Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text PDF (Full Text) PPT slides of all figures Supplemental Material Index Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Nakanishi, K. Articles by Morishima, N. Search for Related Content PubMed PubMed Citation Articles by Nakanishi, K. Articles by Morishima, N. Related Collections Related Article Social Bookmarking                      What's this?

¹ Bioarchitect Research Group, Institute of Physical and Chemical Research, Wako, Saitama 351-0198, Japan
² Cellular and Molecular Biology Laboratory, Institute of Physical and Chemical Research, Wako, Saitama 351-0198, Japan
³ Antibiotics Laboratory, Institute of Physical and Chemical Research, Wako, Saitama 351-0198, Japan
⁴ Department of Biological and Environmental Science, Faculty of Science and Engineering, Saitama University, Saitama, Saitama 338-8570, Japan

Correspondence to Nobuhiro Morishima: morishim{at}riken.jp

Abstract
Although apoptosis occurs during myogenesis, its mechanism of initiation remains unknown. In a culture model, we demonstrate activation of caspase-12, the initiator of the endoplasmic reticulum (ER) stress-specific caspase cascade, during apoptosis associated with myoblast differentiation. Induction of ER stress-responsive proteins (BiP and CHOP) was also observed in both apoptotic and differentiating cells. ATF6, but not other ER stress sensors, was specifically activated during apoptosis in myoblasts, suggesting that partial but selective activation of ER stress signaling was sufficient for induction of apoptosis. Activation of caspase-12 was also detected in developing muscle of mouse embryos and gradually disappeared later. CHOP was also transiently induced. These results suggest that specific ER stress signaling transmitted by ATF6 leads to naturally occurring apoptosis during muscle development.

Abbreviations used in this paper: AEBSF, 4-(2-aminoethyl)benzenesulfonylfluoride; DM, differentiation medium; E, embryonic day; p-APMSF, 4-amidinophenylmethanesulfonyl fluoride; UPR, unfolded protein response.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

Related Article

ER stress shapes muscle

Nicole LeBrasseur
J. Cell Biol. 2005 169: 548. [Full Text] [PDF]

This article has been cited by other articles:

• Kitamura, M. (2008). Endoplasmic reticulum stress and unfolded protein response in renal pathophysiology: Janus faces. Am. J. Physiol. Renal Physiol. 295: F323-F334 [Abstract] [Full Text]  
• Eizirik, D. L., Cardozo, A. K., Cnop, M. (2008). The Role for Endoplasmic Reticulum Stress in Diabetes Mellitus. Endocr. Rev. 29: 42-61 [Abstract] [Full Text]  
• Nakanishi, K., Dohmae, N., Morishima, N. (2007). Endoplasmic reticulum stress increases myofiber formation in vitro. FASEB J. 21: 2994-3003 [Abstract] [Full Text]  
• Azfer, A., Niu, J., Rogers, L. M., Adamski, F. M., Kolattukudy, P. E. (2006). Activation of endoplasmic reticulum stress response during the development of ischemic heart disease. Am. J. Physiol. Heart Circ. Physiol. 291: H1411-H1420 [Abstract] [Full Text]  
• Sonnet, C., Lafuste, P., Arnold, L., Brigitte, M., Poron, F., Authier, F., Chretien, F., Gherardi, R. K., Chazaud, B. (2006). Human macrophages rescue myoblasts and myotubes from apoptosis through a set of adhesion molecular systems. J. Cell Sci. 119: 2497-2507 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents