Peranan Heat Shock Protein Pada Patogenesis Penyakit Infeksi Dan Penyakit Autoimun

Heat shock proteins (Hsp)merupakan suatu chaperones yang tersebar luas dalam sel manusia maupun patogen, yang penting sebagai salah satu sarana untuk beradaptasi terhadap Perubahan lingkungan hidupnya. Semua patogen akan meningkatkan produksi Hsp-nya selama proses infeksi dan akan terdeteksi sebagai antigen oleh sistem imun manusia. Sehingga akan memicu respons imun yang kuat Hsp juga terlibat dalam proses patologis lain misalnya proses autoimun, karena ternyata Hsp manusia dan patogen sangatlah mirip. Sel T dapat mengenali kehadiran Hsp patogen, namun dapat pula bereaksi silang dengan self-Hsp yang mirip dengan Hsp patogen, yang kemudian menyebabkan terjadinya penyakit autoimun. Dapat dikatakan bahwa Hsp patogen merupakan antigen yang lebih penting dari antigen yang lain untuk sistem imun manusia dan memegang peranan penting dalam patogenesis pada penyakit infeksi dan penyakit autoimun tertentu

The Expression of Heat Shock Protein (Hsp) 25 at Compression and Tension Area DuringAlveolar Bone Remodeling

The activation of orthodontic appliance will generate mechanical force. This forceis used to depress tooth and the tissues surrounding it then stimulates alveolarbone remodeling. Alveolar bone remodeling is divided into compression andtension area. This stress becomes a signal to activate heat shock responseyielding heat shock protein (HSP) synthesis, especiallyhsp25isessentialforalveolarboneremodelingprocessitself. The aim of this study was to comparehsp25 expression in compression and tension areas. This study using Guinea pigsmandibular first insicivus that given a mechanical force to see hsp25 expressionin both areas. The HSP25 expressionwas measured by counting this protein afterbeing conducted by immunohystochemistry method. It is analysed statisticallywith one way Anova with level of significant p = 0,05

Kajian Heat Shock Protein 90 (HSP90) Dalam Pencarian Kandidat Penghambatnya Melalui Ekplorasi Bahan Alam Indonesia: Review on Heat Shock Protein 90 (HSP90) for Exploration of Its Inhibitor Candidates Through Indonesian Natural Resources

Exploration on anticancer candidates on inhibition of Heat Shock Protein (HSP) activity are increasing in the past ten years. Some of HSP90 inhibitor candidates were in third phase of clinical trials. However, this issue is not followed by the emergency of HSP90 inhibitor research in Indonesia, not only study on natural source but also on synthetic candidates. This study aims to look the development of tracking HSP90 inhibitor candidates globally so that it can initiate the related research in Indonesia. Study of HSP90 and its inhibitors were taken from scientific articles in the range from 2009 to 2018. HSP90 and its inhibitors have important values in the dynamics of functions and stability of proteins to maintain survival of cells. This also include the oncogene proteins that involve in cell proliferation such as tyrosine kinases, transcription factors, and regulatory proteins that expression and interaction depend on HSP90. Expression of the transcription factor p53, Alk gene, Wnt gene, glucocorticoid receptors have also links with HSP90 protein activity. Some candidates for inhibitor of HSP90 have been entering clinical trials such as geldanamycin analogues, resorcinol derivatives, and purines analog. Candidates from natural sources that are also being developed such as luteolin, licochalcone A, oleochantal, novobiocin, epigallocathecin gallat, silybin, deguelin, and celastrol from terpenoid class, Apigenin from flavon class, Curcumin, and  Gambogat Acid. HSP90 inhibitors which are entering the third phase of clinical trial are ganetespib from the resorcinol derivative and retaspimycin from geldanamisin analog group. Exploration of HSP90 inhibitors from Indonesia natural resources still have great potential to be developed because they have high impact values as anticancer candidates

METHODS AND COMPOSITIONS FOR PROTECTION AGAINST BOVINE VIRAL DISEASES

The present invention relates to methods and compositions for eliciting an immune response against bovine viral epitopes. The methods comprise combining at least one heat shock protein with at least one bovine viral epitope to form a purified epitope/heat shock protein complex and administration of an immune system stimulating amount of the purified epitope/heat shock protein complex. The compositions comprise, a purified epitope/heat shock protein complex comprising at least one bovine viral epitope complexed with at least one heat shock protein, and a pharmaceutically acceptable carrier, diluent or excipient

Self-degradation of heat shock proteins

The 70-kDa heat shock protein of Drosophila decays in vivo at a much faster rate than other abundantly labeled proteins. Degradation also occurs in vitro, even during electrophoresis. It appears that this degradation is not mediated by a general protease and that the 70-kDa heat shock protein has a slow proteolytic action upon itself. Heat-induced proteins in CHO cells and a mouse cell line also degrade spontaneously in vitro, as do certain non-heat shock proteins from Drosophila tissues as well as the cell lines

Phosphorylation and translocation of heat shock protein 27 and αB-crystallin in human myocardium after cardioplegia and cardiopulmonary bypass

