Inhibition of protein cross-linking in calcium-enriched human erythrocytes and activated platelets

Biochemistry ◽  
1987 ◽  
Vol 26 (1) ◽  
pp. 308-313 ◽  
Author(s):  
L. Lorand ◽  
N. Barnes ◽  
J. A. Bruner-Lorand ◽  
M. Hawkins ◽  
M. Michalska
Keyword(s):  
Human Erythrocytes ◽  
Cross Linking ◽  
Activated Platelets ◽  
Protein Cross Linking

scholarly journals Ca2+-induced biochemical changes in human erythrocytes and their relation to microvesiculation

1981 ◽  
Vol 198 (3) ◽  
pp. 433-440 ◽  
Author(s):  
D Allan ◽  
P Thomas
Keyword(s):  
Human Erythrocytes ◽  
Biochemical Changes ◽  
Cross Linking ◽  
Ionophore A23187 ◽  
Cell Shrinkage ◽  
Polypeptide Pattern ◽  
Intracellular Concentrations ◽  
Protein Cross Linking

1. Human erythrocytes were treated with Ca2+ and ionophore A23187 and measurements were made of K+ efflux, polyphosphoinositide breakdown, 1,2-diacylglycerol accumulation, phosphatidate synthesis, changes in membrane polypeptide pattern and release of microvesicles. 2. It was shown that neither transamidase-mediated protein cross-linking, proteolysis of polypeptides 2.1 (ankyrin) or 4.1, nor accumulation of diacylglycerol or phosphatidate appeared to be necessary for microvesiculation to occur. 3. Microvesicles were released only under conditions where KCl efflux leading to cell shrinkage occurred and where polyphosphoinositides were broken down. These circumstances were sufficient to cause microvesiculation only in the presence of increased intracellular concentrations of Ca2+.

Transglutaminases: Protein Cross-Linking Enzymes in Tissues and Body Fluids

1994 ◽  
Vol 71 (04) ◽  
pp. 402-415 ◽  
Author(s):  
Daniel Aeschlimann ◽  
Mats Paulsson
Keyword(s):  
Body Fluids ◽  
Cross Linking ◽  
Protein Cross Linking

Tridegin, a Novel Peptidic Inhibitor of Factor XIIIa from the Leech, Haementeria ghilianii, Enhances Fibrinolysis In Vitro

1997 ◽  
Vol 77 (05) ◽  
pp. 0959-0963 ◽  
Author(s):  
Lisa Seale ◽  
Sarah Finney ◽  
Roy T Sawyer ◽  
Robert B Wallis
Keyword(s):  
Potent Inhibitor ◽  
Platelet Rich Plasma ◽  
Factor Xiiia ◽  
Cross Linking ◽  
Fibrinolytic Enzymes ◽  
Small Polypeptide ◽  
Tissue Plasminogen ◽  
Protein Cross Linking

SummaryTridegin is a potent inhibitor of factor Xllla from the leech, Haementeria ghilianii, which inhibits protein cross-linking. It modifies plasmin-mediated fibrin degradation as shown by the absence of D-dimer and approximately halves the time for fibrinolysis. Plasma clots formed in the presence of Tridegin lyse more rapidly when either streptokinase, tissue plasminogen activator or hementin is added 2 h after clot formation. The effect of Tridegin is markedly increased if clots are formed from platelet-rich plasma. Platelet-rich plasma clots are lysed much more slowly by the fibrinolytic enzymes used and if Tridegin is present, the rate of lysis returns almost to that of platelet- free clots. These studies indicate the important role of platelets in conferring resistance to commonly used fibrinolytic enzymes and suggest that protein cross-linking is an important step in this effect. Moreover they indicate that Tridegin, a small polypeptide, may have potential as an adjunct to thrombolytic therapy.

scholarly journals Glycan-protein cross-linking mass spectrometry reveals sialic acid-mediated protein networks on cell surfaces

2021 ◽  
Author(s):  
Yixuan Xie ◽  
Siyu Chen ◽  
Qiongyu Li ◽  
Ying Sheng ◽  
Michael R Alvarez ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Sialic Acid ◽  
Membrane Proteins ◽  
Cell Membranes ◽  
Sialic Acids ◽  
Cross Linking ◽  
Protein Networks ◽  
Cell Surfaces ◽  
Protein Cross Linking

A cross-linking method is developed to elucidate the glycan-mediated interactions between membrane proteins through sialic acids. The method provides previously unknown extensive glycomic interactions on cell membranes. The vast majority...

