Calpain-dependent calpastatin cleavage regulates caspase-3 activation during apoptosis of Jurkat T cells induced by Entamoeba histolytica

Kim, Kyeong Ah; Lee, Young Ah; Shin, Myoung-Ho

doi:10.1016/j.ijpara.2007.03.011

Cited by 46 publications

(47 citation statements)

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“…This observation is similar to our recent study (30), where ventricular PO caused the activation of both calpain and caspase-3, and treatment with calpeptin abolished both their activation and prevented myocardial cell death. Previous studies show a calpain-mediated mechanism for the activation of caspase-3 in Jurkat T cells that could be prevented by calpeptin treatment (25). TUNEL reactivity and caspase-3 activation are primarily used as markers of apoptosis, although they often overlap with necrotic cell death.…”

Section: Discussionmentioning

confidence: 99%

Calpain inhibition preserves myocardial structure and function following myocardial infarction

Mani¹,

Balasubramanian²,

Zavadzkas³

et al. 2009

American Journal of Physiology-Heart and Circulatory Physiology

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Mani SK, Balasubramanian S, Zavadzkas JA, Jeffords LB, Rivers WT, Zile MR, Mukherjee R, Spinale FG, Kuppuswamy D. Calpain inhibition preserves myocardial structure and function following myocardial infarction. Am J Physiol Heart Circ Physiol 297: H1744 -H1751, 2009. First published September 4, 2009 doi:10.1152/ajpheart.00338.2009.-Cardiac pathology, such as myocardial infarction (MI), activates intracellular proteases that often trigger programmed cell death and contribute to maladaptive changes in myocardial structure and function. To test whether inhibition of calpain, a Ca 2ϩ -dependent cysteine protease, would prevent these changes, we used a mouse MI model. Calpeptin, an aldehydic inhibitor of calpain, was intravenously administered at 0.5 mg/kg body wt before MI induction and then at the same dose subcutaneously once per day. Both calpeptin-treated (n ϭ 6) and untreated (n ϭ 6) MI mice were used to study changes in myocardial structure and function after 4 days of MI, where end-diastolic volume (EDV) and left ventricular ejection fraction (EF) were measured by echocardiography. Calpain activation and programmed cell death were measured by immunohistochemistry, Western blotting, and TdT-mediated dUTP nick-end labeling (TUNEL). In MI mice, calpeptin treatment resulted in a significant improvement in EF [EF decreased from 67 Ϯ 2% pre-MI to 30 Ϯ 4% with MI only vs. 41 Ϯ 2% with MI ϩ calpeptin] and attenuated the increase in EDV [EDV increased from 42 Ϯ 2 l pre-MI to 73 Ϯ 4 l with MI only vs. 55 Ϯ 4 l with MI ϩ calpeptin]. Furthermore, calpeptin treatment resulted in marked reduction in calpain-and caspase-3-associated changes and TUNEL staining. These studies indicate that calpain contributes to MI-induced alterations in myocardial structure and function and that it could be a potential therapeutic target in treating MI patients.cardiomyocytes; cell death SEVERAL CARDIOVASCULAR PATHOLOGIES, including myocardial infarction (MI), are associated with left ventricular (LV) remodeling as defined by changes in LV geometry and structure, and concomitantly, LV pump function can be adversely affected post-MI (7,34,46). At the cellular level, both qualitative and quantitative changes in cardiomyocytes can also contribute to both compromised contractile function (9) and programmed cell death (21,22,30). One common mechanism for this maladaptive remodeling at the cardiomyocyte level is hyperactivation of cellular endopeptidases, such as members of the calpain (6, 15, 16, 58) and caspase families (5,22,26,54). Activation of these proteases may result in the cleavage of several key cellular proteins that result in the loss of contractile proteins and thus function of cardiac muscle cells.Although studies demonstrate activation of both calpain and caspases with cardiac disease states, our laboratory (30) recently demonstrated that calpain activation contributes substantially to programmed cell death in pressure-overloaded (PO) feline myocardium. Calpains are a family of Ca 2ϩ -dependent cysteine proteases. The predominant ...

