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Wyświetlanie 1-8 z 8
Tytuł:
Expression of heat shock protein 70 in the tissue of patients with laryngeal squamous cell carcinoma
Autorzy:
Barańska, Aleksandra
Maziarz, Aleksandra
Roliński, Jacek
Klatka, Janusz
Dudzińska-Ćwiek, Katarzyna
Tabarkiewicz, Jacek
Powiązania:
https://bibliotekanauki.pl/articles/454793.pdf
Data publikacji:
2019
Wydawca:
Uniwersytet Rzeszowski. Wydawnictwo Uniwersytetu Rzeszowskiego
Tematy:
HSP70
LSCC
treatment
Opis:
Introduction. Laryngeal squamous cell carcinoma (LSCC) is a common type of head and neck malignancy. Because of unsatisfactory results of therapy, development of new strategies for LSCC treatment is needed. It is believed that heat shock protein 70 (HSP70) is involved in pathogenesis of LSCC. Thus, targeting HSP70 seems to be promising strategy for laryngeal cancer treatment. Aim. The aim of the study was to assess the HSP70 concentration in laryngeal squamous cell carcinoma specimens and its correlation with tumor volume and TNM staging. Material and methods. An ELISA method and a Bradford protein assay were used to evaluate the HSP70 concentration in peripheral blood cells, tumor tissue and lymph nodes from the patients suffering from LSCC. Results. We demonstrated that the HSP70 concentration is significantly different between examined compartments. The highest level was observed in peripheral blood, while the lowest was in the lymph nodes. The HSP70 expression was correlated to tumor volume. Conclusion. Our results showed varied expression of HSP70 in tissue from patients with LSCC, but there was no association between HSP70 concentration and TNM staging. Currently, application of HSP70 inhibition as a LSCC treatment could be rather associated with systemic blocking of this molecule than target inhibition in tumor tissue. However, further analysis on a larger group of patients is needed.
Źródło:
European Journal of Clinical and Experimental Medicine; 2019, 1; 16-21
2544-2406
2544-1361
Pojawia się w:
European Journal of Clinical and Experimental Medicine
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Exercise training-induced changes in inflammatory mediators and heat shock proteins in canoeists
Autorzy:
Morawin, Barbara
Rynkiewicz, Mateusz
Orysiak, Joanna
Rynkiewicz, Tadeusz
Zembroń-Łacny, Agnieszka
Powiązania:
https://bibliotekanauki.pl/articles/1054611.pdf
Data publikacji:
2014
Wydawca:
Uniwersytet Szczeciński. Wydawnictwo Naukowe Uniwersytetu Szczecińskiego
Tematy:
HSP27
HSP70
cytokines
inflammation
muscle damage
Opis:
According to cytokine overtraining theory, skeletal muscle injuries are related to systemic inflammatory reaction. In response to inflammation, cells rapidly produce a series of proteins known as heat shock proteins (HSPs).These are considered to be molecular chaperones which play a universal role in maintaining cellular homeostasis. Among the subset of stress-responsive proteins, HSP27 and HSP70 are considered to be a new approach to monitoring exercise training and adaptive mechanisms. The study was designed to demonstrate the effect of sport training on changes in pro-inflammatory cytokines and HSPs, and their relation with muscle damage and body composition. Six elite canoeists (19.8 ±2.9 yr) were observed during preparatory training period (March) at the 1st, the 4th and after 7 days of the conditioning camp, and then after 3 days of recovery. The canoeing training did not induce muscle damage, decreased in IL-1β and HSP27, increased in TNFα and HSP70 concentrations. The highest changes in TNFα and HSP70 were observed 3 days after conditioning camp (during recovery) compared to initial level (the 1st day of conditioning camp). TNFα correlated with HSP27 (r = –0.563; P < 0.01) and HSP70 (r = 0.651; P < 0.001). Any significant changes in body composition were not observed. In conclusion, we could say that typical canoeing training improves cytokines and HSPs release, however, the changes are not related to muscle damage.
