Active caspase-3 is required for osteoclast differentiation

2006 ◽  
Vol 209 (3) ◽  
pp. 836-844 ◽  
Author(s):  
K.H. Szymczyk ◽  
T.A. Freeman ◽  
C.S. Adams ◽  
V. Srinivas ◽  
M.J. Steinbeck
Keyword(s):  
Caspase 3 ◽  
Osteoclast Differentiation ◽  
Active Caspase

scholarly journals Effects of Mitochondrial Uncoupling Protein 2 Inhibition by Genipin in Human Cumulus Cells

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Hongshan Ge ◽  
Fan Zhang ◽  
Dan Shan ◽  
Hua Chen ◽  
Xiaona Wang ◽  
...  
Keyword(s):  
Caspase 3 ◽  
Uncoupling Protein ◽  
Physiological Role ◽  
Cumulus Cells ◽  
Mitochondrial Uncoupling ◽  
Mitochondrial Uncoupling Protein ◽  
Cultural Medium ◽  
Cellular Autophagy ◽  
Significant Difference ◽  
Active Caspase

UCP2 plays a physiological role by regulating mitochondrial biogenesis, maintaining energy balance, ROS elimination, and regulating cellular autophagy in numerous tissues. But the exact roles of UCP2 in cumulus cells are still not clear. Genipin, a special UCP2 inhibitor, was added into the cultural medium to explore the roles of UCP2 in human cumulus cells. There were no significant differences in ATP and mitochondrial membrane potential levels in cumulus cells from UCP2 inhibiting groups as compared with the control. The levels of ROS and Mn-SOD were markedly elevated after UCP2 inhibited Genipin. However, the ratio of reduced GSH to GSSG significantly declined after treatment with Genipin. UCP2 inhibition by Genipin also resulted in obvious increase in the active caspase-3, which accompanied the decline of caspase-3 mRNA. The level of progesterone in culture medium declined obviously after Genipin treatment. But there was no significant difference in estradiol concentrations. This study indicated that UCP2 is expressed in human cumulus cells and plays important roles on mediate ROS production, apoptotic process, and steroidogenesis, suggesting UCP2 may be involved in regulation of follicle development and oocyte maturation and quality.

scholarly journals Down-Regulation of Osteoclast Differentiation by Daidzein via Caspase 3

2002 ◽  
Vol 17 (4) ◽  
pp. 630-638 ◽  
Author(s):  
Claudia Maria Rassi ◽  
Michele Lieberherr ◽  
Gilles Chaumaz ◽  
Alain Pointillart ◽  
Giulia Cournot
Keyword(s):  
Caspase 3 ◽  
Osteoclast Differentiation ◽  
Down Regulation

scholarly journals Protective Effects of HBSP on Ischemia Reperfusion and Cyclosporine A Induced Renal Injury

2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
Author(s):  
Yuanyuan Wu ◽  
Junlin Zhang ◽  
Feng Liu ◽  
Cheng Yang ◽  
Yufang Zhang ◽  
...  
Keyword(s):  
Cyclosporine A ◽  
Caspase 3 ◽  
Interstitial Fibrosis ◽  
Ischemia Reperfusion ◽  
Inflammatory Cells ◽  
Protective Effects ◽  
Tubulointerstitial Damage ◽  
Apoptosis And Inflammation ◽  
The Right ◽  
Active Caspase

Ischemia reperfusion (IR) and cyclosporine A (CsA) injuries are unavoidable in kidney transplantation and are associated with allograft dysfunction. Herein, the effect and mechanism of a novel tissue protective peptide, helix B surface peptide (HBSP) derived from erythropoietin, were investigated in a rat model. The right kidney was subjected to 45 min ischemia, followed by left nephrectomy and 2-week reperfusion, with or without daily treatment of CsA 25 mg/kg and/or HBSP 8 nmol/kg. Blood urea nitrogen was increased by CsA but decreased by HBSP at 1 week and 2 weeks, while the same changes were revealed in urinary protein/creatinine only at 2 weeks. HBSP also significantly ameliorated tubulointerstitial damage and interstitial fibrosis, which were gradually increased by IR and CsA. In addition, apoptotic cells, infiltrated inflammatory cells, and active caspase-3+ cells were greatly reduced by HBSP in the both IR and IR + CsA groups. The 17 kD active caspase-3 protein was decreased by HBSP in the IR and IR + CsA kidneys, with decreased mRNA only in the IR + CsA kidneys. Taken together, it has been demonstrated, for the first time, that HBSP effectively improved renal function and tissue damage caused by IR and/or CsA, which might be through reducing caspase-3 activation and synthesis, apoptosis, and inflammation.

