scholarly journals Diagnostic Markers for Tuberculosis Ascites: A Preliminary Study

2010 ◽  
Vol 5 ◽  
pp. BMI.S5196 ◽  
Author(s):  
Rajpal S. Kashyap ◽  
Sonali M. Saha ◽  
Khushboo J. Nagdev ◽  
Sanjeevani S. Kelkar ◽  
Hemant J. Purohit ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Immunoblot Analysis ◽  
Specific Protein ◽  
Diagnostic Markers ◽  
Enzyme Linked Immunosorbent Assay ◽  
Protein Markers ◽  
Heat Shock Protein 65 ◽  
Major Factors

Objective The diagnosis of tuberculosis (TB) ascites is problematic. Delay in the diagnosis and treatment of TB ascites are considered to be major factors that contribute to the high mortality of TB. This study identifies specific protein markers in ascitic fluid which will be useful in diagnosis of TB ascites. Methods We used Two-Dimensional Electrophoresis, liquid chromatography-mass spectrometry/mass spectrometry, immunoblot analysis and Enzyme Linked Immunosorbent assay (ELISA) as a comprehensive quantitative proteomic screening system for the diagnosis of TB ascites. Results The screen identified several antigens of interest: a 30-kilodalton (kDa) protein that demonstrated significant homology to the antigen 85B and 85C (Ag 85) complex; a 65-kDa protein that corresponded to Mycobacterium tuberculosis (MTB) heat shock protein 65 (65-kDa HSP), Rv0440; a 14-kDa protein and 71-kDa protein that exhibits an amino acid sequence identical to that of MTB heat shock protein 14 (14-kDa HSP), GroES; and MTB heat shock protein 71 (71-kDa HSP), Rv0350 respectively. ELISA confirmed that TB ascites patients were consistently positive for these antigens at higher rates than non-TB ascites patients. Conclusion The 65-kDa HSP, 71-kDa HSP, 14-kDa HSP and Ag 85 complex proteins may serve as very useful diagnostic markers for TB ascites.

Oral Tolerization with Mycobacterial Heat Shock Protein 65 Reduces Chronic Experimental Atherosclerosis in Aged Mice

Gerontology ◽  
2017 ◽  
Vol 64 (1) ◽  
pp. 36-48 ◽  
Author(s):  
Cecilia Wick ◽  
Elisabeth Onestingel ◽  
Egon Demetz ◽  
Hermann Dietrich ◽  
Georg Wick
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
T Regulatory Cells ◽  
Stress Protein ◽  
Experimental Atherosclerosis ◽  
Chronic Inflammatory Disease ◽  
Enzyme Linked Immunosorbent Assay ◽  
High Cholesterol Diet ◽  
Normal Chow ◽  
Heat Shock Protein 65

Background: Atherosclerosis is a chronic inflammatory disease of the artery wall where both innate and adaptive immunity play important roles. Modulation of the immune response against the stress protein antigen, heat shock protein (HSP) 60, by administration of mycobacterial HSP65 (mbHSP65) orally and/or nasally shows promising therapeutic results in young animals in the sense of less severe experimental atherosclerosis; however, the case of aged animals with already established atherosclerosis has so far never been investigated. Objective: To investigate if mbHSP65 immunization would further accelerate atherosclerotic progression in aged ApoE-/- mice (18 months old) with already long-established atherosclerosis and if these mice could be orally tolerized against mbHSP65. Methods: Aged wild-type (WT) and ApoE-/- mice (65 weeks) were immunized and/or orally treated with mbHSP65 and then either kept on normal chow or changed to high-cholesterol diet (HCD). Atherosclerosis was assessed by en face analysis and the number of CD4+CD25+FoxP3+ T regulatory cells (Tregs) was assessed by flow cytometry in lymph node and spleen cells. Total cholesterol and triglyceride levels were determined. Soluble mammalian HSP60 and anti-mouse HSP60 (mHSP60) and anti-mbHSP65 antibodies were detected by enzyme-linked immunosorbent assay. Results: As expected, aged WT mice had only minor lesions in the aorta, which did not change under HCD for 14 weeks. Aged ApoE-/- mice already had large complicated plaques, which increased in size under HCD. mbHSP65 immunization led to a significant aggravation of atherosclerosis in both WT and ApoE-/- mice irrespective of the nature of their diet. This increase was accompanied by increased titers of both anti-mHSP60 and anti-mbHSP65 antibodies in the circulation. The increased plaque formation could be significantly diminished with oral mbHSP65 tolerization. An increased number of Tregs and lower or unchanged levels of cholesterol and triglycerides were associated with the reduced size of aortal lesions. Conclusion: Oral tolerization against mbHSP65 could be used both to prevent and to treat chronic atherosclerosis in aged individuals.

