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Mechanism of Action of Chaperones in Protein Function

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Adio W. S., Obunadike C. V., Ogunsanmi A. O.
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vol. 44
333-354
EN
The building blocks of living cells, proteins are enormous collections of nitrogenous organic molecules that are polymers of the amino acids that animals must consume to grow and repair their tissues. ATP-dependent proteins known as chaperones serve as foldases (protein folding assistants), holdases (bind folding intermediates), and disaggregates (convert aberrant protein to monomers). Chaperones include, but are not limited to, DnaJ, DnaK, GrpE, and Hsp33. The majority of chaperones have a cleft containing the nucleotide-binding site that divides the ATPase domain into two subdomains. The features of the C-terminal domain depend on the kind of bound nucleotide. In the presence of ATP, peptides bind and dissociate quickly and with low affinity. In contrast, the affinity increases significantly while the rate of peptide binding reduces when neither ADP nor nucleotide are connected to the N-terminal domain. Hsp90 is a homodimer with a 60 n dissociation constant. In reaction to high temperature or other types of cellular stress that prevent protein folding, several chaperones turn on their activity. Neurodegenerative, Parkinson's, and polyQ diseases, among others, can all be treated with chaperones. This is possible when a protein prevents the accumulation of protein species with improper folding. The suppression of dangerous protein oligomers by clustering, illness response related to protein aggregation, and cancer maintenance are a few new functions for chaperones that are still being discovered.
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Increased levels of antibodies against heat shock proteins in stroke patients

72%
Banecka-Majkutewicz Z., Grabowski M., Kadziński L., Papkov A., Węgrzyn A., Banecki B.
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EN
Ischemic stroke is the second leading cause of death worldwide. One of the main risk factors of the ischemic stroke is atherosclerosis which is a chronic inflammatory and immune-mediated disease. Bacterial infections generate specific human antibodies against various antigens, including Hsps. It has been demonstrated that Hsps are selectively overexpressed in the atherosclerotic lesions. The amino acid sequence homology between human and bacterial Hsps may lead to an autoimmune response by immunological cross-reaction. Such immune response against Hsps overexpressed in the blood vessels under stressful conditions may contribute to inflammatory processes and subsequent development of atherosclerosis. In this study we determined the antibody levels against bacterial and human Hsp by ELISA in blood plasma obtained from stroke patients. Using ANOVA we analyzed levels of Hsp-antibodies in control and patient groups and correlate them with several stroke risk factors. The group of stroke patients had elevated levels of anti-Hsp antibodies compared to the control group. We also discovered an antibody level increase in patients that previously underwent another stroke. Our data provide evidence that autoimmunity could underlie formation of atherosclerosis plaque leading to stroke.
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