Papers by 18_101 ALFIN ARDIANSYAH
Journal of Biological Chemistry, 1973
Journal of Biological Chemistry, 1970
Journal of Biological Chemistry, 1978
Page 1. THE JOURNAL cm BIOLOGICAL CHEMISTRY VoI. 253, No. 20, Issue of October 25, pp. 7346-7354,... more Page 1. THE JOURNAL cm BIOLOGICAL CHEMISTRY VoI. 253, No. 20, Issue of October 25, pp. 7346-7354,1978 Printedin USA Identification of Adenine Nucleotide Binding Proteins in Human Platelet Membranes by Affinity Labeling with &pFluorosulfonylbenzoyl Adenosine * ...
Journal of Biological Chemistry, 1977
Journal of Biological Chemistry, 1981
Blood, 1979
Albumin decreases polymer surface affinity for platelets, and prostaglandin (PG) E1 prevents surf... more Albumin decreases polymer surface affinity for platelets, and prostaglandin (PG) E1 prevents surface-induced platelet activation. PGI2, like PGE1, inhibits platelet function but is unstable in vitro. We evaluated the ability of surface-adsorbed albumin and circulating PGI2 to prevent platelet alterations during simulated extracorporeal circulation. Fresh heparinized human blood (500 ml) was recirculated at 37'C through a silicone rubber circuit containing an 0.8sq m membrane oxygenator. When circuits were filled (primed) directly with blood, platelet counts decreased maximally to 18 % of initial levels, plasma levels of lowaffinity platelet-specific protein factor 4 (LA-PF4) rose from less than 0.5 g/ml to 15 tg / ml (indicating extensive release of granule contents), and platelets quickly became unresponsive to adenosine diphosphate (ADP) and epinephrine. In contrast. when circuits were primed with albumin (2.5 %) prior to recirculation, the circulating platelet counts remained stable at 95 % of initial levels, release of granule contents was prevented, platelet reactivity was preserved, and platelet subcellular architecture was maintained even after 6 hr of recirculation. Addition of PGI2 (3.5 nM) immediately prior to recirculation duplicated the effects of exposure of the circuit to albumin. The preservative actions of PGI2 persisted despite loss of detectable PGI2-induced inhibition in recirculated platelets. Temporary inhibition of platelet function and alteration of the proteins initially adsorbed to the biopolymer are equally effective means of preventing adverse platelet alterations during extracorporeal circulation. Furthermore, the efficacy of prostacyclin (PGI2) further demonstrates that prevention of initial platelet-surface interactions permits the subsequent appearance of polymer biocompatibility.
American Journal of Physiology-Legacy Content, 1973
Abstract : Five monkeys were infused with isologous, isoimmune IgG of high hemolytic titer, and f... more Abstract : Five monkeys were infused with isologous, isoimmune IgG of high hemolytic titer, and five control monkeys received isologous or autologous nonimmune IgG. The former experienced severe intravascular hemolysis, manifested by a fall in hematocrit and a rise in plasma hemoglobin, and disseminated intravascular coagulation (DIC), manifested by a fall in platelet count, fibrinogen, factor V, VIII, and X concentrations and prolongation of thrombin time. The plasma kallikrein system was activated as evidenced by a rise in spontaneous kallikrein activity and a fall in kallikreinogen and kallikrein inhibitor. One monkey demonstrated particularly striking changes with complete disappearance of kallikrein inhibitor and marked decrease in kallikreinogen. Hageman factor (XII) levels also decreased consistently. These changes were associated with sustained arterial hypotension in three of the five animals. Control monkeys had no intravascular hemolysis or DIC, only transient blood pressure changes, and minor fluctuations in the plasma kallikrein system. It is concluded that hemolysis and DIC induced by immune IgG may be accompanied by arterial hypotension activation of the kallikrein system. (Author)
American Journal of Clinical Pathology, 1974
The staphylococcal clumping test was compared with an agglutination test (the recently introduced... more The staphylococcal clumping test was compared with an agglutination test (the recently introduced Thrombo-Wellco test) for the detection of fibrinogen degradation products. The staphylococcal clumping test was found to be superior for the detection of purified fibrinogen and fragments X and Y, whereas the agglutination test was considerably more sensitive in detecting fragments D and E. Despite these differences, there was excellent correlation between the two tests in detecting fibrinogen degradation products in a variety of clinical disorders, including disseminated intravascular coagulation. The agglutination test appears to be a convenient, accurate test for the detection of fibrinogen degradation products.
