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Optimization of Salmonella enteritidis recombinant heat shock protein 60 production

100%

Rainczak K., Bajzert J., Galli J., Selera A., Wieliczko A., Borkowski J., Stefaniak T.

Polish Journal of Veterinary Sciences

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2011

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tom 14

|

nr 1

The aim of the study was to optimize conditions for producing Salmonella Enteritidis recombinant heat shock protein 60 (rHsp60). Seven Escherichia coli host strains (Rosetta, Turner, C41, C43, Origami, BL21pLys, Rosetta pLys) were transformed by a recombinant plasmid containing Hsp60 gene from Salmonella Enteritidis, and then cultured and induced by isopropyl-β-D-thiogalactopyranoside (IPTG). The highest S. Enteritidis rHsp60 yield was obtained using E. coli strain C41. Induction of this strain using IPTG allowed the yield 400 μg of S. Enteritidis Hsp60 protein/2L of culture, but by autoinduction the yield exceeded 800 μg/2L.

2

Potential role of HSP proteins in snails of the genus Helix

100%

Nowakowska A., Rogalska J., Caputa M.

Folia Malacologica

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2016

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tom 24

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nr 1

3

Antigen cross-presentation and heat shock protein-based vaccines

86%

Zachova K., Krupka M., Raska M.

Archivum Immunologiae et Therapiae Experimentalis

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2016

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tom 64

|

nr 1

4

Effect of combined drought and heat stress on heat shock proteins in wheat varieties

86%

Grigorova B., Vasseva I., Demirevska K., Feller U.

Acta Physiologiae Plantarum

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2007

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tom 29

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nr 1 Suppl.

5

Helicobacter pylori inhibits expression of heat shock protein 70 (HSP70) in human epithelial cell line. Importance of Cag A protein

86%

Targosz A., Pierzchalski P., Krawiec A., Szczyrk U., Brzozowski T., Konturek S. J., Pawlik W. W.

Journal of Physiology and Pharmacology

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2006

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tom 57

|

nr 2

Heat shock proteins (HSP) are crucial for the maintenance of cell integrity under normal cell growth and at pathophysiological conditions such as colonization of gastric mucosa by Helicobacter pylori (Hp). The effect of Hp on mRNA expression for HSP70 in the gastric epithelial cells in vitro has been little studied and remains inconclusive. In this study we attempted to determine the alterations in gene expression for HSP70 induced by two live strains of Hp in the epithelial MKN7 cells. The following Hp strains were employed; 1) Hp strain expressing cagA and vacA, and 2) cagA and vacA negative Hp strain without or with addition of exogenous recombinant protein CagA. MKN7 cells were incubated in a standard medium RPMI 1640 supplemented with 10% fetal bovine serum at 37°C with 5% CO2 and humidified atmosphere under basal condition or in a presence of Hp (1x109 CFU per dish) without or with the recombinant CagA (10 µg/ml of RPMI 1640 medium). After 3h, 24h and 48 h of incubation with Hp and in some experiments with the prolonged incubation time up to 72 h, the cells were harvested, the total cellular RNA was isolated and the expression of mRNA for HSP70 was determined by RT-PCR. The incubation of the MKN cells with CagA protein alone failed to affect significantly the expression of HSP70. In contrast, the strain Hp (cagA+, vacA+) inhibited in time-dependent manner the expression of mRNA for HSP70. When the MKN7 cells were coincubated with Hp (cagA+, vacA+) and exogenous CagA, the significant inhibition of the signal intensity for HSP70 mRNA was observed at 3 h and 24 h of incubation and these effects were followed by complete disappearance of the signal for HSP70 mRNA at 48 h. The incubation of MKN7 with Hp (cagA-, vacA-) also significantly attenuated the expression of HSP70 mRNA with the most pronounced inhibitory effect observed at 72 h of incubation with this Hp strain. Addition of the recombinant CagA to Hp (cagA-, vacA-) completely suppressed the expression of HSP70 at 48 h and 72 h after the end of incubation periods. We conclude that 1) both, Hp (cagA+, vacA+) and Hp (cagA-, vacA-) inhibit expression of HSP70 in MKN7 human gastric epithelial cells independently of the presence or absence of cagA gene, and that 2) recombinant CagA protein may exert biological activity in vitro via acceleration of inhibitory effect of Hp negative for Cag A and VacA on HSP70 expression in epithelial cells infected with this bacteria.

