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ICE-like protease (caspase) is involved in transforming growth factor beta1-mediated apoptosis in FaO rat hepatoma cell line.
Hepatology. 1998 Feb; 27(2):415-21.Hep

Abstract

Transforming growth factor-beta1 (TGF-beta1) arrests growth and/or stimulates apoptosis of a variety of cells. The biochemical pathways involved in the apoptotic processes, however, remain poorly defined. TGF-beta1 induces DNA fragmentation together with morphological changes, which are characteristic of apoptosis in the FaO rat hepatoma cell line. Histones were remarkably enriched in lysates of these cells during TGF beta1-induced apoptosis. We identified U1-70 kd as a death substrate which is cleaved following TGF-beta1 treatment. The tetrapeptide caspase inhibitor carbobenzoxy-valyl-alanly-aspartyl-(beta-O-methyl)-fluoromethyl ketone (ZVAD-FMK) prevented TGF beta1-induced apoptotic DNA fragmentation and cleavage of the U1-70 kd protein, showing that caspase(s) are involved in TGF beta1-mediated apoptosis. To identify specific caspases involved in apoptosis induced by TGF-beta1 in FaO cells, proteolytic activation of several of these caspases and their substrates were studied as a function of time following TGF beta1-treatment. TGF beta1-treatment induced the progressive proteolytic processing of caspase-2 (ICH-1L/Nedd-2), whereas caspase-1 itself did not show any cleavage from the precursor. Pretreatment with ZVAD-FMK abrogated the maturation of caspase-2 and blocked the apoptotic progress. These results suggest that caspase-2, but not caspase-1, may play a crucial role in TGF beta1-induced apoptosis in these cells.

Authors+Show Affiliations

Department of Biochemistry, Ajou University School of Medicine, Suwon, Korea.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9462639

Citation

Choi, K S., et al. "ICE-like Protease (caspase) Is Involved in Transforming Growth Factor Beta1-mediated Apoptosis in FaO Rat Hepatoma Cell Line." Hepatology (Baltimore, Md.), vol. 27, no. 2, 1998, pp. 415-21.
Choi KS, Lim IK, Brady JN, et al. ICE-like protease (caspase) is involved in transforming growth factor beta1-mediated apoptosis in FaO rat hepatoma cell line. Hepatology. 1998;27(2):415-21.
Choi, K. S., Lim, I. K., Brady, J. N., & Kim, S. J. (1998). ICE-like protease (caspase) is involved in transforming growth factor beta1-mediated apoptosis in FaO rat hepatoma cell line. Hepatology (Baltimore, Md.), 27(2), 415-21.
Choi KS, et al. ICE-like Protease (caspase) Is Involved in Transforming Growth Factor Beta1-mediated Apoptosis in FaO Rat Hepatoma Cell Line. Hepatology. 1998;27(2):415-21. PubMed PMID: 9462639.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - ICE-like protease (caspase) is involved in transforming growth factor beta1-mediated apoptosis in FaO rat hepatoma cell line. AU - Choi,K S, AU - Lim,I K, AU - Brady,J N, AU - Kim,S J, PY - 1998/2/14/pubmed PY - 1998/2/14/medline PY - 1998/2/14/entrez SP - 415 EP - 21 JF - Hepatology (Baltimore, Md.) JO - Hepatology VL - 27 IS - 2 N2 - Transforming growth factor-beta1 (TGF-beta1) arrests growth and/or stimulates apoptosis of a variety of cells. The biochemical pathways involved in the apoptotic processes, however, remain poorly defined. TGF-beta1 induces DNA fragmentation together with morphological changes, which are characteristic of apoptosis in the FaO rat hepatoma cell line. Histones were remarkably enriched in lysates of these cells during TGF beta1-induced apoptosis. We identified U1-70 kd as a death substrate which is cleaved following TGF-beta1 treatment. The tetrapeptide caspase inhibitor carbobenzoxy-valyl-alanly-aspartyl-(beta-O-methyl)-fluoromethyl ketone (ZVAD-FMK) prevented TGF beta1-induced apoptotic DNA fragmentation and cleavage of the U1-70 kd protein, showing that caspase(s) are involved in TGF beta1-mediated apoptosis. To identify specific caspases involved in apoptosis induced by TGF-beta1 in FaO cells, proteolytic activation of several of these caspases and their substrates were studied as a function of time following TGF beta1-treatment. TGF beta1-treatment induced the progressive proteolytic processing of caspase-2 (ICH-1L/Nedd-2), whereas caspase-1 itself did not show any cleavage from the precursor. Pretreatment with ZVAD-FMK abrogated the maturation of caspase-2 and blocked the apoptotic progress. These results suggest that caspase-2, but not caspase-1, may play a crucial role in TGF beta1-induced apoptosis in these cells. SN - 0270-9139 UR - https://www.unboundmedicine.com/medline/citation/9462639/ICE_like_protease__caspase__is_involved_in_transforming_growth_factor_beta1_mediated_apoptosis_in_FaO_rat_hepatoma_cell_line_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0270913998000627 DB - PRIME DP - Unbound Medicine ER -