The Journal of laboratory and clinical medicine, 1993
The leukocyte integrin Mac-1 (alpha m beta 2, CD11b/18 CR3, MO1), in addition to binding iC3b, ha... more The leukocyte integrin Mac-1 (alpha m beta 2, CD11b/18 CR3, MO1), in addition to binding iC3b, has been shown to be the receptor for the coagulation proteins fibrinogen, factor X, and high molecular weight kininogen. Mac-1 is known to be upregulated by agonists that stimulate neutrophils or monocytes. Previous studies from this laboratory have documented neutrophil activation during cardiopulmonary bypass. We therefore used an experimental model for cardiopulmonary bypass, a simulated extracorporeal circulation, to study the surface expression of Mac-1 on peripheral blood leukocytes by immunofluorescence flow cytometry. The number of Mac-1 receptors in polymorphonuclear leukocytes had increased 2.2 times and 2.9 times baseline by 2 hours at 37 degrees C and 28 degrees C, respectively (p < 0.001). Neutrophil elastase-alpha 1-proteinase inhibitor complexes (a measure of neutrophil degranulation) increased more than sixfold from 41 micrograms/L to 256 micrograms/L after 2 hours at 2...
Investigative ophthalmology, 1973
ABSTRACT
Journal of Clinical Investigation, 1975
A B STRA CT The possibility that bradykinin, a potent vasodilator, might be a physiological antag... more A B STRA CT The possibility that bradykinin, a potent vasodilator, might be a physiological antagonist of the renin-angiotensin system was investigated. 11 norman subjects, ranging in age from 21 to 33 yr were studied. Seven of the subjects were given a 10 meq sodium, 100 meq potassium, 2,500 ml isocaloric diet. After metabolic balance was achieved, they were infused with either 1 liter of 5% glucose over 2 h or 2 liters of 0.9,% saline over 4 h. During the infusions, plasma renin activity (PRA), angiotensin II (A II), prekallikrein, bradvkinin, and aldosterone levels were frequently determined. Plasmna prekallikrein and kallikrein inhibitor did not change during the infusion of either glucose or saline. In subjects receiving saline, plasma bradykinin fell from 3.9+1.5 (SEM) ng/ml at 0 min to 0.93±0.2 at 30 min and 0.95±0.3 at 120 min. These changes paralleled the decrease in PRA over the same period (7.9±1.3 ng/ml-l/h to 5.6±0.8 at 30 min and 3.5±0.7 at 120 min). Similarly, A II fell from 113±12 pg/ml to 62±10 and 48+5, respectively, at 30 and 120 min. In contrast, the control group infused wvith glucose showed no change in bradykinin, A II, or PRA. Another four subjects were given a constant 200 meq sodium/100 meq potassium isocaloric diet.
British Journal of Haematology, 1972
The development of an intrinsic two-stage assay for factor V using highly purified protein compon... more The development of an intrinsic two-stage assay for factor V using highly purified protein components is described. Phospholipid, activated factor X, calcium ion and factor V are incubated together to form a prothrombinase. After addition of prothrombin, sequential aliquots are removed and tested for thrombin activity using fibrinogen as a substrate. The rate of thrombin generation is linear for at least 10 min and increases with increasing concentrations of factor V or activated factor X. At a fixed concentration of activated factor X, a linear relationship is observed between the logarithm of the initial rate of thrombin generation and the logarithm of the factor V concentration. Oligomeric forms of factor V generate parallel but non-identical concentration curves indicating differing abilities to form prothrombinase. The rate of thrombin generation eventually decreases and a maximum thrombin concentration is attained. This phenomenon is not attributable to substrate exhaustion or to decay of prothrombinase activity. Evidence for the formation of an inhibitor during prothrombin conversion, which is directed against both prothrombinase and the reaction of thrombin with fibrinogen, is offered. Activation of factor V by thrombin is demonstrable in the two-stage intrinsic system and in a modified extrinsic sequential technique. In both systems the time course and extent of activation are similar to those observed using a one-stage extrinsic assay. Thrombin formation began immediately with or without prior exposure of factor V to thrombin. The 'lag time' observed by some previous workers is shown to be an artifact due to inappropriate extrapolation of the standard thrombin curve. The optimal rate of conversion of prothrombin to thrombin in both the extrinsic and intrinsic systems of blood coagulation requires the presence of activated factor X (factor Xa), lipid, calcium ion, and factor V. Hanahan and his colleagues (Papahadjopoulos & Hanahan, 1964; Barton & Hanahan, 1969) have shown that these reactants form a molecular complex which exhibits protlirombinase activity. Although it had been suggested that an altered form of factor V was the prothrombin-converting enzyme, it has now been established that the enzyme is factor Xa (Milstone, 1964; Barton et a!, 1967).
Annual Review of Medicine, 1979
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Papers by 18_101 ALFIN ARDIANSYAH