Effect of protein cross-linking aldehydes on nerve activity

1981 ◽  
Vol 89 (2) ◽  
pp. 159-165 ◽  
Author(s):  
D. G. Margineanu ◽  
Eva Katona ◽  
Junona Popa
Keyword(s):  
Cross Linking ◽  
Nerve Activity ◽  
Protein Cross Linking

A Novel Protein Cross-Linking Reaction in Stressed Neutral Protamine Hagedorn Formulations of Insulin

1999 ◽  
Vol 88 (3) ◽  
pp. 331-336 ◽  
Author(s):  
Ronald C. Beavis ◽  
Michael D. Kneirman ◽  
David Sharknas ◽  
Mark A. Heady ◽  
Bruce H. Frank ◽  
...  
Keyword(s):  
Cross Linking ◽  
Neutral Protamine Hagedorn ◽  
Novel Protein ◽  
Protein Cross Linking

scholarly journals Model of the Mediator middle module based on protein cross-linking

2013 ◽  
Vol 41 (20) ◽  
pp. 9266-9273 ◽  
Author(s):  
Laurent Larivière ◽  
Clemens Plaschka ◽  
Martin Seizl ◽  
Evgeniy V. Petrotchenko ◽  
Larissa Wenzeck ◽  
...  
Keyword(s):  
Cross Linking ◽  
Protein Cross Linking

scholarly journals Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II

2014 ◽  
Vol 111 (45) ◽  
pp. 16178-16183 ◽  
Author(s):  
Manjula P. Mummadisetti ◽  
Laurie K. Frankel ◽  
Henry D. Bellamy ◽  
Larry Sallans ◽  
Jost S. Goettert ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Cross Linking ◽  
Higher Plant ◽  
Protein Cross Linking

scholarly journals CLMSVault: A Software Suite for Protein Cross-Linking Mass-Spectrometry Data Analysis and Visualization

2017 ◽  
Vol 16 (7) ◽  
pp. 2645-2652 ◽  
Author(s):  
Mathieu Courcelles ◽  
Jasmin Coulombe-Huntington ◽  
Émilie Cossette ◽  
Anne-Claude Gingras ◽  
Pierre Thibault ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Data Analysis ◽  
Mass Spectrometry Data ◽  
Cross Linking ◽  
Software Suite ◽  
Protein Cross Linking

scholarly journals Antigenicity of the infected-erythrocyte and merozoite surfaces in Falciparum malaria.

1979 ◽  
Vol 150 (5) ◽  
pp. 1241-1254 ◽  
Author(s):  
S G Langreth ◽  
R T Reese
Keyword(s):  
Plasmodium Falciparum ◽  
Falciparum Malaria ◽  
Infected Erythrocyte ◽  
Falciparum Infection ◽  
Human Erythrocytes ◽  
Cross Linking ◽  
Common Antigens

The antigenicity of altered structures induced by Plasmodium falciparum in the membranes of infected Aotus monkey and human erythrocytes was examined. Antisera were obtained from monkeys made immune to malaria. Bound antibodies were shown to be localized on the knob protrusions of infected erythrocytes of both human and monkey origin and from both in vitro and in vivo infections. Therefore, P. falciparum infection has produced similar antigenic changes in the erythrocyte surfaces of both man and monkey. Uninfected erythrocytes and all knobless-infected erythrocytes bound no antibody from immune sera. Strains of P. falciparum from widely different geographic areas that were cultured in vitro in human erythrocytes induced structures (knobs) which have common antigenicity. Merozoites were agglutinated by cross-linking of their cell coats when incubated with immune sera. The binding of ferritin-labeled antibody was heavy on the coats of both homologous and heterologous strains of the parasite, indicating that the merozoite surfaces of these strains share common antigens.

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