ObjectivesCardiac surgery using cardioplegia and cardiopulmonary bypass subjects myocardium to hypothermic reversible ischemic injury that can impair cardiac function. Research in animal and cell models demonstrates that acute myocardial ischemia/reperfusion injury causes phosphorylation of heat shock protein 27 and αB-crystallin. Phosphorylation of heat shock protein 27 and αB-crystallin is implicated in the regulation of both beneficial and detrimental responses to ischemic injury. The phosphorylation status of these proteins in human myocardium after ischemic insults associated with cardioplegia and cardiopulmonary bypass is unknown.MethodsRight atrial appendage and chest wall skeletal muscle samples were collected from patients before and after cardioplegia and cardiopulmonary bypass. Cardioplegia and cardiopulmonary bypass-induced changes in phosphorylation and localization of heat shock protein 27 and αB-crystallin were determined using immunoblot and confocal microscopy with total and phospho-specific antibodies.ResultsCardioplegia and cardiopulmonary bypass increased the phosphorylation of heat shock protein 27 on serine 15, 78, and 82, and αB-crystallin on serine 59 and 45, but not serine 19. The majority of heat shock protein 27 and αB-crystallin localized to I-bands of cardiac myofilaments and shifted to a detergent insoluble fraction after cardioplegia and cardiopulmonary bypass. Cardioplegia and cardiopulmonary bypass–induced phosphorylation of specific heat shock protein 27 and αB-crystallin residues were associated with additional subcellular locations. Increases in phosphorylation of heat shock protein 27 and αB-crystallin were negatively correlated with cardiac function after surgery.ConclusionCardiac surgery using cardioplegia and cardiopulmonary bypass is associated with phosphorylation and myofilament translocation of heat shock protein 27 and αB-crystallin in human myocardium. Phosphorylation of specific heat shock protein 27 and αB-crystallin serine residues is associated with distinct localization. Understanding the human myocardial small heat shock protein response may have significant implications for surgical myocardial protection

cDNA cloning and mRNA expression of heat shock protein 70 gene in blood clam Tegillarca granosa against heavy metals challenge

In this study, the full-length heat shock protein 70 of Tegillarca granosa was cloned from cDNA library by rapid amplification of cDNA end (RACE). The open reading frame (ORF) of heat shock protein 70 was 1968 bp, and it encoded a protein of 655 amino acids with a predicted molecular weight of 71.48 kDa and an isoelectric point of 5.25. Basic local alignment search tool (BLAST) analysis showed that the heat shock protein 70 of T. granosa shared high similarity with other species, supporting that it is a new member of heat shock protein family. Western blot analysis revealed that the generated polyclonal antibodies could specially detect native protein from whole cell lysate of T. granosa. The spatial distribution confirmed that the heat shock protein 70 was abundant in visceral mass, gill and haemocytes, and weakly in foot, mantle and adductor. Heavy metal pollutes such as lead (Pb2+), cadmium (Cd2+) and copper (Cu2+) could induce the gene expression in similar manners by quantitative real-time polymerase chain reaction (PCR). The present results indicate that heat shock protein 70 of T. granosa may be involved in environmental pollution challenges and should be considered as one of T. granosa promising molecular marker candidates.Keywords: Tegillarca granosa, heat shock protein 70, heavy metals, quantitative real-time polymerase chain reaction (PCR) African Journal of Biotechnology Vol. 12(18), pp. 2341-235

Immunotherapeutic targeting of membrane Hsp70-expressing tumors using recombinant human granzyme B

Background: We have previously reported that human recombinant granzyme B (grB) mediates apoptosis in membrane heat shock protein 70 (Hsp70)-positive tumor cells in a perforin-independent manner

The Expression of Heat Shock Protein 70 Gene with Organic Selenium Supplementation and Its Effetc on Productivity of Broilers in Tropical Environment

The purpose of this experiment is to study the effect of organic selenium (Se) supplementation on the expression of heat shock protein 70 gene (HSP70), glutathione peroxidase (GSH-Px) enzyme activity, malondialdehyde (MDA) and productivity of broilers in tropical environment. Three kinds of environmental pens were designed in this experiment: comfortable environment pens with temperature of air conditioner adjusted at 22oC (R0), tropical environment pens (±30oC ) without organic Se (R1), and tropical environment pens supplemented with 0.30 ppm organic Se (R2). One hundred and twenty broiler chickens (unisex) were used in this study. There were 40 chicks per pen for each treatment. The experimental design was completely randomized with four replications for each treatment. The data were statistically analyzed using the general linear model of SAS program. Results showed that R0 and R2 groups had significantly increased (P<0.05) feed intake, body weight, body weight gain, and decreased feed conversion ratio compared to R1 groups. Meanwhile, the expression of HSP70, GSH-Px enzyme activity and MDA of R2 groups and R0 groups were significantly lower (P<0.05) than that of R1 groups. It was concluded that the broilers given 0.30 ppm organic Se in tropical environment had similar productivity and expression of HSP 70 with broilers kept in comfortable environment

Sleep deprivation increase the expression of inducible heat shock protein 70 in rat gastric mucosa

Aim: To investigate if sleep deprivation is able to increase the expression of inducible heat shock protein 70 in gastric mucosa and its possible role in mucosal defense. Methods: Rats for sleep disruption were placed inside a computerized rotating drum, gastric mucosa was taken from rats with 1, 3 and 7 d sleep deprivation. RT-PCR, immunohistochemistry and Western blotting were used to determine the expression of heat shock protein 70. Ethanol (500 mL.L-1, i.g.) was used to induce gastric mucosa damage. Results: RT-PCR, Western blotting and immunostaining confirmed that the sleep deprivation as a stress resulted in significantly greater expression of inducible heat shock protein 70 in gastric mucosa of rats. After the 500mL.L-1 ethanol challenge, the ulcer area found in the rats with 7 d sleep deprivation (19.15 ± 4.2) mm2 was significantly lower (P<0.01) than the corresponding control (53.7 ± 8.1) mm2. Conclusion: Sleep deprivation as a stress, in addition to lowering the gastric mucosal barrier, is able to stimulate the expression of inducible heat shock protein 70 in gastric mucosa of rats, the heat shock protein 70 may play an important role in gastric mucosal protection.published_or_final_versio