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At least 1,423 records · Page 79Linked to original sources
PubMed1998

Apolipoprotein(a) binds to low-density lipoprotein at two distant sites in lipoprotein(a).

Lipoprotein(a) [Lp(a)] consists of low-density lipoprotein (LDL) and apolipoprotein(a) [apo(a)] linked with a disulfide bond. Scanning force microscopy (SFM) of Lp(a) showed, for the first time, a belt-like structure of apo(a) with both ends attached to a spherical LDL. The two ends of apo(a) were bound to the LDL sphere at two distant sites. Occasionally, the ends were attached to two touching spheres. Under the same imaging conditions, LDL appeared as individual spheres. Electron microscopy (EM) studies of Lp(a) by several groups over the past decade failed to reveal this belt-like structure of apo(a). Images of isolated apo(a) in air or in phosphate buffer showed apo(a) as individual belts, and these belts tended to crowd together. Lp(a) formed leaf-like aggregates; apo(a) aggregates were fishnet-like, whereas LDL aggregates were less characteristic. Quantitative analysis of Lp(a) showed the diameter of the LDL to be 24.8 +/- 8.7 nm (n = 46), which is close to the reported value of 24.2 +/- 4.2 nm found with EM. The length of the belts attached to the spheres was measured to be 173.5 +/- 6.6 nm (n = 15). I also found, by using a functionalized tip, that the interaction force between apo(a) and its ligand, lysine, was related to the ionic strength of the bulk solution. This force can be reduced by the presence of epsilon-aminocaproic acid.

Apolipoproteins A↗
PubMedDate not supplied

A simple and effective method for producing nonrandom peptide libraries using cotton as a carrier in continuous flow peptide synthesizers.

A method has been developed for generating nonrandom peptide libraries on cotton. Disks of cotton fabric were chemically modified to enable peptide synthesis. Incorporation of a 6-aminocaproic acid residue handle on the cellulose turned out to be advantageous. Disks were labeled with silver ink, stacked one on top of another in a continuous flow peptide synthesizer column, and simultaneously subjected to automated synthesis procedures. Depending on the sequences to be synthesized, the automatic synthesis procedure was stopped, and the disks were removed from the column, sorted, and reapplied to subsequent synthesis steps. In this way, individual peptides could be easily prepared in milligram quantities on each of the cotton disks.

Automation↗
PubMed1999

Production and specificity of polyclonal antibodies to hexanal-lysine adducts.

Hexanal content is a widely used index of lipid oxidation in foods. The objectives of this study were to develop antibodies to hexanal-lysine adducts, devise an ELISA, and characterize antibody specificity. Hexanal was made immunogenic by covalent attachment to lysine side chains of bovine serum albumin via reductive alkylation. Polyclonal antibodies had antiserum titers as high as 6.15 x 10(5). A competitive indirect ELISA was developed with a detection limit of 0.7 ng of hexanal/mL. Antibodies were carrier-independent, reacting with hexanal conjugates of several proteins but not with the corresponding native proteins. Cross-reactivities with chicken serum albumin conjugates of n-heptanal, n-pentanal, and n-octanal were 86. 3, 11.8, and 2.2%, respectively. Antibodies reacted strongly with hexanal-modified lysine and hexanal-modified epsilon-aminocaproic acid but did not recognize free amino acids or free hexanal. It may be feasible to use this ELISA to monitor lipid oxidation in food provided hexanal is alkylated to a carrier protein prior to analysis.

Aldehydes↗
PubMed2005

Tailoring aqueous solubility of functionalized single-wall carbon nanotubes over a wide pH range through substituent chain length.

Carboxylic acid-functionalized SWNTs prepared via the reaction of an amino acid, NH2(CH2)nCO2H, with fluoronanotubes show similar levels of sidewall functionalization; however, the solubility in water is controlled by the length of the hydrocarbon side chain (i.e., n). The 6-aminohexanoic acid derivative is soluble in aqueous solution (0.5 mg mL(-1)) between pH 4 and 11, whereas the glysine and 11-aminoundecanoic acid derivatives are insoluble across all pH values.

Amino Acids↗
PubMed1998

The influence of antiestrogens on the release of plasminogen activator (uPA) by MDA-MB-231 and MCF-7 breast cancer cells.

