Pea Seedling Extracts Catalyze Protein Amine Binding and Protein Cross-Linking. 1. Evidence for the Role of a Diamine Oxidase

1996 ◽  
Vol 44 (11) ◽  
pp. 3717-3722
Author(s):  
Marileusa D. Chiarello ◽  
Colette Larré ◽  
Zenon M. Kedzior ◽  
Jacques Gueguen
Keyword(s):  
Diamine Oxidase ◽  
Cross Linking ◽  
Pea Seedling ◽  
Protein Cross Linking

Pea Seedling Extracts Catalyze Protein Amine Binding and Protein Cross-Linking. 2. Contribution of Diamine Oxidase to These Reactions

1996 ◽  
Vol 44 (11) ◽  
pp. 3723-3726 ◽  
Author(s):  
Marileusa D. Chiarello ◽  
Colette Larré ◽  
Zenon M. Kedzior ◽  
Jacques Gueguen
Keyword(s):  
Diamine Oxidase ◽  
Cross Linking ◽  
Pea Seedling ◽  
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.

Direct evidence for the role of Maillard reaction products in protein cross-linking in milk powder during storage

2013 ◽  
Vol 31 (2) ◽  
pp. 83-91 ◽  
Author(s):  
Thao T. Le ◽  
John W. Holland ◽  
Bhesh Bhandari ◽  
Paul F. Alewood ◽  
Hilton C. Deeth
Keyword(s):  
Maillard Reaction ◽  
Direct Evidence ◽  
Milk Powder ◽  
Cross Linking ◽  
Maillard Reaction Products ◽  
Reaction Products ◽  
Protein Cross Linking

The Role of Redox-Active Amino Acids on Compound I Stability, Substrate Oxidation, and Protein Cross-Linking in Yeast CytochromecPeroxidase†

Biochemistry ◽  
2001 ◽  
Vol 40 (49) ◽  
pp. 14942-14951 ◽  
Author(s):  
Thomas D. Pfister ◽  
Alan J. Gengenbach ◽  
Sung Syn ◽  
Yi Lu
Keyword(s):  
Amino Acids ◽  
Substrate Oxidation ◽  
Cross Linking ◽  
Compound I ◽  
Redox Active ◽  
Protein Cross Linking

Role of transglutaminase and protein cross-linking in the repair of mucosal stress erosions

1992 ◽  
Vol 262 (5) ◽  
pp. G818-G825 ◽  
Author(s):  
J. Y. Wang ◽  
L. R. Johnson
Keyword(s):  
Enzyme Activity ◽  
Oral Administration ◽  
Specific Inhibitor ◽  
Duodenal Mucosa ◽  
Mucosal Healing ◽  
Cross Linking ◽  
Xiphoid Process ◽  
Transglutaminase Activity ◽  
Protein Cross Linking

We have recently demonstrated that polyamines are absolutely required for gastric and duodenal mucosal repair after stress. Polyamines act as substrates for transglutaminase and facilitate protein cross-linking. The current study tests whether transglutaminase and protein cross-linking are involved in the mechanism of mucosal healing. Rats were fasted 22 h, placed in restraint cages, and immersed in water to the xiphoid process for 6 h. Animals were killed immediately or 4, 12, or 24 h after stress. Gastric and duodenal mucosa were examined histologically and grossly, and transglutaminase activity was measured. Transglutaminase activity in gastric and duodenal mucosa was increased significantly from 0 to 8 h, peaking 4 h after the 6-h stress period. By 12 h, enzyme activity in duodenal mucosa had returned to control values while gastric mucosal transglutaminase did not decrease to control values until 24 h. Mucosal recovery from lesions produced by stress was evident 12 h after stress and was almost complete by 24 h. Dansylcadaverine (100 mg/kg, orally), a specific inhibitor of protein cross-linking, not only prevented the increases in transglutaminase but significantly decreased healing in both tissues. Oral administration of the polyamine spermidine (100 mg/kg) immediately after stress totally prevented inhibition of repair caused by blocking ornithine decarboxylase with difluoromethylornithine (DFMO, 500 mg/kg). Administration of dansylcadaverine, together with spermidine, significantly prevented the beneficial effect of spermidine on mucosal healing in the DFMO-treated animals.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals The role of the thiol group in protein modification with methylglyoxal

