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IAPs block apoptotic events induced by caspase‐8 and cytochrome c by direct inhibition of distinct caspases
It is demonstrated that IAPs can suppress different apoptotic pathways by inhibiting distinct caspases and identify pro‐caspase‐9 as a new target for IAP‐mediated inhibition of apoptosis.
Pro-caspase-3 Is a Major Physiologic Target of Caspase-8*
In a purified system, the initiator caspases-8 and -10 directly process the executioner pro-caspase-3 with activation rates of 8.7 × 105 and 2.8 × 105 m −1 s−1, respectively, which are of sufficient magnitude to indicate direct processing in vivo.
Identification of three new members of the phospholipid scramblase gene family.
Interaction of the baculovirus anti-apoptotic protein p35 with caspases. Specificity, kinetics, and characterization of the caspase/p35 complex.
P35 is an active-site-directed inhibitor highly adapted to inhibiting caspases, verified by demonstrating that purified recombinant p35 inhibits human caspase-1, -3, -6, -7, -8, and -10 with kass values from 1.2 x 10(3) to 7x 10(5) (M-1 s-1), and with upper limits of Ki values from 0.1 to 9 nM.
The S-type lectin from calf heart tissue binds selectively to the carbohydrate chains of laminin.
Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids.
Mutation of residues within the putative EF hand loop of human PL scramblase resulted in loss of its PL mobilizing function, suggesting that these residues directly participate in the Ca2+-induced active conformation of the polypeptide.
Contortrostatin, a dimeric disintegrin from Agkistrodon contortrix contortrix, inhibits breast cancer progression.
We report the results of a multidisciplinary study on the inhibitory effect of a snake venom disintegrin, contortrostatin, a 13.5 kDa homodimeric protein isolated from Agkistrodon contortrix…
Transcriptional control of the human plasma membrane phospholipid scramblase 1 gene is mediated by interferon-alpha.
Analysis of 5' flanking genomic sequence in reporter constructs showed that transcriptional control of PLSCR1 was entirely regulated by a single IFN-stimulated response element located in the first exon, indicating that remodeling of the cell surface requires both exposure to IFN and a second yet-to-be identified event to stimulate plasma membrane phospholipid scramblase activity and to mobilize phosphatidylserine to thecell surface.
Activation of pro-caspase-7 by serine proteases includes a non-canonical specificity.
Cathepsin G activated the caspase-7 zymogen by cleaving at a Gln-Ala bond, indicating that the canonical cleavage specificity at aspartic acid is not required for activation.
Change in conformation of plasma membrane phospholipid scramblase induced by occupancy of its Ca2+ binding site.
Mutation in the segment Asp273-Asp284 reduced Tb3+ incorporation and attenuated the change in CD spectrum induced by bound metal ligand, confirming that this suspected EF-hand loopike segment of the polypeptide directly contributes to the Ca2+ binding site.