The fate of SPE B after internalization and its implication in SPEB-induced apoptosis.

Chia Wen Chang, Wan Hua Tsai, Woei-Jer Chuang, Yee-Shin Lin, Jiunn Jong Wu, Ching-Chuan Liu, Pei-Jane Tsai, Ming T. Lin

研究成果: Article

4 引文 (Scopus)

摘要

After streptococcal pyrogenic exotoxin B (SPE B) induces apoptosis, its fate is unknown. Using confocal time-course microscopy at 37 degrees C, we detected green fluorescence 20 min after adding FITC-SPE B. Orange fluorescence, an indication of co-localization of SPE B with lysosomes which were labeled with a red fluorescent probe, was maximal at 40 min and absent by 60 min. SPE B was co-precipitated with clathrin, which is consistent with endocytotic involvement. Western blotting assay also indicated that uptake of SPE B was maximal at 40 min and disappeared after 60 min. However, in the presence of chloroquine, a lysosome inhibitor, the uptake of SPE B was not detectable. The disappearance of TCA-precipitated FITC-SPE B was parallel to the appearance of TCA soluble FITC-SPE B; in the presence of chloroquine, however, no SPE B degradation occurred. Chloroquine increased the level of SPE B-induced apoptosis by inhibiting the degradation of SPE B. These results suggest that the internalization and degradation of SPE B in cells may be a host defense system that removes toxic substances by sacrificing the exposed cells.

原文English
頁(從 - 到)419-427
頁數9
期刊Journal of biomedical science
14
發行號3
DOIs
出版狀態Published - 2007 一月 1

指紋

Apoptosis
Fluorescein-5-isothiocyanate
Chloroquine
Lysosomes
Degradation
Fluorescence
erythrogenic toxin
Clathrin
Poisons
Fluorescent Dyes
Microscopy
Assays
Microscopic examination
Western Blotting

All Science Journal Classification (ASJC) codes

  • Endocrinology, Diabetes and Metabolism
  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology
  • Biochemistry, medical
  • Pharmacology (medical)

引用此文

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title = "The fate of SPE B after internalization and its implication in SPEB-induced apoptosis.",
abstract = "After streptococcal pyrogenic exotoxin B (SPE B) induces apoptosis, its fate is unknown. Using confocal time-course microscopy at 37 degrees C, we detected green fluorescence 20 min after adding FITC-SPE B. Orange fluorescence, an indication of co-localization of SPE B with lysosomes which were labeled with a red fluorescent probe, was maximal at 40 min and absent by 60 min. SPE B was co-precipitated with clathrin, which is consistent with endocytotic involvement. Western blotting assay also indicated that uptake of SPE B was maximal at 40 min and disappeared after 60 min. However, in the presence of chloroquine, a lysosome inhibitor, the uptake of SPE B was not detectable. The disappearance of TCA-precipitated FITC-SPE B was parallel to the appearance of TCA soluble FITC-SPE B; in the presence of chloroquine, however, no SPE B degradation occurred. Chloroquine increased the level of SPE B-induced apoptosis by inhibiting the degradation of SPE B. These results suggest that the internalization and degradation of SPE B in cells may be a host defense system that removes toxic substances by sacrificing the exposed cells.",
author = "Chang, {Chia Wen} and Tsai, {Wan Hua} and Woei-Jer Chuang and Yee-Shin Lin and Wu, {Jiunn Jong} and Ching-Chuan Liu and Pei-Jane Tsai and Lin, {Ming T.}",
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The fate of SPE B after internalization and its implication in SPEB-induced apoptosis. / Chang, Chia Wen; Tsai, Wan Hua; Chuang, Woei-Jer; Lin, Yee-Shin; Wu, Jiunn Jong; Liu, Ching-Chuan; Tsai, Pei-Jane; Lin, Ming T.

於: Journal of biomedical science, 卷 14, 編號 3, 01.01.2007, p. 419-427.

研究成果: Article

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T1 - The fate of SPE B after internalization and its implication in SPEB-induced apoptosis.

AU - Chang, Chia Wen

AU - Tsai, Wan Hua

AU - Chuang, Woei-Jer

AU - Lin, Yee-Shin

AU - Wu, Jiunn Jong

AU - Liu, Ching-Chuan

AU - Tsai, Pei-Jane

AU - Lin, Ming T.

PY - 2007/1/1

Y1 - 2007/1/1

N2 - After streptococcal pyrogenic exotoxin B (SPE B) induces apoptosis, its fate is unknown. Using confocal time-course microscopy at 37 degrees C, we detected green fluorescence 20 min after adding FITC-SPE B. Orange fluorescence, an indication of co-localization of SPE B with lysosomes which were labeled with a red fluorescent probe, was maximal at 40 min and absent by 60 min. SPE B was co-precipitated with clathrin, which is consistent with endocytotic involvement. Western blotting assay also indicated that uptake of SPE B was maximal at 40 min and disappeared after 60 min. However, in the presence of chloroquine, a lysosome inhibitor, the uptake of SPE B was not detectable. The disappearance of TCA-precipitated FITC-SPE B was parallel to the appearance of TCA soluble FITC-SPE B; in the presence of chloroquine, however, no SPE B degradation occurred. Chloroquine increased the level of SPE B-induced apoptosis by inhibiting the degradation of SPE B. These results suggest that the internalization and degradation of SPE B in cells may be a host defense system that removes toxic substances by sacrificing the exposed cells.

AB - After streptococcal pyrogenic exotoxin B (SPE B) induces apoptosis, its fate is unknown. Using confocal time-course microscopy at 37 degrees C, we detected green fluorescence 20 min after adding FITC-SPE B. Orange fluorescence, an indication of co-localization of SPE B with lysosomes which were labeled with a red fluorescent probe, was maximal at 40 min and absent by 60 min. SPE B was co-precipitated with clathrin, which is consistent with endocytotic involvement. Western blotting assay also indicated that uptake of SPE B was maximal at 40 min and disappeared after 60 min. However, in the presence of chloroquine, a lysosome inhibitor, the uptake of SPE B was not detectable. The disappearance of TCA-precipitated FITC-SPE B was parallel to the appearance of TCA soluble FITC-SPE B; in the presence of chloroquine, however, no SPE B degradation occurred. Chloroquine increased the level of SPE B-induced apoptosis by inhibiting the degradation of SPE B. These results suggest that the internalization and degradation of SPE B in cells may be a host defense system that removes toxic substances by sacrificing the exposed cells.

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