scholarly journals B Cell–Activating Factor Promotes B Cell Survival in Ectopic Lymphoid Tissues in Nasal Polyps

2021 ◽  
Vol 11 ◽  
Author(s):  
Zhe-Zheng Wang ◽  
Jia Song ◽  
Hai Wang ◽  
Jing-Xian Li ◽  
Qiao Xiao ◽  
...  
Keyword(s):  
B Cells ◽  
B Cell ◽  
Cell Survival ◽  
Stromal Cells ◽  
Caspase 3 ◽  
Lymphoid Tissues ◽  
B Cell Activating Factor ◽  
B Cell Survival ◽  
Active Caspase

Ectopic lymphoid tissues (eLTs) characterized by B cell aggregation contribute to the local immunoglobulin production in nasal polyps (NPs). B cell-activating factor (BAFF) is vital for B cell survival, proliferation, and maturation. The purpose of this study is to investigate whether BAFF is involved in the B cell survival and eLT formation in NPs. The mRNA and protein levels of BAFF in NP tissues with and without eLTs were detected by PCR and ELISA assay, respectively. The cellular sources of BAFF and active caspase-3-positive B cells in NPs were studied by immunofluorescence staining. B cells purified from NP tissues were stimulated with BAFF and were analyzed by flow cytometry. Stromal cells purified from NP tissues were stimulated with lymphotoxin (LT) α1β2, and BAFF levels in culture supernatants were analyzed by ELISA. Compared with those in control tissues and NPs without eLTs, the BAFF levels were elevated in NPs with eLTs. Abundant BAFF-positive cells and few active caspase-3-positive apoptotic B cells were found in NPs with eLTs, in contrast to those in NPs without eLTs. There was a negative correlation between the numbers of BAFF-positive cells and frequencies of apoptotic B cells in total B cells in NP tissues. BAFF protected nasal polyp B cells from apoptosis in vitro. Stromal cells were an important cellular source of BAFF in NPs with eLTs. LTα1β2 induced BAFF production from nasal stromal cells in vitro. We propose that BAFF contribute to eLT formation in NPs by promoting B cell survival.

Potent Therapy and Transcriptional Profile of Combined Erythropoietin Derived Peptide CHBP and Caspase-3 siRNA against Kidney Ischemia/Reperfusion Injury in mice

2020 ◽  
Author(s):  
Yuanyuan Wu ◽  
Weiwei Chen ◽  
Yufang Zhang ◽  
Aifen Liu ◽  
Cheng Yang ◽  
...  
Keyword(s):  
Caspase 3 ◽  
Ischemia Reperfusion Injury ◽  
Early Stage ◽  
Synergistic Effects ◽  
Ischemia Reperfusion ◽  
Combined Treatment ◽  
Specific Treatment ◽  
Transcriptional Profile ◽  
Apoptosis And Inflammation ◽  
Active Caspase

Abstract Cause-specific treatment and timely diagnosis are still not available for acute kidney injury (AKI) apart from supportive therapy and serum creatinine measurement. A novel erythropoietin-derived cyclic helix B surface peptide (CHBP) protects kidneys against AKI with different causes, but the underlying mechanism is not fully defined. Herein, we investigated the transcriptional profile of renoprotection induced by CHBP and its potential synergistic effects with siRNA targeting caspase-3, an executing enzyme of apoptosis and inflammation, (CASP3siRNA) on ischemia/reperfusion (IR)-induced AKI. Utilizing a mouse model with 30-min renal bilateral ischemia and 48-h reperfusion, the renoprotection of CHBP or CASP3siRNA was demonstrated in renal function and structure, active caspase-3 and HMGB1 expression. Combined treatment of CHBP and CASP3siRNA further preserved kidney structure, and reduced active caspase-3 and HMGB1. Furthermore, differentially expressed genes (DEGs) were identified with fold change > 1.414 and P < 0.05. In IR kidneys, 281 DEGs induced by CHBP were mainly involved in promoting cell division and improving cellular function and metabolism (up-regulated STAT5B and SLC22A7). The additional administration of CASP3siRNA caused 504 and 418 DEGs in IR + CHBP kidneys with or without NCsiRNA, with 37 genes in common. These DEGs were associated with modulated apoptosis and inflammation (up-regulated BCL6, SLPI and SERPINA3M), and immunity, injury and microvascular homeostasis (up-regulated CFH and GREM1, and down-regulated ANGPTL2). This proof-of-effect study indicated the potent renoprotection of CASP3siRNA upon CHBP at the early stage of IR-induced AKI. Underlying genes, BCL6, SLPI, SERPINA3M, GREM1 and ANGPTL2, might be potential new biomarkers for clinical applications.