6

Nuclear matrix localization of chicken HSP108

86%

Altieri F., Eufemi M., Maras B., Turano C.

Cellular and Molecular Biology Letters

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1997

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tom 02

|

nr 4

A glycoprotein purified from the internal nuclear matrix of chicken liver nuclei has been identified, by partial sequencing and by Western blotting, as hsp108, which is a component of the hsp90 superfamily. This protein has been previously characterized as a protein which copurifies with the cytoplasmic progesterone receptor and as a transferrin-binding protein of the chicken oviduct cell membrane. We have found that hsp108 is present in the nuclear matrix even in the absence of a heat shock or of other noxious conditions. Some of the properties already described for its homologous proteins (endoplasmin, grp94, hsp100) might explain its function at the nuclear matrix level. Hsp108 isolated from the liver nuclear matrix has a carbohydrate composition significantly different from that of the protein of the oviduct cell membrane.

7

Toll-like receptor expression and function in airway epithelial cells

86%

Greene C. M., McElvaney N. G.

Archivum Immunologiae et Therapiae Experimentalis

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2005

|

tom 53

|

nr 5

8

Role of anti-HSP 60/65 antibodies in atherogenesis in patients with type 2 diabetes and lower limb ischemia

72%

Rabczynski M., Fiodorenko-Dumas Z., Adamiec R., Paprocka-Borowicz M., Dumas I.

Journal of Physiology and Pharmacology

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2012

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tom 63

|

nr 6

9

Ratio of proliferation markers and HSP90 gene expression as a predictor of pathological complete response in breast cancer neoadjuvant chemotherapy

72%

Jarzab M., Kowal M., Bal W., Oczko-Wojciechowska M., Rembak-Szynkiewicz J., Kowalska M., Stobiecka E., Chmielik E., Tyszkiewicz T., Kaszuba M., Nowicka E., Lange B., Czarniecka A., Krajewska J., Dyla A., Dobrut M., Lange D., Jarzab B., Bobek-Billewicz B., Tarnawski R.

Folia Histochemica et Cytobiologica

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2016

|

tom 54

|

nr 4

10

Heat-shock proteins in amoeba. II. The effect of cooling on Amoeba borokensis

72%

Kalinina L. V., Khrebtukova I. A., Wasik A., Sikora J.

Acta Protozoologica

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1990

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tom 29

|

nr 2

11

Heat shock response in gastrointestinal tract

72%

Sikora A., Grzesiuk E.

Journal of Physiology and Pharmacology. Supplement

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2007

|

tom 58

|

nr 3

43-62

12

Kynuramines induce overexpression of heat shock proteins in pancreatic cancer cells via 5-hydroxytryptamine and melatonin MT1/MT2 receptors

72%

Leja-Szpak A., Pierzchalski P., Goralska M., Nawrot-Porabka K., Bonior J., Link-Lenczowski P., Jastrzebska M., Jaworek J.

Journal of Physiology and Pharmacology

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2015

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tom 66

|

nr 5

13

Hsp27 expression in invasive ductal breast carcinoma

72%

Grzegrzolka J., Kurnol K., Piotrow P., Pula B., Kobierzycki C., Piotrowska A., Jablonska K., Wojnar A., Rys J., Dziegiel P., Podhorska-Okolow M.

Folia Histochemica et Cytobiologica

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2012

|

tom 50

|

nr 4

14

Monocytes and vascular endothelial cells apoptosis. Role of p-HSP27

72%

Gawad A., Ptak-Belowska A., Brzozowski T., Pawlik W. W.

