Induction of Heat-Shock Protein (hsp) by Moxibustion

1995 ◽  
Vol 23 (03n04) ◽  
pp. 327-330 ◽  
Author(s):  
Kazuko Kobayashi
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Hsp 70 ◽  
Protein Patterns ◽  
Two Dimensional Gel Electrophoresis ◽  
Hip Muscle ◽  
And Control ◽  
Muscular Tissues

Rats were treated by moxibustion at the point of hip muscle, and intramuscular temperature was kept at 40°C for 15 minutes. The rats were sacrificed under deep anesthesia and the muscular tissues were excised immediately, three hours and 24 hours after stimulation. Proteins were extracted from the homogenized and centrifuged tissues of the stimulated rats and control rats. Two-dimensional gel electrophoresis of the proteins was carried out. Heat-shock protein (hsp) with molecular weight of 70,000 (hsp 70), 85,000 (hsp 85) and 100,000 (hsp 100) was detected in rats sacrificed three hours after the stimulation by moxibustion. Protein patterns were analyzed and the ratios of the hsps were obtained.

A stress-inducible 40 kDa protein (hsp40): purification by modified two-dimensional gel electrophoresis and co-localization with hsc70(p73) in heat-shocked HeLa cells

1993 ◽  
Vol 104 (3) ◽  
pp. 629-638 ◽  
Author(s):  
H. Hattori ◽  
T. Kaneda ◽  
B. Lokeshwar ◽  
A. Laszlo ◽  
K. Ohtsuka
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hela Cells ◽  
Gel Electrophoresis ◽  
Recovery Period ◽  
Chinese Hamster ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Terminal Amino ◽  
Kinetics Of

We have previously reported that a novel 40 kDa protein is induced by heat shock and several environmental stresses in mammalian and avian cells and that the N-terminal amino acid sequence of this 40 kDa protein has homology with the bacterial DnaJ heat-shock protein. We have purified this protein (40 kDa heat-shock protein, hsp40) from HeLa cells by modified two-dimensional gel electrophoresis and generated a polyclonal antibody against hsp40. This antibody was highly specific for human hsp40 and cross-reacted weakly with rat and Chinese hamster hsp40. Indirect immunofluorescence revealed that the hsp40 in HeLa cells accumulates in the nucleus, especially in the nucleolus, during heat shock and returns to the cytoplasm during the recovery period. The kinetics of the accumulation in the nucleoli and subsequent return to the cytoplasm of hsp40 was similar to that of hsp70. In addition, hsp40 was co-localized with hsc70(p73) in heat-shocked HeLa cells as demonstrated by double immunofluorescence staining. These results suggest that hsp40 (a DnaJ homologue) and hsp70 (a DnaK homologue) may act in concert to repair (refold) denatured proteins and protein aggregates in the nuclei and nucleoli of heat-shocked HeLa cells.

scholarly journals Comparison of protein patterns after two-dimensional gel electrophoresis from leaves of in vitro cultures and seedlings of Rubus chamaemorus L.

2014 ◽  
Vol 71 (4) ◽  
pp. 299-305 ◽  
Author(s):  
Barbara Thiem ◽  
Andrzej Kalinowski
Keyword(s):  
Gel Electrophoresis ◽  
In Vitro Cultures ◽  
Two Dimensional ◽  
Detailed Data ◽  
Protein Patterns ◽  
Two Dimensional Gel Electrophoresis ◽  
Rubus Chamaemorus ◽  
Protein Map ◽  
And Control

Proteins from leaves of <em>Rubus chamaemorus</em> propagated in vitro were subjected to miniaturized 2-D electrophoresis. The 2-DE patterns of proteins showed qualitative differences between plants propagated in vitro and control seedlings. More proteins of a high molecular weight were observed in leaves of plants from in vitro culture. A two-dimensional map of proteins from leaves provides detailed data concerning both polymorphism and protein patterns of this species. This makes it possible to start constructing a protein map of <em>R. chamaemorus</em>. The reasons for qualitative differences are discussed.

scholarly journals Simian virus 40 and polyoma virus induce synthesis of heat shock proteins in permissive cells.