Źródło:
Central European Journal of Sport Sciences and Medicine; 2014, 8, 4; 27-34
2300-9705
2353-2807
Pojawia się w:
Central European Journal of Sport Sciences and Medicine
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Increased levels of antibodies against heat shock proteins in stroke patients
Autorzy:
Banecka-Majkutewicz, Zyta
Grabowski, Michał
Kadziński, Leszek
Papkov, Aliaksei
Węgrzyn, Alicja
Banecki, Bogdan
Powiązania:
https://bibliotekanauki.pl/articles/1039307.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
HSP
Heat Shock Proteins
Stroke
DnaK
DnaJ
GroEL
Hsp70
ELISA
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2014, 61, 2; 379-383
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Role of heat-shock proteins and cobalamine in maintaining methionine synthase activity
Autorzy:
Grabowski, Michał
Banasiuk, Rafał
Węgrzyn, Alicja
Kędzierska, Barbara
Lica, Jan
Banecka-Majkutewicz, Zyta
Banecki, Bogdan
Powiązania:
https://bibliotekanauki.pl/articles/1039633.pdf
Data publikacji:
2012
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
vitamin B12
HtpG
cobalamine
HSP
methionine syntase (MetH)
Hsp 70/100
Opis:
Atheromatous plaque is one of the most common cardiovascular-related diseases. Reports show a connection between its development and the levels of homocysteine. In pathological states high levels of homocysteine in the organism can be caused by the malfunction of the methionine synthase pathway. Bacterial methionine synthase (MetH) is a homologue of the human methionine syntase (MS). In this study we aimed to investigate the functional relations between MetH and its cofactor - cobalamine - under stress conditions. We have demonstrated that heat shock proteins (Hsp 70/100 system or HtpG) can protect MetH activity under stress conditions. Moreover, in the presence of cobalamine they can restore the activity of partially denatured methionine synthase.
Źródło:
Acta Biochimica Polonica; 2012, 59, 4; 489-493
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The DnaK chaperones from the archaeon Methanosarcina mazei and the bacterium Escherichia coli have different substrate specificities
Autorzy:
Żmijewski, Michal
Skórko-Glonek, Joanna
Tanfani, Fabio
Banecki, Bogdan
Kotlarz, Agnieszka
Macario, Alberto
Lipińska, Barbara
Powiązania:
https://bibliotekanauki.pl/articles/1040934.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
archaeal DnaK quaternary structure
archaeal Hsp70(DnaK)
substrate-binding by archaeal DnaK
Opis:
Hsp70 (DnaK) is a highly conserved molecular chaperone present in bacteria, eukaryotes, and some archaea. In a previous work we demonstrated that DnaK from the archaeon Methanosarcina mazei (DnaKMm) and the DnaK from the bacterium Escherichia coli (DnaKEc) were functionally similar when assayed in vitro but DnaKMm failed to substitute for DnaKEc in vivo. Searching for the molecular basis of the observed DnaK species specificity we compared substrate binding by DnaKMm and DnaKEc. DnaKMm showed a lower affinity for the model peptide (a-CALLQSRLLS) compared to DnaKEc. Furthermore, it was unable to negatively regulate the E. coli σ32 transcription factor level under heat shock conditions and poorly bound purified σ32, which is a native substrate of DnaKEc. These observations taken together indicate differences in substrate specificity of archaeal and bacterial DnaKs. Structural modeling of DnaKMm showed some structural differences in the substrate-binding domains of DnaKMm and DnaKEc, which may be responsible, at least partially, for the differences in peptide binding. Size-exclusion chromatography and native gel electrophoresis revealed that DnaKMm was found preferably in high molecular mass oligomeric forms, contrary to DnaKEc. Oligomers of DnaKMm could be dissociated in the presence of ATP and a substrate (peptide) but not ADP, which may suggest that monomer is the active form of DnaKMm.