2009 ◽  
Vol 74 (8-9) ◽  
pp. 867-883 ◽  
Author(s):  
Jelena Acimovic ◽  
Bojana Stanimirovic ◽  
Ljuba Mandic
Keyword(s):  
Protein Modification ◽  
Time Course ◽  
Thiol Group ◽  
Model Systems ◽  
Cross Linking ◽  
Thiol Groups ◽  
Serum Albumins ◽  
Stable Product ◽  
Protein Cross Linking

Methylglyoxal is a highly reactive ?-oxoaldehyde with elevated production in hyperglycemia. It reacts with nucleophilic Lys and Arg side-chains and N-terminal amino groups causing protein modification. In the present study, the importance of the reaction of the Cys thiol group with methylglyoxal in protein modification, the competitiveness of this reaction with those of amino and guanidine groups, the time course of these reactions and their role and contribution to protein cross-linking were investigated. Human and bovine serum albumins were used as model systems. It was found that despite the very low levels of thiol groups on the surface of the examined protein molecules (approx. 80 times lower than those of amino and guanidino groups), a very high percentage of it reacts (25-85 %). The amount of reacted thiol groups and the rate of the reaction, the time for the reaction to reach equilibrium, the formation of a stable product and the contribution of thiol groups to protein cross-linking depend on the methylglyoxal concentration. The product formed in the reaction of thiol and an insufficient quantity of methylglyoxal (compared to the concentrations of the groups accessible for modification) participates to a significant extent (4 %) to protein cross-linking. Metformin applied in equimolar concentration with methylglyoxal prevents its reaction with amino and guanidino groups but, however, not with thiol groups.

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

Platelet Accumulation on Fibrin-coated Polyethylene: Role of Platelet Activation and Factor XIII

1995 ◽  
Vol 73 (05) ◽  
pp. 850-856 ◽  
Author(s):  
F D Rubens ◽  
D W Perry ◽  
M W C Hatton ◽  
P D Bishop ◽  
M A Packham ◽  
...  
Keyword(s):  
Factor Xiii ◽  
Cross Linking ◽  
Internal Diameter ◽  
Static System ◽  
Graft Occlusion ◽  
Platelet Binding ◽  
Coated Surface ◽  
Platelet Accumulation ◽  
Polyethylene Tubing

SummaryPlatelet accumulation on small- and medium-calibre vascular grafts plays a significant role in graft occlusion. We examined platelet accumulation on the surface of fibrin-coated polyethylene tubing (internal diameter 0.17 cm) during 10 min of flow (l0ml/min) at high wall shear rate (764 s-1). Washed platelets labelled with 51Cr were resuspended in Tyrode solution containing albumin, apyrase and red blood cells (hematocrit 40%). When the thrombin that was used to form the fibrin-coated surface was inactivated with FPRCH2C1 before perfusion of the tubes with the platelet:red blood cell suspension, the accumulation of platelets was 59,840 ± 27,960 platelets per mm2, whereas accumulation on fibrin with residual active thrombin was 316,750 ± 32,560 platelets per mm2 (n = 4). When the fibrin on the surface was cross-linked by including recombinant factor XIII (rFXIII) in the fibrinogen solution used to prepare the fibrin-coated surface, platelet accumulation, after thrombin neutralization, was reduced by the cross-linking from 46,974 ± 9702 to 36,818 ± 7964 platelets per mm2 (n = 12, p <0.01). Platelet accumulation on tubes coated with D-dimer was ten times less than on tubes coated with D-domain; this finding also supports the observation that cross-linking of fibrin with the formation of γ-γ dimers reduces platelet accumulation on the fibrin-coated surface. Thrombin-activated platelets themselves were shown to cross-link fibrin when they had adhered to it during perfusion, or in a static system in which thrombin was used to form clots from FXIII-free fibrinogen in the presence of platelets. Thus, cross-linking of fibrin by FXIII in plasma or from platelets probably decreases the reactivity of the fibrin-containing thrombi to platelets by altering the lysine residue at or near the platelet-binding site of each of the γ-chains of the fibrinogen which was converted into the fibrin of these thrombi.

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...

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