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+.

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 The effects of Ca2+ and Sr2+ on Ca2+-sensitive biochemical changes in human erythrocytes and their membranes

1981 ◽  
Vol 198 (3) ◽  
pp. 441-445 ◽  
Author(s):  
D Allan ◽  
P Thomas
Keyword(s):  
Direct Interaction ◽  
Human Erythrocytes ◽  
Biochemical Changes ◽  
Intracellular Concentration ◽  
Ionophore A23187 ◽  
Erythrocyte Ghosts ◽  
High Concentration ◽  
Intact Cells ◽  
Whole Cells

1. The Ca2+-dependency of K+ efflux, microvesiculation and breakdown of polyphosphoinositides and of ankyrin have been measured in intact human erythrocytes exposed to ionophore A23187 and HEDTA [N'-(2-hydroxyethyl)ethylenediamine NNN'-triacetate]-Ca2+ buffers. Half-maximal responses were observed at pCa values of 6.4, 4.1, 5.0 and 4.8 respectively. 2. The Ca2+ dependencies of K+ efflux and breakdown of polyphosphoinositides and ankyrin measured in erythrocyte ghosts without addition of ionophore showed almost identical values with those seen in whole cells treated with ionophore. 3. We conclude that ionophore A23187 is able to cause rapid equilibration of extracellular and intracellular [Ca2+] in intact cells and that in the presence of a suitable Ca2+ buffer, ionophore A23187 can be used to precisely fix the intracellular concentration of Ca2+ in erythrocytes. 4. The relatively high concentration of Ca2+ required to produce microvesiculation in intact cells may indicate that microvesiculation could be at least partly dependent on a direct interaction of Ca2+ with phospholipid. 5. Results obtained with Sr2+ paralleled those with Ca2+, although higher Sr2+ concentrations were required to achieve the same effects as Ca2+. Mg2+ produced none of the changes seen with Ca2+ or Sr2+.

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

scholarly journals FLIm and Raman Spectroscopy for Investigating Biochemical Changes of Bovine Pericardium upon Genipin Cross-Linking

Molecules ◽  
2020 ◽  
Vol 25 (17) ◽  
pp. 3857
Author(s):  
Tanveer Ahmed Shaik ◽  
Alba Alfonso-Garcia ◽  
Martin Richter ◽  
Florian Korinth ◽  
Christoph Krafft ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Fluorescence Lifetime ◽  
Density Functional ◽  
Bovine Pericardium ◽  
Biochemical Changes ◽  
Blue Pigment ◽  
Cross Linking ◽  
Fluorescence Lifetime Imaging ◽  
Fluorescence Intensity Ratio ◽  
Cross Linker

Biomaterials used in tissue engineering and regenerative medicine applications benefit from longitudinal monitoring in a non-destructive manner. Label-free imaging based on fluorescence lifetime imaging (FLIm) and Raman spectroscopy were used to monitor the degree of genipin (GE) cross-linking of antigen-removed bovine pericardium (ARBP) at three incubation time points (0.5, 1.0, and 2.5 h). Fluorescence lifetime decreased and the emission spectrum redshifted compared to that of uncross-linked ARBP. The Raman signature of GE-ARBP was resonance-enhanced due to the GE cross-linker that generated new Raman bands at 1165, 1326, 1350, 1380, 1402, 1470, 1506, 1535, 1574, 1630, 1728, and 1741 cm−1. These were validated through density functional theory calculations as cross-linker-specific bands. A multivariate multiple regression model was developed to enhance the biochemical specificity of FLIm parameters fluorescence intensity ratio (R2 = 0.92) and lifetime (R2 = 0.94)) with Raman spectral results. FLIm and Raman spectroscopy detected biochemical changes occurring in the collagenous tissue during the cross-linking process that were characterized by the formation of a blue pigment which affected the tissue fluorescence and scattering properties. In conclusion, FLIm parameters and Raman spectroscopy were used to monitor the degree of cross-linking non-destructively.

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
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