Journal of Physiology and Pharmacology

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2009

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tom 60

|

nr 4

55-61

The aim of this study was to find out whether stimulated monocytes could trigger apoptosis of vascular endothelial cells. Human umbilical vein endothelial cells (HUVEC) (EC) were co-cultured for 24 h and 48 h with monocytes isolated from peripheral blood (peripheral blood monocytes) or MonoMac6 cell line activated previously with proinflammatory cytokines. Real-time PCR was conducted to investigate p53 up-regulated modulator of apoptosis (PUMA), heat shock protein HSP70 and HSP27 genes expression. Changes in the level of PUMA, HSP70, HSP27 and phospho-heat shock protein 27 (p-HSP27) proteins were analyzed by means of immunoprecipitation. Apoptosis was determined by TUNEL and poli-(ADP ribose) polymerase ( PARP ) cleavage assay. In HUVEC cells stimulated with monocytes hardly any increase of PUMA mRNA was observed, but the PUMA protein level was significantly up regulated especially after 24 h. Heat shock proteins (HSP70 and HSP27) mRNA expression was elevated after 24 h and 48h and confirmatory up regulation of these proteins was observed in HUVEC cells stimulated with peripheral blood monocytes but not with MonoMac6 cells. Interestingly, in nuclear compartment of HUVECs exposed to the monocytic line and native monocytes, a significant increase of p-HSP27 level has appeared. TUNEL and PARP cleavage assay did not show any apoptotic HUVEC cells after stimulation with monocytes. The main observations of this study indicate that monocytes do not trigger apoptosis of vascular endothelial cells. Proapoptotic activation mediated by PUMA that was observed seemed to be counterbalanced by significant increase of antiapoptotic HSP70, HSP27 and especially phospho-HSP27 proteins level.

15

Antibodies to heat shock proteins 90alpha and 90beta in psoriasis

72%

Damasiewicz-Bodzek A., Szumska M., Tyrpien-Golder K.

Archivum Immunologiae et Therapiae Experimentalis

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2020

|

tom 68

|

nr 2

16

SDS-PAGE heat-shock protein profiles of environmental Aeromonas strains

72%

Osman K. M., Amin Z. M. S., Aly M. A. K., Hassan H., Soliman W. S.

Polish Journal of Microbiology

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2011

|

tom 60

|

nr 2

Aeromonas microorganisms normally grow at temperatures between 5°C and 45°C and therefore should have high thermotolerance. Thus it was of interest to find out whether A. hydrophila, A. caviae and A. veronii biovar sobria serovars respond to abrupt temperature changes with a heat shock-like response. To this end the present study was undertaken to determine whether Aeromonas species exhibits a heat shock response to different temperatures and time factors. The response of Aeromonas serovars to 24 h and 48 h of thermal stress at 25°C, 42°C and 50°C involved the synthesis of 12–18 heat shock proteins (HSPs) bands with molecular weights ranging between 83.5–103.9 kDa in the high HSP molecular mass and 14.5–12.0 as low molecular mass HSP. Electrophoretic analysis of the HSPs showed that the serovars do not cluster very tightly and also that they are distinct from each other.

17

Mass spectrometry-based identification of transglutaminase protein substrates in senescing chloroplasts of barley leaves

72%

Sobieszczuk-Nowicka E., Luczak M., Legocka J.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

|

nr 3

18

Increase of heat shock protein gene expression by melatonin in AR42J cells

72%

Bonior J., Jaworek J., Konturek S. J., Pawlik W. W.

