HeLa cells synthesize a specific heat shock protein upon exposure to heat shock at 42°C but not at 45°C

Heat Shock Protein 27 (Hsp27) is overexpressed in cervical cancer as a response to stress conditions. Hsp27 overexpression increase invasion, migration, and adhesion pathways of cancer cells. The Yogurt supernatant contains Short-Chain Fatty Acids (SCFA) include acetate, lactate, and butyrate which have anticancer activity. This study aimed to investigate supernatant of LBA-ST (Lactobacillusbulgaricus-acidophilus, Streptococcusthermophillus) Yogurt can decrease the expression of Hsp27 in HeLa culture cells. The mechanism on how supernatant yogurt inhibit invasion, migration, and adhesion was studied by immunocytochemistry. The data was then collected and analyzed using One-Way ANOVA. From this study, it can be concluded that the expression of proteins that play a role in invasion, adhesion, and migration of the Hsp27 was proven to be decreased (p< 0.05 ± 0.005).Keywords: HeLa cells, yogurt supernatant, Lactobacillus bulgaricus-acidophilus, Streptococcus thermophillus, Hsp27

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Characterization of a 42°C-Specific Heat Shock Protein of Mammalian Cells1

The Journal of Biochemistry ◽

10.1093/oxfordjournals.jbchem.a122244 ◽

1988 ◽

Vol 103 (1) ◽

pp. 81-85 ◽

Cited By ~ 13

Author(s):

Ken-ichi Honda ◽

Takumi Hatayama ◽

Munehiko Yukioka

Keyword(s):

Heat Shock ◽

Heat Shock Protein ◽

Specific Heat

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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

Journal of Cell Science ◽

10.1242/jcs.104.3.629 ◽

1993 ◽

Vol 104 (3) ◽

pp. 629-638 ◽

Cited By ~ 2

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.

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