scholarly journals Ceramide synthase 6 modulates TRAIL sensitivity and nuclear translocation of active caspase-3 in colon cancer cells

Oncogene ◽  
2009 ◽  
Vol 28 (8) ◽  
pp. 1132-1141 ◽  
Author(s):  
S White-Gilbertson ◽  
T Mullen ◽  
C Senkal ◽  
P Lu ◽  
B Ogretmen ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cancer Cells ◽  
Caspase 3 ◽  
Nuclear Translocation ◽  
Ceramide Synthase ◽  
Colon Cancer Cells ◽  
Trail Sensitivity ◽  
Active Caspase

An anti-apoptotic pattern correlates with multidrug resistance in acute myeloid leukemia patients: a comparative study of active caspase-3, cleaved PARPs, Bcl-2, Survivin and MDR1 gene

Hematology ◽  
2010 ◽  
Vol 15 (3) ◽  
pp. 135-143 ◽  
Author(s):  
Margarita L. Guenova ◽  
Gueorgui N. Balatzenko ◽  
Vessela R. Nikolova ◽  
Branimir V. Spassov ◽  
Spiro M. Konstantinov
Keyword(s):  
Acute Myeloid Leukemia ◽  
Multidrug Resistance ◽  
Comparative Study ◽  
Myeloid Leukemia ◽  
Caspase 3 ◽  
Mdr1 Gene ◽  
Acute Myeloid ◽  
Active Caspase

scholarly journals Activation of Membrane-associated Procaspase-3 Is Regulated by Bcl-2

1999 ◽  
Vol 144 (5) ◽  
pp. 915-926 ◽  
Author(s):  
Joseph F. Krebs ◽  
Robert C. Armstrong ◽  
Anu Srinivasan ◽  
Teresa Aja ◽  
Angela M. Wong ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Caspase 3 ◽  
Caspase Activity ◽  
Intracellular Membrane ◽  
Caspase Activation ◽  
Intracellular Membranes ◽  
Membrane Bound ◽  
Spontaneous Activation ◽  
Active Caspase

The mechanism by which membrane-bound Bcl-2 inhibits the activation of cytoplasmic procaspases is unknown. Here we characterize an intracellular, membrane-associated form of procaspase-3 whose activation is controlled by Bcl-2. Heavy membranes isolated from control cells contained a spontaneously activatable caspase-3 zymogen. In contrast, in Bcl-2 overexpressing cells, although the caspase-3 zymogen was still associated with heavy membranes, its spontaneous activation was blocked. However, Bcl-2 expression had little effect on the levels of cytoplasmic caspase activity in unstimulated cells. Furthermore, the membrane-associated caspase-3 differed from cytosolic caspase-3 in its responsiveness to activation by exogenous cytochrome c. Our results demonstrate that intracellular membranes can generate active caspase-3 by a Bcl-2–inhibitable mechanism, and that control of caspase activation in membranes is distinct from that observed in the cytoplasm. These data suggest that Bcl-2 may control cytoplasmic events in part by blocking the activation of membrane-associated procaspases.

scholarly journals Caspase-3–dependent cleavage of Bcl-xL in the stroma exosomes is required for their uptake by hematological malignant cells

Blood ◽  
2016 ◽  
Vol 128 (23) ◽  
pp. 2655-2665 ◽  
Author(s):  
Ioulia Vardaki ◽  
Claire Sanchez ◽  
Pedro Fonseca ◽  
Magnus Olsson ◽  
Dimitrios Chioureas ◽  
...  
Keyword(s):  
Caspase 3 ◽  
Malignant Cells ◽  
Key Points ◽  
Chemical Inhibition ◽  
Active Caspase

Key Points Bcl-xL is a substrate for active caspase-3 in the exosomes. Molecular or chemical inhibition of exosomal Bcl-xL cleavage attenuates uptake of exosomes by hematological malignant cells.

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