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Öğe Acute myocardial infarction in a patient with essential thrombocythemia treated with glycoprotein IIb/IIIa inhibitor(Sage Publications Inc, 2004) Gül, Ç; Kürüm, T; Demir, M; Özbay, G; Vural, Ö; Iqbal, O; Fareed, JEssential thrombocythemia (ET) rarely causes obstruction of coronary arteries or acute myocardial infarction. Treatment of acute myocardial infarction in patients with ET may be a problem due to the important role of platelets in the pathogenesis of infarction. There is no reported case of acute myocardial infarction with essential thrombocythemia treated with a glycoprotein IIb/IIIa inhibitor. In this report, a 49-year-old woman with essential thrombocythemia, admitted with a diagnosis of acute inferolateral myocardial infarction, was treated with tirofiban, a glycoprotein IIb/IIIa receptor blocker.Öğe Anticoagulant and antiprotease effects of a novel heparinlike compound from shrimp (Penaeus brasiliensis) and its neutralization by heparinase I(Sage Publications Inc, 2001) Demir, M; Iqbal, O; Dietrich, CP; Hoppensteadt, DA; Ahmad, S; Daud, AN; Fareed, JHeparin is usually obtained from mammalian organs, such as beef lung, beef mucosa, porcine mucosa, and sheep intestinal mucosa. Because of the increased use of heparin in the production of low-molecular-weight heparin (LMWH), there is a growing shortage of the raw material needed to produce LMWHs. A previous report described the structural features of a novel LMWH from the shrimp (Penaeus brasiliensis). In order to compare anticoagulant and antiprotease effects of this heparin, global anticoagulant tests, such as the prothrombin time, activated partial thromboplastin time, thrombin time, and Heptest(R), were used. Amidolytic anti-Xa and anti-IIa activities were also measured. The relative susceptibility of this heparin to flavobacterial heparinase was also evaluated. The United States Pharmacopeia (USP) potency of shrimp heparin (SH) was found to be 28 U/mg. SH produced a concentration-dependent prolongation of all of the clotting tests and exhibited marked inhibition of FXa and FIIa. Heparinase treatment resulted in a marked decrease of the anticoagulant effects and neutralized the in vitro anti-IIa actions. However, the anti-Xa activities were only partially neutralized. Protamine sulfate was only partially effective in neutralizing the anticoagulant and antithrombin effects of SH. SH also produced marked prolongation of activated clotting time, which was neutralized by heparinase but not by protamine sulfate. These results suggest that SH is a strong anticoagulant with comparable properties to mammalian heparins and can be used in the development of clinically useful antithrombotic-anticoagulant drugs.Öğe Ecarin clotting time is sensitive to heparinoids: Comparison of two different techniques(Lippincott Williams & Wilkins, 2001) Demir, M; Iqbal, O; Untch, B; Hoppensteadt, DA; Gaikwad, BS; Fareed, JEcarin clotting time (ECT) is currently developed for the specific monitoring of antithrombin drugs, such as hirudin, argatroban, and hirulog. Aqueous reagent and dry chemistry technology have become available for ECT monitoring of antithrombin agents. Currently, many heparinoids and heparinomimetic drugs are being developed. These agents activate heparin cofactor II (HCII) and primarily mediate their effects by inhibiting thrombin. Although the test is specific for antithrombin agents, heparin cofactor II-mediated thrombin inhibitors are capable of prolonging the ECT. In order to study the relative effects of some of these agents, ECT was measured in human plasma supplemented with PI-88 (a sulfated pentomanose; Progen Industries Limited, Sydney, Australia), aprosulate, pentosan polysulfate, dermatan sulfate, unfractionated heparin (UFH), and recombinant hirudin (r-hirudin). All agents were supplemented to the citrated-pooled plasma prepared from 10 healthy volunteers at a graded dosage of 0 to 100 mug/ml. These techniques gave comparable results for all of the agents used (PI-88, r(2) = 0.99; r-hirudin, r(2) = 0.98; UFH, r(2) = 0.98; dermatan sulfate, r(2) = 0.95; aprosulate, r(2) = 0.95; pentosan polysulfate, r(2) = 0.94). The relative anticoagulant effects of various agents used on ECT varied widely, exhibiting their potency in the following order: r-hirudin = pentosan polysulfate > dermatan sulfate > PI-88 > aprosulate > UFH. The sensitivity of ECT was adjusted by varying the concentration of the ecarin reagent. The results suggest that HCII-mediated inhibition of thrombin can be detected by using ECT reagents.