Antiheparin proteins secreted by human platelets. purification, characterization, and radioimmunoassay

Rucinski, Boguslaw; Niewiarowski, Stefan; James, Pranee; Walz, Daniel A.; Budzynski, Andrei Z.

doi:10.1182/blood.v53.1.47.47

Cited by 173 publications

(41 citation statements)

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“…Threshold doses of adenosine diphosphate were then used to measure aggregation as a function of percent light transmittance in subsequent samples (5). A radioimmunoassay was performed as described, measuring plasma levels of platelet ~-thromboglobulin (32). Addition ofArg 358 cx 1 -antitrypsin alone did not effect the measurement of platelet ~-thromboglobulin.…”

Section: Methodsmentioning

confidence: 99%

α1-Antitrypsin Pittsburgh (Met358 → Arg) Inhibits the Contact Pathway of Intrinsic Coagulation and Alters the Release of Human Neutrophil Elastase during Simulated Extracorporeal Circulation

et al. 1994

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SummaryCardiopulmonary bypass prolongs bleeding time, increases postoperative blood loss, and triggers activation of plasma proteolytic enzyme systems and blood cells referred to as the “whole body inflammatory response”. Contact of blood with synthetic surfaces leads to qualitative and quantitative alterations in platelets, neutrophils, contact and complement systems. Contact and complement pathway proteins both induce neutrophil activation, a j-antitrypsin Pittsburgh (Met358 → Arg), a mutant of α1-antitrypsin, is a potent inhibitor of plasma kalli-krein and thrombin. We investigated whether this recombinant mutant protein inhibited platelet activation, as well as contact and/or complement-induced neutrophil activation during simulated extracorporeal circulation.Arg358 α1-antitrypsin did not prevent the 34% drop in platelet count at 5 min of recirculation, did not block the 50% decrease in ADP-induced platelet aggregation at 120 min of recirculation, nor inhibit the release of 6.06 α 1.07 µg/ml (3-thromboglobulin at 120 min of recirculation suggesting that the inhibitor had little effect on platelet activation. However, Arg358 α1 arantitrypsin totally blocked kallikrein-Cl-in-hibitor complex formation but not Cl-Cl-inhibitor complex formation. Most importantly, Arg358 α1-antitrypsin decreased the release of 1.11 α 0.16 µg/ml human neutrophil elastase by 43%. The attenuation of neutrophil activation in the absence of an effect on complement activation via the classical pathway, supports the concept that kallikrein is a major mediator of neutrophil degranulation during cardiopulmonary bypass.

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Section: Methodsmentioning

confidence: 99%

α1-Antitrypsin Pittsburgh (Met358 → Arg) Inhibits the Contact Pathway of Intrinsic Coagulation and Alters the Release of Human Neutrophil Elastase during Simulated Extracorporeal Circulation

et al. 1994

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“…The proteins released from the platelets were examined by electrophoresis on a 20% SDS-acrylamide gel. Two a-granule proteins, |3-thromboglobulin ((3-TG) and platelet factor 4 (PF4) were identified using polyclonal antibodies (18).…”

Section: A-granule Release From Plateletsmentioning

confidence: 99%

Interaction of Echicetin with a High Affinity Thrombin Binding Site on Platelet Glycoprotein GPIb

Peng

Emig

Mao³

et al. 1995

Thromb Haemost

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SummaryEchicetin, a protein isolated from Echis carinatus snake venom, inhibited platelet aggregation and secretion induced by low concentrations of thrombin (<0.2 U/ml), by binding to platelet glycoprotein lb (GPIb). The inhibition was not observed when the platelets were stimulated with higher concentrations of thrombin (>0.2 U/ml). Echicetin competed with thrombin for binding to the high affinity site on GPIb. Thrombin also inhibited 50% of the binding of 125I-echicetin to the platelets.

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“…Both proteins, platelet factor 4 (PF4) and beta‐TG‐related proteins (platelet basic protein (PBP), LA‐PF4, beta‐TG and beta‐TG‐F) being constituents of α‐granules are secreted from platelets upon stimulation (Kaplan et al, 1979; Rucinski et al, 1979). These proteins have been considered specific, since their concentration in platelets is about 20,000 times higher than the concentrations measured in plasma.…”

Section: Discussionmentioning

confidence: 99%

Experimental thermal lesions induce beta-thromboglobulin release from activated platelets

Blunk

Sauerstein²,

Schmelz

2011

European Journal of Pain

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Time courses of beta-thromboglobulin release, and protein extravasation after thermal inflammation of human skin was compared to neurogenic inflammation induced by histamine iontophoresis. Beta-TG and protein levels were sampled by intradermal microdialysis. Three microdialysis membranes were inserted at each stimulation site. The collected samples were measured photometrically for protein by the Coomassie blue method and for beta-TG by ELISA. Heat stimuli of 40°C and 47°C, and histamine iontophoresis were inflicted directly above the membranes. In vitro recovery rates of beta-TG and bovine albumin were measured using a latex chamber. Recovery rates at a continuous flow rate of 3 μl/min for bovine albumin ranged between 20% and 35%; those for beta-TG ranged between 14% and 17%. Heat stimulation at 40°C showed a slight but insignificant increase of beta-TG during the stimulation period. Temperatures of 47°C produced a significant, long-lasting increase of beta-TG, whereas histamine iontophoresis did not. Protein extravasation corresponded with beta-TG release; a long-lasting significant increase during and after the burn lesion, and only an initial increase of protein extravasation during the 40°C heat stimulus. Long lasting heat stimuli to the skin induced beta-TG release from platelets, whereas histamine iontophoresis although provoking protein extravasation and neurogenic flare, did not. Using microdialysis techniques we detected beta-TG release during an inflammatory response. We conclude that local platelet activation is induced by the heating stimulus. Platelet mediators, such as beta-TG might contribute to the subsequent inflammatory process which is also characterized by mechanical and heat hyperalgesia.

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Antiheparin proteins secreted by human platelets. purification, characterization, and radioimmunoassay

Cited by 173 publications

References 0 publications

α1-Antitrypsin Pittsburgh (Met358 → Arg) Inhibits the Contact Pathway of Intrinsic Coagulation and Alters the Release of Human Neutrophil Elastase during Simulated Extracorporeal Circulation

α1-Antitrypsin Pittsburgh (Met358 → Arg) Inhibits the Contact Pathway of Intrinsic Coagulation and Alters the Release of Human Neutrophil Elastase during Simulated Extracorporeal Circulation

Interaction of Echicetin with a High Affinity Thrombin Binding Site on Platelet Glycoprotein GPIb

Experimental thermal lesions induce beta-thromboglobulin release from activated platelets

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