Journal of Physiology and Pharmacology

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2005

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tom 56

|

nr 3

Heat shock proteins (HSPs) have been reported to protect the pancreatic cells from the acute damage produced by caerulein overstimulation. However the effects of caerulein, melatonin or hyperthermia preconditioning on mRNA signal for HSP60 in the pancreatic acinar cells has not been examined yet. The aims of this study were: 1. To investigate the gene expression for HSP60 in the pancreatic AR42J cells stimulated by melatonin, caerulein or combination of both these substances. 2. To compare above changes with mRNA signal for HSP60 in pancreatic AR42J cells subjected to hyperthermia preconditioning. AR42J cells were incubated in standard medium at 37°C for: 0, 1, 3, 5, 12 or 24 h, under basal conditions. Above cells were then subjected to heat shock (42°C) for 0, 1 or 3 h. In the next part of the study AR42J cells were incubated in presence of caerulein (10-11, 10-9 or 10-7M), melatonin (10-8 or 10-6M), or combination of above under basal conditions or following heat shock pretreatment. Gene expression for HSP60 was determined by RT-PCR. The mRNA signal for HSP60 has been observed in AR42J cells under basal conditions, and this signal was markedly and time-dependently increased in these cells subjected to hyperthermia preconditioning. Incubation of AR42J cells in presence of melatonin (10-8 or 10-6M) resulted in the significant and dose-dependent increase of gene expression for HSP60 in both groups of AR42J cells: preconditioned and in those, which were not subjected to hyperthermia. Caerulein stimulation reduced mRNA signal for HSP60. The strongest signal has been observed after the exposition of AR42J cells to hyperthermia preconditioning, combined with melatonin and caerulein. We conclude that: 1. Gene expression for HSP60 has been detected in pancreatic AR42J cells under basal conditions. 2. Hyperthermia preconditioning resulted in a significant and time-dependent increase of HSP60 signal in pancreatic AR42J cells. 3. HSP60 gene expression was significantly increased in pancreatic AR42J cells stimulated by melatonin whereas caerulein reduced this signal. 4. The strongest gene expression for HSP60 has been found in the cells subjected to the combination of hyperthermia preconditioning, caerulein and melatonin.

19

The GC-box is critical for high level expression of the testis-specific Hsp70.2-Hst70 gene

72%

Widlak W., Vydra N., Dudaladava V., Scieglinska D., Winiarski B., Krawczyk Z.

Acta Biochimica Polonica

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2007

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tom 54

|

nr 1

The Hsp70.2/Hst70 gene, which belongs to the 70 kDa heat-shock protein (HSP) family, is expressed specifically in primary spermatocytes and spermatids. The regulatory elements required for a high level of testis-specific expression of the gene are placed between the two major transcription start sites T1 and T2 (approximately 350 and 115 bp upstream of the starting ATG codon). Here we have shown that sequences proximal to the exon1/intron splicing site in the 5' untranslated region of the Hsp70.2/Hst70 gene, which include a highly conserved element called box B, are required for efficient expression of the chloramphenicol acetyltransferase reporter gene in testes of transgenic mice. However, in spite of the drastically reduced overall activity, the stage-specific expression pattern of the transgene was preserved after removal of these sequences. We have also shown that GC-box located downstream of the box B (approximately 210 bp upstream of the starting ATG codon) is indispensable for efficient expression of the Hsp70.2/Hst70 gene promoter in spermatogenic cells. The GC-box specifically binds proteins present in nuclear extracts from testes (putatively Sp1-like factors). A change in the pattern of such GC-box-interacting factors corresponds to activation of the Hsp70.2/Hst70 gene, confirming the importance of this regulatory element.

20

The effect of quercetin on apoptosis and necrosis induction in human colon adenocarcinoma cell line LS180

72%

Pawlikowska-Pawlega B., Jakubowicz-Gil J., Rzymowska J., Gawron A.

Folia Histochemica et Cytobiologica

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2001

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tom 39

|

nr 2

Ograniczanie wyników

Optimization of Salmonella enteritidis recombinant heat shock protein 60 production

Potential role of HSP proteins in snails of the genus Helix

Antigen cross-presentation and heat shock protein-based vaccines

Effect of combined drought and heat stress on heat shock proteins in wheat varieties

Helicobacter pylori inhibits expression of heat shock protein 70 (HSP70) in human epithelial cell line. Importance of Cag A protein

Nuclear matrix localization of chicken HSP108

Toll-like receptor expression and function in airway epithelial cells

Role of anti-HSP 60/65 antibodies in atherogenesis in patients with type 2 diabetes and lower limb ischemia

Ratio of proliferation markers and HSP90 gene expression as a predictor of pathological complete response in breast cancer neoadjuvant chemotherapy

Heat-shock proteins in amoeba. II. The effect of cooling on Amoeba borokensis

Heat shock response in gastrointestinal tract

Kynuramines induce overexpression of heat shock proteins in pancreatic cancer cells via 5-hydroxytryptamine and melatonin MT1/MT2 receptors

Hsp27 expression in invasive ductal breast carcinoma

Monocytes and vascular endothelial cells apoptosis. Role of p-HSP27

Antibodies to heat shock proteins 90alpha and 90beta in psoriasis