Inhibition of Vesicular Stomatitis Virus Replication by Prostaglandin A1 in Aedes albopictus Cells

2004 ◽  
Vol 59 (1-2) ◽  
pp. 127-131 ◽  
Author(s):  
Fernanda M. Burlandy ◽  
Davis F. Ferreira ◽  
Moacyr A. Rebello
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Vesicular Stomatitis Virus ◽  
Aedes Albopictus ◽  
Virus Production ◽  
Immunoblot Analysis ◽  
Specific Protein ◽  
Mammalian Cell Lines ◽  
Vesicular Stomatitis ◽  
Prostaglandin A1

Cyclopentenone prostaglandins (PGs) exhibit antiviral activity against RNA and DNA viruses in mammalian cell lines, and this effect has been associated with the induction of a heat shock protein (hsp70). We investigated the effect of prostaglandin A1 (PGA1) on the replication of vesicular stomatitis virus (VSV) in Aedes albopictus (mosquito) cells. PGA1 was found to inhibit VSV replication dose dependently. Virus yield was reduced to 50% (3 μg PGA1/ml) and to 95% with 8 μg PGA1/ml. Even with the dramatic reduction of virus production observed in cells treated with PGA1, VSV-specific protein synthesis was unaltered. Treatment of cells with PGA1 (5 μg/ml) stimulated the synthesis of a polypeptide identified as a heat-shock protein (hsp) by immunoblot analysis. PGA1 induced hsp70 synthesis in uninfected cells. However, in VSV-infected cells the induction of hsp70 by PGA1 was reduced. This is the first report of antiviral effects of PGs affecting the replication of VSV in a mosquito cell line.

Epitope Specificity of Anti–Heat Shock Protein 65/60 Serum Antibodies in Atherosclerosis

1997 ◽  
Vol 17 (3) ◽  
pp. 536-541 ◽  
Author(s):  
Bernhard Metzler ◽  
Georg Schett ◽  
Roman Kleindienst ◽  
Ruurd van der Zee ◽  
Tom Ottenhoff ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Serum Antibodies ◽  
Epitope Specificity ◽  
Heat Shock Protein 65

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.

A Th2 immune shift to heat shock protein 65 fails to arrest atherosclerosis: Proatherogenic role of Th2-deviated autoantibodies

Autoimmunity ◽  
2009 ◽  
Vol 42 (6) ◽  
pp. 475-483 ◽  
Author(s):  
Qiyan Xiong ◽  
Liang Jin ◽  
Jianping Li ◽  
Hao Fan ◽  
Rongyue Cao ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 65

scholarly journals Mycobacterial heat shock protein 65 mediated metabolic shift in decidualization of human endometrial stromal cells

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Elavarasan Subramani ◽  
Arun Prabhu Rameshbabu ◽  
Manivannan Jothiramajayam ◽  
Bhuvaneshwaran Subramanian ◽  
Debangana Chakravorty ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Stromal Cells ◽  
Metabolic Shift ◽  
Endometrial Stromal Cells ◽  
Heat Shock Protein 65

scholarly journals Ribosome Profiling Reveals HSP90 Inhibitor Effects on Stage-Specific Protein Synthesis in Leishmania donovani

mSystems ◽  
2018 ◽  
Vol 3 (6) ◽  
Author(s):  
Eugenia Bifeld ◽  
Stephan Lorenzen ◽  
Katharina Bartsch ◽  
Juan-José Vasquez ◽  
T. Nicolai Siegel ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Leishmania Donovani ◽  
Specific Protein ◽  
Ribosome Profiling ◽  
Severe Illness ◽  
Content Type ◽  
Hsp90 Activity

ABSTRACT The 90-kDa heat shock protein (HSP90) of eukaryotes is a highly abundant and essential chaperone required for the maturation of regulatory and signal proteins. In the protozoan parasite Leishmania donovani, causative agent of the fatal visceral leishmaniasis, HSP90 activity is essential for cell proliferation and survival. Even more importantly, its inhibition causes life cycle progression from the insect stage to the pathogenic, mammalian stage. To unravel the molecular impact of HSP90 activity on the parasites’ gene expression, we performed a ribosome profiling analysis of L. donovani, comparing genome-wide protein synthesis patterns in the presence and absence of the HSP90-specific inhibitor radicicol and an ectopically expressed radicicol-resistant HSP90 variant. We find that ribosome-protected RNA faithfully maps open reading frames and represents 97% of the annotated protein-coding genes of L. donovani. Protein synthesis was found to correlate poorly with RNA steady-state levels, indicating a regulated translation as primary mechanism for HSP90-dependent gene expression. The results confirm inhibitory effects of HSP90 on the synthesis of Leishmania proteins that are associated with the pathogenic, intracellular stage of the parasite. Those include heat shock proteins, redox enzymes, virulence-enhancing surface proteins, proteolytic pathways, and a complete set of histones. Conversely, HSP90 promotes fatty acid synthesis enzymes. Complementing radicicol treatment with the radicicol-resistant HSP90rr variant revealed important off-target radicicol effects that control a large number of the above-listed proteins. Leishmania lacks gene-specific transcription regulation and relies on regulated translation instead. Our ribosome footprinting analysis demonstrates a controlling function of HSP90 in stage-specific protein synthesis but also significant, HSP90-independent effects of the inhibitor radicicol. IMPORTANCE Leishmania parasites cause severe illness in humans and animals. They exist in two developmental stages, insect form and mammalian form, which differ in shape and gene expression. By mapping and quantifying RNA fragments protected by protein synthesis complexes, we determined the rates of protein synthesis for >90% of all Leishmania proteins in response to the inhibition of a key regulatory protein, the 90-kDa heat shock protein. We find that Leishmania depends on a regulation of protein synthesis for controlling its gene expression and that heat shock protein 90 inhibition can trigger the developmental program from insect form to mammalian form of the pathogen.

Heat — Shock protein 65 — But not cholesterol-induced arteriosclerotic lesions regress in rabbit aortae

1995 ◽  
Vol 115 ◽  
pp. S64
Author(s):  
R. Kleindienst ◽  
Q. Xu ◽  
G. Schett ◽  
H. Dietrich ◽  
G. Wick
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 65
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