Źródło:
Acta Biochimica Polonica; 2007, 54, 3; 509-522
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Regulatory effects of 1,25-dihydroxyvitamin D3 on vascular smooth muscle cells
Autorzy:
Tukaj, Stefan
Trzonkowski, Piotr
Tukaj, Cecylia
Powiązania:
https://bibliotekanauki.pl/articles/1039718.pdf
Data publikacji:
2012
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
IκB-α
TNF-α
calcitriol
HSP70
NF-κB
IL-6
vitamin D
VSMC
Opis:
Inflammatory response has been recognized as a central feature in the development and progression of atherosclerosis, and VSMCs (Vascular Smooth Muscle Cells) - the main cellular component of media, play an important role in this process. Many reports indicate that the biologically active vitamin D metabolite - 1,25-dihydroxyvitamin D3 (1,25(OH)2D3 = calcitriol), besides its well established role in calcium homeostasis, plays an essential role in the regulation of the inflammation process. The aim of this study was to determine the regulatory effects of calcitriol, applied at two supra-physiological doses (10 nM and 100 nM), in VSMC culture. Secretion of the pro-inflammatory cytokines, IL-6 and TNF-α, was significantly attenuated in calcitriol-treated VSMC culture, but the level of anti-inflammatory TGF-β was generally unchanged. Since in advanced atherosclerosis lesions several cell types, including VSMCs, overproduce the HSP70 chaperone protein, we also checked the effects of calcitriol on its synthesis. The presence of 1,25(OH)2D3 did not affect HSP70 synthesis under physiological conditions but the synthesis of HSP70 in VSMCs exposed to heat shock was significantly inhibited by calcitriol (=100 nM). We observed that 1,25(OH)2D3 induced SOD 1 activity, stimulated the expression of IκB-α, and did not influence the level of NF-κB-p65 in VSMCs. The results of our study suggest that 1,25(OH)2D3 may serve as a natural anti-inflammatory agent and may therefore play a beneficial role in the physiology of VSMC in some contexts of atherosclerosis.
Źródło:
Acta Biochimica Polonica; 2012, 59, 3; 395-400
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Structural basis of the interspecies interaction between the chaperone DnaK(Hsp70) and the co-chaperone GrpE of archaea and bacteria
Autorzy:
Żmijewski, Michał
Skórko-Glonek, Joanna
Tanfani, Fabio
Banecki, Bogdan
Kotlarz, Agnieszka
Macario, Alberto
Lipińska, Barbara
Powiązania:
https://bibliotekanauki.pl/articles/1041069.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
substrate-binding domain
DnaK-GrpE complex
archaeal Hsp70(DnaK)
archaeal DnaK structure
molecular chaperones
ATPase domain
Opis:
Hsp70s are chaperone proteins that are conserved in evolution and present in all prokaryotic and eukaryotic organisms. In the archaea, which form a distinct kingdom, the Hsp70 chaperones have been found in some species only, including Methanosarcina mazei. Both the bacterial and archaeal Hsp70(DnaK) chaperones cooperate with a GrpE co-chaperone which stimulates the ATPase activity of the DnaK protein. It is currently believed that the archaeal Hsp70 system was obtained by the lateral transfer of chaperone genes from bacteria. Our previous finding that the DnaK and GrpE proteins of M. mazei can functionally cooperate with the Escherichia coli GrpE and DnaK supported this hypothesis. However, the cooperation was surprising, considering the very low identity of the GrpE proteins (26%) and the relatively low identity of the DnaK proteins (56%). The aim of this work was to investigate the molecular basis of the observed interspecies chaperone interaction. Infrared resolution-enhanced spectra of the M. mazei and E. coli DnaK proteins were almost identical, indicating high similarity of their secondary structures, however, some small differences in band position and in the intensity of amide I' band components were observed and discussed. Profiles of thermal denaturation of both proteins were similar, although they indicated a higher thermostability of the M. mazei DnaK compared to the E. coli DnaK. Electrophoresis under non-denaturing conditions demonstrated that purified DnaK and GrpE of E. coli and M. mazei formed mixed complexes. Protein modeling revealed high similarity of the 3-dimensional structures of the archaeal and bacterial DnaK and GrpE proteins.
Źródło:
Acta Biochimica Polonica; 2007, 54, 2; 245-252
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The application of in vitro cattle embryo production system to study the influence of elevated temperature on oocyte maturation, fertilization and early embryonic development
Autorzy:
Rynkowska, A.
Rapala, L.
Trzeciak, P.
Duszewska, A.M.
Powiązania:
https://bibliotekanauki.pl/articles/80225.pdf
Data publikacji:
2011
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
antioxidant
apoptosis
cattle
embryo
embryonic development
female reproductive system
fertilization
glutathione
heat shock protein
Hsp70 protein
hyperthermia
in vitro
oocyte
oocyte maturation
sperm
temperature
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2011, 92, 1
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-8 z 8

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