1983 ◽  
Vol 3 (1) ◽  
pp. 1-8 ◽  
Author(s):  
E W Khandjian ◽  
H Türler
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Gel Electrophoresis ◽  
Mammalian Cells ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Polyoma Virus ◽  
Two Dimensional Gel Electrophoresis ◽  
Mouse Cells ◽  
Stimulation Of

During the lytic infection of monkey and mouse cells with simian virus 40 and polyoma virus, respectively, the preferentially increased synthesis of two host proteins of 92,000 and 72,000 Mr was observed by 15 to 20 h after infection besides the general stimulation of most cellular proteins. The incubation of uninfected monkey and mouse cell cultures for 30 to 60 min at 43.5 degrees C induced the enhanced synthesis of at least three proteins of 92,000, 72,000 and 70,000 Mr, the last one being the major heat shock protein of mammalian cells. Two-dimensional gel electrophoresis and partial proteolytic digestion confirmed that the same 92,000- and 72,000-Mr proteins are stimulated by virus infection and thermal treatment. In simian virus 40-infected CV-1 cells, we also observed the weak stimulation of a 70,000-Mr protein comigrating in gel electrophoresis with the major heat shock protein. The 92,000-, 72,000- and 70,000-Mr proteins of monkey cells are structurally very similar to the corresponding proteins of mouse cells. In immunoprecipitations, no specific association of these proteins to simian virus 40 T antigens was noticed.

Proteins in normal, irradiated, and postmortem human brain quantitatively compared by using two-dimensional gel electrophoresis.

1984 ◽  
Vol 30 (12) ◽  
pp. 1989-1995 ◽  
Author(s):  
R K Narayan ◽  
W E Heydorn ◽  
G J Creed ◽  
P L Kornblith ◽  
D M Jacobowitz
Keyword(s):  
Cerebral Cortex ◽  
Gel Electrophoresis ◽  
Protein Pattern ◽  
Relative Molecular Mass ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Human Cerebral Cortex ◽  
Postmortem Human Brain ◽  
Two Dimensional Gel Electrophoresis ◽  
Fresh Frozen

Abstract Using a combination of two-dimensional gel electrophoresis (2DE), silver staining, and computerized densitometry, we studied protein patterns in human cerebral cortex: normal fresh-frozen, fresh-frozen but previously irradiated, and post-mortem. The relative molecular mass of the resolved proteins ranged from 14 400 to 100 000, the isoelectric points from 4.75 to 7.0. The pattern of proteins (six of them identified) was essentially the same for all three groups. However, computerized densitometry demonstrated significant alterations in the density of several spots in the irradiated and postmortem groups as compared with the normal controls. Irradiated cortex showed statistically significant changes in only six spots (three increased and three decreased in density); postmortem material showed 20 altered spots (16 diminished and four increased). Evidently normal human cerebral cortex has a consistent protein pattern on 2DE, which is quantitatively (but not qualitatively) altered in irradiated and postmortem material. These findings provide a point of reference against which proteins from abnormal brain material can be compared, both qualitatively and quantitatively.

scholarly journals Arsenate induces stress proteins in cultured rat myoblasts.

1983 ◽  
Vol 96 (2) ◽  
pp. 393-400 ◽  
Author(s):  
Y J Kim ◽  
J Shuman ◽  
M Sette ◽  
A Przybyla
Keyword(s):  
Heat Shock ◽  
Gel Electrophoresis ◽  
Stress Proteins ◽  
Transfer Reactions ◽  
Pituitary Cells ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Myogenic Cells ◽  
Methionine Residues ◽  
Related Proteins

The induction of stress proteins was examined in rat myoblast cultures by two-dimensional gel electrophoresis. Data obtained by this analysis led to the following observations. (a) Arsenate, which behaves as a phosphate analogue in cellular phosphate-transfer reactions, stresses cultured rat cells and induces the synthesis of a unique set of proteins. (b) Most of the proteins synthesized after the addition of arsenate are identical to proteins synthesized in rat myoblasts in response to heat shock or arsenite stress. (c) However, both arsenic salts induce the synthesis of two unique proteins not induced by heat shock. (d) Five 25-30-kdalton stress proteins of rat cells do not contain methionine residues. (e) A majority of the proteins synthesized in stressed myogenic cells are also induced by stress in other rat cells such as hepatoma cells, pituitary tumor cells, and fibroblasts. The 25-30-kdalton stress-related proteins identified in myogenic cells, on the other hand, are induced in fibroblasts but not hepatoma or pituitary cells.

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