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Section: Discussionmentioning

confidence: 99%

Calpain inhibition preserves myocardial structure and function following myocardial infarction

Mani¹,

Balasubramanian²,

Zavadzkas³

et al. 2009

American Journal of Physiology-Heart and Circulatory Physiology

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“…E. histolytica causes apoptosis of cells that lack caspase-8 or have been treated with caspase-9 inhibitors (38), suggesting that classic upstream activation of caspase-8 or -9 is either an accessory for or not involved in the activation of caspase-3. However, upon coincubation with trophozoites, human lymphocytes (Jurkat T cells) exhibited a higher intracellular Ca 2ϩ concentration and calpain proteolytic activity, which led (via a mitochondrion-independent mechanism) to caspase-3 cleavage and activation (45). The observed in vitro relevance of amoebiasis in this mechanism needs to be confirmed in vivo during ALA development.…”

Section: Fig 4 Control Of Host Responses By Entamoeba Histolyticamentioning

confidence: 98%

Host-Microbe Interactions and Defense Mechanisms in the Development of Amoebic Liver Abscesses

2009

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SUMMARY Amoebiasis by Entamoeba histolytica is a major public health problem in developing countries and leads to several thousand deaths per year. The parasite invades the intestine (provoking diarrhea and dysentery) and the liver, where it forms abscesses (amoebic liver abscesses [ALAs]). The liver is the organ responsible for filtering blood coming from the intestinal tract, a task that implies a particular structure and immune features. Amoebae use the portal route and break through the sinusoidal endothelial barrier to reach the hepatic parenchyma. When faced with systemic and cell-mediated defenses, trophozoites adapt to their new environment and modulate host responses, leading to parasite survival and the formation of inflammatory foci. Cytopathogenic effects and the onset of inflammation may be caused by diffusible products originating from parasites and/or immune cells either by their secretion or by their release after cell death. Liver infection thus results from the interplay between E. histolytica and hepatic cells. Despite its importance in terms of public health burden, the lack of integrated data on ALA genesis means that we have only an incomplete description of the initiation and development of hepatic amoebiasis. Here, we review the main steps of ALA development as well as the responses triggered in both the host and the parasite. Transcriptome studies highlighted parasite factors involved in adherence to human cells, cytopathogenic effects, and adaptative and stress responses. An understanding of their role in ALA development will help to unravel the host-pathogen interactions and their evolution throughout the infection.

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“…Loss of adhesion may in turn trigger apoptosis (anoikis). Elements intervening in E. histolytica contact-dependent apoptosis of LSEC were inferred from data obtained with the human lymphoma line Jurkat [47][48][49]. Upon contact with trophozoites, the protein tyrosine phosphorylation level rapidly decreases and the concentration of free intracellular calcium drastically rises.…”

Section: Resultsmentioning

confidence: 99%

New insights into host-pathogen interactions duringEntamoeba histolyticaliver infection

Faust¹,

Markiewicz²,

Santi-Rocca³

et al. 2011

European Journal of Microbiology and Immunology

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Amoebiasis is the third worldwide disease due to a parasite. The causative agent of this disease, the unicellular eukaryote Entamoeba histolytica, causes dysentery and liver abscesses associated with inflammation and human cell death. During liver invasion, before entering the parenchyma, E. histolytica trophozoites are in contact with liver sinusoidal endothelial cells (LSEC). We present data characterizing human LSEC responses to interaction with E. histolytica and identifying amoebic factors involved in the process of cell death in this cell culture model potentially relevant for early steps of hepatic amoebiasis. E. histolytica interferes with host cell adhesion signalling and leads to diminished adhesion and target cell death. Contact with parasites induces disruption of actin stress fibers and focal adhesion complexes. We conclude that interference with LSEC signalling may result from amoeba-triggered changes in the mechanical forces in the vicinity of cells in contact with parasites, sensed and transmitted by focal adhesion complexes. The study highlights for the first time the potential role in the onset of hepatic amoebiasis of the loss of liver endothelium integrity by disturbance of focal adhesion function and adhesion signalling. Among the amoebic factors required for changed LSEC adherence properties we identified the Gal/GalNAC lectin, cysteine proteases and KERP1.

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Calpain-dependent calpastatin cleavage regulates caspase-3 activation during apoptosis of Jurkat T cells induced by Entamoeba histolytica

Cited by 46 publications

References 46 publications

Calpain inhibition preserves myocardial structure and function following myocardial infarction

Calpain inhibition preserves myocardial structure and function following myocardial infarction

Host-Microbe Interactions and Defense Mechanisms in the Development of Amoebic Liver Abscesses

New insights into host-pathogen interactions duringEntamoeba histolyticaliver infection

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