Öğe Global anticoagulant effects of a novel sulfated pentomanan oligosaccharide mixture(Lippincott Williams & Wilkins, 2001) Piccolo, P; Iqbal, O; Demir, M; Ma, Q; Gerbutavicius, R; Fareed, JPI-88 is a potent antiproliferative agent, which is developed for various indications in cancer. This agent is obtained from yeast fermentation and is primarily composed of pentamannose and tetramannose oligosaccharide units. PI-88 is capable of producing anticoagulant effects, which are mediated by heparin cofactor II. The purpose of this study was to determine the anticoagulant properties of PI-88 in native whole blood, freshly drawn from human volunteers, supplemented with PI-88 at various concentrations (0-100 mug/mL). Whole blood activated clotting time (ACT) was measured using Hemochron instruments. PI-88 produced a strong anticoagulant effect at 100 mug/mL (479.0 +/- 59.5 sec). This anticoagulant effect was comparable to that observed in interventional cardiology and open-heart surgery. At the lower level, PI-88 produced concentration-dependent effects on ACT. Using thromboelastographic techniques (TEG), the effect of PI-88 was measured in terms of various parameters. PI-88 produced potent anticoagulant effects in the TEG studies. At the concentration of 25 mug/mL, it produced a complete anticoagulant effect in whole blood. Whole blood samples supplemented with PI-88 showed a concentration-dependent decrease in the generation of various markers of clotting activation. These results clearly suggest that PI-88 exerts an anticoagulant effect in whole blood. Because of the low-molecular-weight nature and a novel mechanism of action, this new drug may be considered for further development, particularly in cancer patients.Öğe Hyperhomocysteinemia in cancer patients with thrombosis is independent of methylene tetrahydrofolate reductase gene mutation.(Amer Soc Hematology, 2004) Fareed, J; Tobu, M; Hoppensteadt, DA; Cunanan, J; Iqbal, O; Demir, M; Deitcher, S[Abstract Not Available]Öğe Molecular and pharmacologic profile of tinzaparin and a comparable low-molecular-weight bacterial sulfaminoheparosan(Sage Publications Inc, 2004) Maddineni, J; Ma, Q; Hoppensteadt, DA; Demir, M; Manoni, M; Cornelli, U; Fareed, JLow-molecular-weight heparins (LMWH) represent depolymerized porcine mucosal heparin derivatives, which are commonly used for the management of thrombotic disorders. Because of their widespread usage, the supplies of the raw material namely unfractionated heparin are nearly exhausted. Porcine mucosal tissue is almost exclusively used for the preparation of these agents. Thus, there is a timely need for the production of heparin like drugs from other sources. Fermentation techniques have been used to produce carbohydrates such as dextran and innulin for therapeutic purposes. Bacterial cell wall polysaccharide mimics the linear hexose units, which constitute heparin. Utilizing Escherichia coli cell membranes produced by fermentation technology, chemical sulfation and enzymatic epimerization, sulfamincheparosan type of polymer mimicking the structure of heparin has been produced. These semi-synthetic sulfaminoheparosans exhibit biologic actions comparable to that observed with heparin. The sulfaminoheparosan core can also be degraded to obtain low-molecular-weight (LMW) derivatives mimicking LMWHs. Using this technique, a novel LMW sulfaminoheparosan derivative (Q93C/239) was produced by Inalco, Milan, Italy. To compare this heparin analogue, a LMWH, namely tinzaparin, was used to determine the relative anticoagulant, antiprotease, and molecular profile. Additional studies were carried out to determine the susceptibility of this agent to heparinase-I. These comparative studies exhibited both antiprotease and anticoagulant properties similar to those of tinzaparin. However LMW sulfaminoheparosan resisted heparinase-I digestion at low heparinase-I concentrations. These studies demonstrate that the sulfaminoheparosan derived LMW components exhibit similar molecular and anticoagulant profile as tinzaparin and warrant additional preclinical and clinical development to determine their potential usefulness as antithrombotic agents.Öğe Molecular heterogeneity in recombinant erythropoietin using surface enhanced laser induced desorption ionization (SELDI). clinical implications(Amer Soc Hematology, 2005) James, E; Maddineni, J; Fareed, J; Florian-Kujawski, M; Baltasar, F; Jeske, W; Hoppensteadt, D[Abstract Not Available]Öğe Potential role of ADAMTS13/FXI complexes in the pathogenesis of end stage rental disease(Amer Soc Hematology, 2005) Fareed, J; Hoppensteadt, D; Cunanan, J; Patel, C; Maddineni, J; Baltasar, F; Fareed, D[Abstract Not Available]Öğe Role of PAI-1 and TAFI in the mediation of fibrinolytic deficit in cancer patients.(Amer Soc Clinical Oncology, 2004) Florian-Kujawski, MR; Hoppensteadt, D; Iqbal, O; Demir, M; Tobu, M; Fareed, D; Fareed, J[Abstract Not Available]Öğe Upregulation of monocyte chemotactic protein-1 and CD40 ligand in cancer and its modulation by a LMWH enoxaparin: Observations from the Oncenox study.(Amer Soc Hematology, 2003) Fareed, J; Hoppensteadt, D; Iqbal, O; Tobu, M; Demir, A; Cort, S; Deitcher, SR[Abstract Not Available]Öğe Upregulation of monocyte chemotactic protein-1 and CD40 ligand in cancer patients and their modulation by subcutaneous enoxaparin-results from the ONCENOX study(Amer Soc Clinical Oncology, 2004) Iqbal, O; Tobu, M; Demir, MA; Hoppensteadt, D; Fareed, J; Cort, S; Deitcher, S[Abstract Not Available]
