Inhibition of nonlysosomal calcium-dependent proteolysis by glycine during anoxic injury of rat hepatocytes

Nichols, Jenna; Bronk, Steven F.; Mellgren, Ronald L.; Gores, Gregory J.

doi:10.1016/s0016-5085(94)95147-0

Cited by 79 publications

(44 citation statements)

References 27 publications

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“…Glycine decreases oxidative stress [15][16][17][18][19] by different and partly indirect mechanisms that prevent reactive oxygen species formation. Furthermore, glycine protects renal tubular cells, hepatocytes and endothelial cells against injury from hypoxia, ischemia-reperfusion and ATP depletion [16,[36][37][38][39] . Most studies show that glycine protects plasma membrane integrity, but does not restore ATP levels or affect intracellular pH [16,[38][39][40] .…”

Section: How Does Dietary Glycine Decrease Cholestasis-induced Liver mentioning

confidence: 99%

Dietary glycine blunts liver injury after bile duct ligation in rats

Froh¹,

Zhong²,

Walbrun³

et al. 2008

WJG

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Section: How Does Dietary Glycine Decrease Cholestasis-induced Liver mentioning

confidence: 99%

Dietary glycine blunts liver injury after bile duct ligation in rats

Froh¹,

Zhong²,

Walbrun³

et al. 2008

WJG

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“…The synthetic substrate LLVY can be cleaved by the proteasome and the calpains [11,[15][16][17]. In order to investigate the activity of these proteases in the intact mouse lens, the lenses were preincubated for 1 h with the proteasome inhibitor lactacystin, diluted to a final concentration of 10 ÌM from a 1 mM (H 2 O) stock solution or with the calpain inhibitor calpeptin, 50 ÌM (0.1% DMSO) or an inhibitor of acid lysosomal enzymes, monensin 10 ÌM (0.2% ethanol).…”

Section: Proteolytic Activity In the Mouse Lensmentioning

confidence: 99%

A New Model for Assessing Proteolysis in the Intact Mouse Lens in Organ Culture

et al. 2004

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Purpose: To develop a new method to investigate proteolysis in the intact lens in organ culture. Methods: Intact mouse lenses were assayed at regular intervals for proteolytic activity using fluorogenic peptide substrates ± addition of ionomycin. Specific inhibitors were used to determine the activity of calpains, the proteasome and acid lysosomal enzymes. Results: Significant levels of proteolytic activity were present in the intact lens. Proteolysis was stimulated by ionomycin. Preincubation with an inhibitor to the proteasome significantly decreased proteolysis whereas inhibitors of calpain and acid lysosomal enzymes did not. Conclusion: This study indicates that in the intact mouse lens in culture, the proteasome is an important protease. Its activity is at least partially regulated by calcium.

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“…Other substrates not localized at membranes include the nuclear protein cyclin D1 (Choi et al, 1997). Calpains have been implicated in many cellular processes including platelet aggregation, cytoskeletal reorganization during endocytosis and exocytosis and in several models of cell death including some instances of necrosis and apoptosis (Kawasaki and Kawashima, 1996;Geeraerts et al, 1991;Lee et al, 1991;Nichols et al, 1994;Nath et al, 1996;Squier and Cohen, 1997).…”

Section: Introductionmentioning

confidence: 99%

Bax cleavage is mediated by calpain during drug-induced apoptosis

et al. 1998

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The anti-apoptotic molecule Bcl-2 is located in the mitochondrial and endoplasmic reticulum membranes as well as the nuclear envelope. Although its location has not been as rigorously de®ned, the pro-apoptotic molecule Bax appears to be mainly a cytosolic protein which translocates to the mitochondria upon induction of apoptosis. Here we identify a protease activity in mitochondria-enriched membrane fractions from HL-60 cells capable of cleaving Bax which is absent from the cytosolic fraction. Bax protease activity is blocked in vitro by cysteine protease inhibitors including E-64 which distinguishes it from all known caspases and granzyme B, both of which are involved in apoptosis. Protease activity is also blocked by inhibitors against the calciumactivated neutral cysteine endopeptidase calpain. Partial puri®cation of the Bax protease activity from HL-60 cell membrane fractions by column chromatography revealed that a calpain-like activity was the protease responsible for Bax cleavage. In addition, puri®ed calpain enzymes cleaved Bax in a calcium-dependent manner. Pretreatment of HL-60 cells with the speci®c calpain inhibitor calpeptin eectively blocked both drug-induced Bax cleavage and calpain activation, but not PARP cleavage or cell death. These results suggest that calpains and caspases are activated during drug-induced apoptosis and that calpains, along with caspases, may be involved in modulating cell death by acting selectively on cellular substrates.

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Inhibition of nonlysosomal calcium-dependent proteolysis by glycine during anoxic injury of rat hepatocytes

Cited by 79 publications

References 27 publications

Dietary glycine blunts liver injury after bile duct ligation in rats

Dietary glycine blunts liver injury after bile duct ligation in rats

A New Model for Assessing Proteolysis in the Intact Mouse Lens in Organ Culture

Bax cleavage is mediated by calpain during drug-induced apoptosis

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