RNAi silencing of calcium-regulated heat-stable protein of 24 kDa in Schistosoma japonicum affects parasite growth

2010 ◽  
Vol 108 (3) ◽  
pp. 567-572 ◽  
Author(s):  
Xiang Zou ◽  
Ya-mei Jin ◽  
Ping-ping Liu ◽  
Qi-jin Wu ◽  
Jin-ming Liu ◽  
...  
Keyword(s):  
Schistosoma Japonicum ◽  
Parasite Growth ◽  
Rnai Silencing ◽  
Heat Stable ◽  
Heat Stable Protein

scholarly journals Genome-wide CRISPR/Cas9 screening identifies CARHSP1 responsible for radiation resistance in glioblastoma

2021 ◽  
Vol 12 (8) ◽  
Author(s):  
Guo-dong Zhu ◽  
Jing Yu ◽  
Zheng-yu Sun ◽  
Yan Chen ◽  
Hong-mei Zheng ◽  
...  
Keyword(s):  
Cold Shock ◽  
Mrna Level ◽  
Critical Role ◽  
Inflammatory Signaling ◽  
Heat Stable ◽  
Genome Wide ◽  
Attractive Therapeutic Target ◽  
Heat Stable Protein ◽  
Signaling Activation ◽  
Shock Proteins

AbstractGlioblastomas (GBM) is the most common primary malignant brain tumor, and radiotherapy plays a critical role in its therapeutic management. Unfortunately, the development of radioresistance is universal. Here, we identified calcium-regulated heat-stable protein 1 (CARHSP1) as a critical driver for radioresistance utilizing genome-wide CRISPR activation screening. This is a protein with a cold-shock domain (CSD)-containing that is highly similar to cold-shock proteins. CARHSP1 mRNA level was upregulated in irradiation-resistant GBM cells and knockdown of CARHSP1 sensitized GBM cells to radiotherapy. The high expression of CARHSP1 upon radiation might mediate radioresistance by activating the inflammatory signaling pathway. More importantly, patients with high levels of CARHSP1 had poorer survival when treated with radiotherapy. Collectively, our findings suggested that targeting the CARHSP1/TNF-α inflammatory signaling activation induced by radiotherapy might directly affect radioresistance and present an attractive therapeutic target for GBM, particularly for patients with high levels of CARHSP1.

Regulation of protein kinase by vasopressin in renal medulla in situ

1977 ◽  
Vol 232 (1) ◽  
pp. F50-F57
Author(s):  
T. P. Dousa ◽  
L. D. Barnes
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Kinase Activity ◽  
Kinase Inhibitor ◽  
Renal Medulla ◽  
Protein Kinase Activity ◽  
Kinase Activation ◽  
Heat Stable ◽  
Protein Kinase Activation ◽  
Heat Stable Protein

Results of this study demonstrate that vasopressin activates protein kinase in intact renal medullary cells as detected by measurement of the (-cyclic AMP/+cyclic AMP) protein kinase activity ratios in freshly prepared tissue extracts (40,000 X g supernates) from bovine renal medullary slices. The activation of protein kinase was specific for vasopressin since parathyroid hormone, histamine, angiotensin II, or the inactive analog of vasopressin did not activate protein kinase. There was a direct correlation between the extent of protein kinase activation and the elevation in tissue levels of cyclic AMP elicited by increasing doses of vasopressin or with an increase in incubation time. The elevation of tissue cyclic AMP level and maximum activation of protein kinase reached maximum level at a vasopressin concentration of about 2 X 10(-9) M. Incubation of slices with vasopressin caused a dose-dependent decrease in the cyclic AMP-dependent protein kinase activity in the 40,000 X g supernate of homogenate from the renal medullary slices. This effect of vasopressin was specific for protein kinase since activity of lactate dehydrogenase or a specific [3H]colchicine-binding activity was not affected, and the decrease in the protein kinase was not due to the accumulation of a heat-stable protein kinase inhibitor. There was an increase in protein kinase was not due to the accumulation of a heat-stable protein kinase inhibitor. There was an increase in protein kinase activity extracted from 40,000 X g pellets of homogenate prepared from slices exposed to vasopressin. Results thus provide evidence that cyclic AMP-mediated protein kinase activation in the intact cells is an integral part of cellular response of the mammalian renal medulla to vasopressin.

scholarly journals Milk Protein Fragments Induce the Biosynthesis of Macedocin, the Lantibiotic Produced by Streptococcus macedonicus ACA-DC 198

2009 ◽  
Vol 76 (4) ◽  
pp. 1143-1151 ◽  
Author(s):  
Marina Georgalaki ◽  
Marina Papadelli ◽  
Elina Chassioti ◽  
Rania Anastasiou ◽  
Anastassios Aktypis ◽  
...  
Keyword(s):  
Milk Protein ◽  
Mass Spectrometric ◽  
Partial Purification ◽  
Protein Fragments ◽  
Reverse Transcription Pcr ◽  
Heat Stable ◽  
Heat Stable Protein ◽  
Tandem Mass Spectrometric ◽  
Protein Components ◽  
First Time

ABSTRACT The aim of the present work was to study the mode of the induction of the biosynthesis of macedocin, the lantibiotic produced by Streptococcus macedonicus ACA-DC 198. Macedocin was produced when the strain was grown in milk but not in MRS or M17 broth. No autoinduction mechanism was observed. Production did not depend on the presence of lactose or galactose in the culture medium or on a coculture of the producer strain with macedocin-sensitive or macedocin-resistant strains. Induction seemed to depend on the presence of one or more heat-stable protein components produced when S. macedonicus ACA-DC 198 was grown in milk. The partial purification of the induction factor was performed by a combination of chromatography methods, and its activity was confirmed by a reverse transcription-PCR approach (RT-PCR). Mass spectrometric (MS) and tandem mass spectrometric (MS/MS) analyses of an induction-active fraction showed the presence of several peptides of low molecular mass corresponding to fragments of αS1- and β-casein as well as β-lactoglobulin. The chemically synthesized αS1-casein fragment 37-55 (2,253.65 Da) was proven to be able to induce macedocin biosynthesis. This is the first time that milk protein degradation fragments are reported to exhibit a bacteriocin induction activity.

