibroblasts, F4/80 negative, surfactant protein-A-positive type II pneumocytes, and F4/80-positive macrophages. RT-PCR also demonstrated an increase of HSP47 mRNA expression in BLM-treated lungs. Moreover, the relative amounts of HSP47 mRNA correlated significantly with the lung hydroxyproline content as an indicator of pulmonary fibrosis in BLM-treated lungs ( r = 0.406, P <0.05). Our results suggest that these cells may play a role in the fibrotic process of BLM-treated lungs through upregulation of HSP47.

IS HEAT SHOCK PROTEIN A POTENTIAL PROTECTIVE MECHANISM AGAINST ISCHEMIA-REPERFUSION INJURY?

1999 ◽  
Vol 103 (1) ◽  
pp. 336-337 ◽  
Author(s):  
Sean Lille ◽  
Ching-Yuan Su ◽  
Michael Neumeister ◽  
Robert C. Russell ◽  
Chen-Ching Lai
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Reperfusion Injury ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Protein A ◽  
Protective Mechanism

Heat shock protein 80 ofNeurospora crassa: Sequence analysis of the gene and expression during the asexual phase

2000 ◽  
Vol 46 (11) ◽  
pp. 981-991 ◽  
Author(s):  
T L Girvitz ◽  
P M Ouimet ◽  
M Kapoor
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Immunoblot Analysis ◽  
Sequence Motifs ◽  
Gene Encoding ◽  
Putative Promoter Region ◽  
Calculated Molecular Mass ◽  
Transcription Start Sites ◽  
Oligomeric Complex ◽  
A Minor

Heat shock protein 80 (Hsp80) of Neurospora crassa, a member of the stress-90 protein family, is a cytosolic molecular chaperone that interacts directly with Hsp70 to form a hetero-oligomeric complex. The complete nucleotide sequence of the gene encoding this protein, along with the 5'- and 3'-flanking DNA, is reported. The coding sequence is interrupted by two introns, 61 and 30 nucleotides, respectively, in length. The deduced amino acid sequence corresponds to a 695-residue polypeptide with a calculated molecular mass of 78 894 Da and an average pI of 4.94. Primer extension experiments demonstrated two transcription start sites, a major and a minor one. No sequence motifs resembling the standard eukaryotic heat shock elements were evident in the putative promoter region. Immunoblot analysis showed Hsp80 protein to be present in the mature, dormant conidia, while the hsp80 transcripts were not detected. Both the transcripts and the protein were present in the germinating conidia in the absence of externally applied stress.Key words: Hsp90, filamentous fungi, sequence, conidia, germination.

scholarly journals A Histidine-rich and Cysteine-rich Metal-binding Domain at the C Terminus of Heat Shock Protein A fromHelicobacter pylori

2008 ◽  
Vol 283 (22) ◽  
pp. 15142-15151 ◽  
Author(s):  
Shujian Cun ◽  
Hongyan Li ◽  
Ruiguang Ge ◽  
Marie C. M. Lin ◽  
Hongzhe Sun
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Metal Binding ◽  
Protein A ◽  
Binding Domain ◽  
C Terminus ◽  
Metal Binding Domain

Mammalian CHORD-containing protein 1 is a novel heat shock protein 90-interacting protein

FEBS Letters ◽  
2004 ◽  
Vol 579 (2) ◽  
pp. 421-426 ◽  
Author(s):  
Jianchun Wu ◽  
Shouqing Luo ◽  
Hai Jiang ◽  
Honglin Li
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Interacting Protein
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