Active Site Peptides with CXXC Motif on Map-Resin Can Mimic Protein Disulfide Isomerase Activity

1995 ◽  
Vol 213 (3) ◽  
pp. 746-751 ◽  
Author(s):  
T. Ookura ◽  
K. Kainuma ◽  
H.J. Kim ◽  
A. Otaka ◽  
N. Fujii ◽  
...  
Keyword(s):  
Active Site ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Cxxc Motif ◽  
Isomerase Activity ◽  
Protein Disulfide ◽  
Disulfide Isomerase Activity

scholarly journals Protein disulfide isomerase activity is released by activated platelets

Blood ◽  
1992 ◽  
Vol 79 (9) ◽  
pp. 2226-2228 ◽  
Author(s):  
K Chen ◽  
Y Lin ◽  
TC Detwiler
Keyword(s):  
Disulfide Bonds ◽  
Protein Disulfide Isomerase ◽  
Ph Dependence ◽  
Gel Filtration ◽  
Disulfide Isomerase ◽  
Isomerase Activity ◽  
Activated Platelets ◽  
Protein Disulfide ◽  
Supernatant Solution ◽  
Disulfide Isomerase Activity

Abstract The release of protein disulfide isomerase by activated platelets was hypothesized on the basis of reported intermolecular and intramolecular thiol-disulfide exchange and disulfide reduction involving released thrombospondin in the supernatant solution of activated platelets (Danishefsky, Alexander, Detwiler: Biochemistry, 23:4984, 1984; Speziale, Detwiler: J Biol Chem, 265:17859, 1990; Speziale, Detwiler: Arch Biochem Biophys 286:546, 1991). Protein disulfide isomerase activity, measured by catalysis of the renaturation of ribonuclease inactivated by randomization of disulfide bonds, was detected in the supernatant solution after platelet activation. The activity was inhibited by peptides known to inhibit protein disulfide isomerase; the peptides also inhibited formation of disulfide-linked thrombospondin- thrombin complexes. The reaction catalyzed by the supernatant solution showed a pH dependence distinct from that of the uncatalyzed reaction. The activity was excluded by a 50-Kd dialysis membrane, and it was eluted in the void volume of a gel-filtration column, indicating that it was associated with a macromolecule. The activity was not removed by centrifugation at 100,000 g for 150 minutes indicating that it was not associated with membrane microvesicles. Possible functions for the release of protein disulfide isomerase by activated platelets are discussed.

Correlation Between Attenuation of Protein Disulfide Isomerase Activity Through S-Mercuration and Neurotoxicity Induced by Methylmercury

2014 ◽  
Vol 27 (2) ◽  
pp. 99-105 ◽  
Author(s):  
Kento Makino ◽  
Kosaku Okuda ◽  
Eisuke Sugino ◽  
Tadashi Nishiya ◽  
Takashi Toyama ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Isomerase Activity ◽  
Protein Disulfide ◽  
Disulfide Isomerase Activity

scholarly journals Protein disulfide isomerase activity is released by activated platelets

Blood ◽  
1992 ◽  
Vol 79 (9) ◽  
pp. 2226-2228 ◽  
Author(s):  
K Chen ◽  
Y Lin ◽  
TC Detwiler
Keyword(s):  
Disulfide Bonds ◽  
Protein Disulfide Isomerase ◽  
Ph Dependence ◽  
Gel Filtration ◽  
Disulfide Isomerase ◽  
Isomerase Activity ◽  
Activated Platelets ◽  
Protein Disulfide ◽  
Supernatant Solution ◽  
Disulfide Isomerase Activity

The release of protein disulfide isomerase by activated platelets was hypothesized on the basis of reported intermolecular and intramolecular thiol-disulfide exchange and disulfide reduction involving released thrombospondin in the supernatant solution of activated platelets (Danishefsky, Alexander, Detwiler: Biochemistry, 23:4984, 1984; Speziale, Detwiler: J Biol Chem, 265:17859, 1990; Speziale, Detwiler: Arch Biochem Biophys 286:546, 1991). Protein disulfide isomerase activity, measured by catalysis of the renaturation of ribonuclease inactivated by randomization of disulfide bonds, was detected in the supernatant solution after platelet activation. The activity was inhibited by peptides known to inhibit protein disulfide isomerase; the peptides also inhibited formation of disulfide-linked thrombospondin- thrombin complexes. The reaction catalyzed by the supernatant solution showed a pH dependence distinct from that of the uncatalyzed reaction. The activity was excluded by a 50-Kd dialysis membrane, and it was eluted in the void volume of a gel-filtration column, indicating that it was associated with a macromolecule. The activity was not removed by centrifugation at 100,000 g for 150 minutes indicating that it was not associated with membrane microvesicles. Possible functions for the release of protein disulfide isomerase by activated platelets are discussed.

scholarly journals OR04-5 Stimulation of Protein Disulfide Isomerase Activity by Activation of The Renin-Angiotensin System

2019 ◽  
Vol 3 (Supplement_1) ◽  
Author(s):  
Jose Irizarry ◽  
Nanivette Echevarria-Lorenzo ◽  
David Sanchez ◽  
Yaritza Inostroza ◽  
Alicia Rivera ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Renin Angiotensin System ◽  
Angiotensin System ◽  
Disulfide Isomerase ◽  
Renin Angiotensin ◽  
Isomerase Activity ◽  
Protein Disulfide ◽  
Disulfide Isomerase Activity ◽  
Stimulation Of
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