scholarly journals CaM kinase II regulation of CRHSP-28 phosphorylation in cultured mucosal T84 cells

2003 ◽  
Vol 285 (6) ◽  
pp. G1300-G1309 ◽  
Author(s):  
Kala M. Kaspar ◽  
Diana D. H. Thomas ◽  
William B. Taft ◽  
Eriko Takeshita ◽  
Ning Weng ◽  
...  
Keyword(s):  
Membrane Trafficking ◽  
Apical Membrane ◽  
Digestive Enzyme ◽  
Pancreatic Acinar Cells ◽  
Cellular Mechanisms ◽  
T84 Cells ◽  
Heat Stable ◽  
Heat Stable Protein ◽  
Phosphopeptide Mapping

Ca2+-regulated heat-stable protein of 28 kDa (CRHSP-28; a member of the tumor protein D52 family) is highly expressed in exocrine glands and was shown to regulate digestive enzyme secretion from pancreatic acinar cells. We found CRHSP-28 highly expressed in cultured mucosal secretory T84 cells, consistent with an important regulatory role in apical membrane trafficking. Stimulation of cells with carbachol (CCh) induced rapid, concentration-dependent phosphorylation of CRHSP-28 on at least two serine residues. Isoelectric focusing and immunoblotting were used to characterize cellular mechanisms governing CRHSP-28 phosphorylation. Phosphorylation depends on elevated cellular Ca2+, being maximally induced by ionomycin and thapsigargin and fully inhibited by BAPTAAM. In vitro phosphorylation of recombinant CRHSP-28 was 10-fold greater by casein kinase II (CKII) than Ca2+/calmodulin-dependent protein kinase II (CaMKII). However, phosphopeptide mapping studies demonstrated that CaMKII induced an identical phosphopeptide profile to endogenous CRHSP-28 immunoprecipitated from T84 cells. Although calmodulin antagonists had no effect on CCh-stimulated phosphorylation, disruption of actin filaments by cytochalasin D inhibited phosphorylation by 50%. Confocal microscopy indicated that CRHSP-28 is expressed in perinuclear regions of cells and accumulates immediately below the apical membrane of polarized monolayers following CCh stimulation. CaMKII was also localized to the subapical cytoplasm and was clearly displaced following actin filament disruption. These data suggest that CRHSP-28 phosphorylation is regulated by a CaMKII-like enzyme and likely involves a translocation of the protein within the apical cytoplasm of epithelial cells.

scholarly journals MucR binds multiple target sites in the promoter of its own gene and is a heat‐stable protein: Is MucR a H‐ NS ‐like protein?

FEBS Open Bio ◽  
2018 ◽  
Vol 8 (4) ◽  
pp. 711-718 ◽  
Author(s):  
Ilaria Baglivo ◽  
Luciano Pirone ◽  
Gaetano Malgieri ◽  
Roberto Fattorusso ◽  
Roy Martin Roop II ◽  
...  
Keyword(s):  
Multiple Target ◽  
Heat Stable ◽  
Target Sites ◽  
Heat Stable Protein

Biochemical parameters regulating forward motility initiation in vitro in goat immature epididymal spermatozoa

1998 ◽  
Vol 10 (4) ◽  
pp. 299 ◽  
Author(s):  
Bijay S. Jaiswal ◽  
Gopal C. Majumder
Keyword(s):  
Cyclic Amp ◽  
Sperm Motility ◽  
Biochemical Parameters ◽  
Vital Role ◽  
Dependent Manner ◽  
Alkaline Ph ◽  
Heat Stable ◽  
Heat Stable Protein ◽  
Dose Dependent

An investigation was carried out to analyse the biochemical parameters influencing forward motility (FM) initiation in vitro in the goat caput-epididymal immature spermatozoa. Forward motility was induced in approximately 55% of caput-sperm upon incubation in an alkaline (pH 8.0) modified Ringer’s solution containing theophylline (30 mM) (an inhibitor of cyclic AMP phosphodiesterase), dialysed epi-didymal plasma (EP) and bicarbonate. Both EP and bicarbonate induced sperm motility in a dose-dependent manner, and at saturating doses EP (0.6 mg protein mL–1) and bicarbonate (25 mM) induced FM in approx-imately 38% and 44% of the cells, respectively. The motility-promoting efficacy of EP was attributed to a heat-stable protein termed ‘forward motility protein’ (FMP). Bicarbonate served as an initiator as well as a stabilizer of FM and its action was not dependent on FMP. FMP can induce FM in the caput-sperm, but it is not essential for sperm motility initiation. Alteration of the medium pH from 6.60 to 8.00 caused a marked increase in the EP or bicarbonate-dependent sperm FM initiation, as well as intrasperm pH. At the physio-logical pH, bicarbonate served as a much more potent motility activator than FMP, although both the motility promoters showed maximal efficacy at alkaline pH (~7.8). EP as well as bicarbonate elevated the intrasperm cyclic AMP level. Unlike EP, bicarbonate is capable of increasing intrasperm pH. The intrasperm pH increased from 6.54 0.02 to 6.77 0.03 during sperm transit from caput to cauda. The data are con-sistent with the view that FMP activates sperm forward motility by enhancing the intrasperm cyclic AMP level and that extracellular bicarbonate and pH play a vital role in the initiation of sperm FM during the epi-didymal transit.

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