Results 11 to 20 of about 346,133 (262)

Caspase-1, but Not Caspase-3, Promotes Diabetic Nephropathy [PDF]

open access: yesJournal of the American Society of Nephrology, 2016
Glomerular apoptosis may contribute to diabetic nephropathy (dNP), but the pathophysiologic relevance of this process remains obscure. Here, we administered two partially disjunct polycaspase inhibitors in 8-week-old diabetic (db/db) mice: M-920 (inhibiting caspase-1, -3, -4, -5, -6, -7, and -8) and CIX (inhibiting caspase-3, -6, -7, -8, and -10 ...
Khurrum, Shahzad   +11 more
openaire   +2 more sources

Apoptosis in the absence of caspase 3 [PDF]

open access: yesOncogene, 2001
MCF-7 human breast cancer cells do not express caspase 3, thought by some to be a critical component of the apoptosis cascade. Nonetheless, both mock- and bcl-2-transfected MCF-7 cells undergo apoptosis after treatment with a variety of stimuli, including the DNA-cleaving antimitotic agent, neocarzinostatin (NCS).
Y, Liang, C, Yan, N F, Schor
openaire   +2 more sources

Rewiring Pyroptosis to Potentiate Cancer Immunotherapy via a Gasdermin D Agonist Bypassing Caspase-3. [PDF]

open access: yesAdv Sci (Weinh)
This work introduces a small‐molecule agonist, DIBDO, that bypasses Casp‐3 to directly trigger GSDMD‐mediated pyroptosis in tumors. Activated by glutathione, DIBDO generates singlet oxygen and molecular iodine, blocking Casp‐3 pathways and inducing immunogenic cell death.
Zhao D   +6 more
europepmc   +2 more sources

DECAY, a novel Drosophilacaspase related to mammalian caspase-3 and caspase-7. [PDF]

open access: yesJournal of Biological Chemistry, 1999
Caspases are key effectors of programmed cell death in metazoans. In Drosophila, four caspases have been described so far. Here we describe the identification and characterization of the fifth Drosophila caspase, DECAY. DECAY shares a high degree of homology with the members of the mammalian caspase-3 subfamily, particularly caspase-3 and caspase-7 ...
Dorstyn, L.   +4 more
openaire   +3 more sources

Metalloporphyrins inactivate caspase‐3 and ‐8 [PDF]

open access: yesThe FASEB Journal, 2005
ABSTRACT Activation of caspases represents one of the earliest biochemical indicators for apoptotic cell death. Therefore, measurement of caspase activity is a widely used and generally accepted method to determine apoptosis in a wide range of in vivo and in vitro settings.
Blumenthal, Signe B.   +8 more
openaire   +3 more sources

Molecular Dynamics Studies of Caspase-3 [PDF]

open access: yesBiophysical Journal, 2003
Caspase-3 is a fundamental target for pharmaceutical interventions against a variety of diseases involving disregulated apoptosis. The enzyme is active as a dimer with two symmetry-related active sites, each featuring a Cys-His catalytic dyad and a selectivity loop, which recognizes the characteristic DEVD pattern of the substrate.
Sulpizi, M.   +2 more
openaire   +3 more sources

Caspase-1 Is an Apical Caspase Leading to Caspase-3 Cleavage in the AIM2 Inflammasome Response, Independent of Caspase-8 [PDF]

open access: yesJournal of Molecular Biology, 2018
Canonical inflammasomes are multiprotein complexes that can activate both caspase-1 and caspase-8. Caspase-1 drives rapid lysis of cells by pyroptosis and maturation of interleukin (IL)-1β and IL-18. In caspase-1-deficient cells, inflammasome formation still leads to caspase-3 activation and slower apoptotic death, dependent on caspase-8 as an apical ...
Sagulenko, Vitaliya   +4 more
openaire   +5 more sources

FADD, Caspase-3, and Caspase-8 and Incidence of Coronary Events [PDF]

open access: yesArteriosclerosis, Thrombosis, and Vascular Biology, 2017
Objective— To investigate the relationship between 3 markers of apoptosis, that is, FADD (Fas-associated death domain–containing protein), caspase-3, and caspase-8, and incidence of coronary events (CEs) in a population-based cohort study.
Xue L   +9 more
openaire   +3 more sources

Pro-caspase-3 Is a Major Physiologic Target of Caspase-8 [PDF]

open access: yesJournal of Biological Chemistry, 1998
The apoptotic signal triggered by ligation of members of the death receptor family is promoted by sequential activation of caspase zymogens. We show here that in a purified system, the initiator caspases-8 and -10 directly process the executioner pro-caspase-3 with activation rates (kcat/Km) of 8.7 x 10(5) and 2.8 x 10(5) M-1 s-1, respectively.
H R, Stennicke   +13 more
openaire   +2 more sources

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