Plasminogen activators are known to be involved in the metastatic spread of breast cancer. In the present study we examined the effects of antiestrogens [Analog II (1,1-dichloro-cis-2,3-diphenyl cyclopropane) (AII), ICI-182,780 (ICI) and tamoxifen (TAM)], on the in vitro release of uPA from estrogen receptor (ER)-positive MCF-7 (MCF) and ER-negative MDA-MB-231 (MDA) human breast cancer cell lines. Using a solid-phase radioassay, uPA activity was found to be higher in the culture medium from MDA cells compared to MCF cells. Aminocaproic acid, a specific plasmin inhibitor, produced a 50-60% reduction in the degradation of labeled substrate, in the solid phase assay, using culture medium from both cell lines, thus indicating that most of the proteolysis observed was due to uPA-mediated plasmin generation from plasminogen. In the absence of plasminogen, the enzyme activity was not detected in either the quantitative assay or by zymography. In MDA cells, uPA release was not altered by any of the antiestrogens used alone or in the presence of estradiol. In contrast, in MCF cells, ICI alone produced maximal inhibition (40%) of enzyme release, while estradiol alone produced a 120% increase in enzyme activity. When co-administered with estradiol, in MCF cultures, each antiestrogen reduced enzyme activity to control levels. Substrate gel zymography revealed that the urokinase-type PA is the predominant form of PA released by both cell lines. Comparison of the activity of all three antiestrogens used in this study indicates that ICI is the most potent inhibitor of enzyme activity in ER-positive MCF cells.

Breast Neoplasms↗
PubMed1998

Influence of fibrin structure on the formation and maintenance of capillary-like tubules by human microvascular endothelial cells.

Fibrin is a temporary matrix which not only covers a wound, but also provides a structure for invading cells during healing. Changes in the polymerization conditions before gelation of the clot affect the structure of fibrin and thus might influence the interaction with invading cells. Therefore we tested whether changes in the fibrin structure influence the formation of capillary-like tubular structures by human microvascular endothelial cells (hMVEC) in an in vitro angiogenesis model. Opaque [125I]fibrin structures prepared at pH 7.0, fibrin matrices at pH 7.4 and transparent [125I]fibrin structures prepared at pH 7.8 were neutralized (pH 7.4) before seeding hMVEC on top of them in confluent density. Endothelial cells were stimulated with a growth factor [basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF)165] and a cytokine [tumor necrosis factor (TNF)-alpha] to induce the u-PA/u-PA receptor-dependent formation of capillary-like tubular structures. The formation of these structures was quantified by determining the length of the invasive structures by image analysis and by measuring the accompanying [125I]fibrin degradation. Ingrowth of tubular structures proceeded at a faster rate in opaque matrices consisting of thick fibrin fibers as compared to transparent gels with fine fibrin fibers. The more rapid ingrowth of tubular structures in opaque fibrin gels induced by bFGF/TNF-alpha or VEGF165/TNF-alpha was accompanied by a larger extent of fibrin degradation. Both processes were inhibited by aprotinin and epsilon-aminocaproic acid indicating the involvement of plasmin. They were also inhibited by anti-u-PA or anti-u-PA receptor IgG, but not by anti-t-PA IgG, suggesting the involvement of cell-bound u-PA activity. However, in the opaque fibrin gels, the tubular structures dissolved upon prolonged incubation due to excessive fibrin degradation. Simulation of hMVEC with bFGF alone did not induce tubular structures, but ca used a high degree of t-PA- and plasmin-dependent fibrin lysis, and, after several days, a partial detachment of sheets of cells. Gradual inhibition of the excessive fibrin degradation by a series of aprotinin concentrations did not lead to tube formation in bFGF-treated cells. These data indicate that the formation and stability of tubular structures by hMVEC in fibrin is accompanied by controlled fibrinolysis and depends critically not only on cell-bound u-PA-dependent plasminogen activation, but also on the fibrin structure. Because the fibrin structure is largely influenced by the conditions in which fibrin has been polymerized, these conditions may have considerable impact on angiogenesis during wound healing and vascularization of tumour stroma.

Journal Article↗
PubMed2001

Interaction of amorphous calcium phosphate with fibrin in vitro causes decreased fibrinolysis and altered protease profiles: implications for atherosclerotic disease.

Previously, we demonstrated that amorphous calcium phosphate (ACP), chemical precursor to apatite, strongly interacted with fibrin and facilitated binding of matrix metalloproteinase (MMP)-9, a type IV collagenase. Plasmin-dependent fibrinolysis resulted in coordinate MMP-9 activation. Here we report on the effect(s) of ACP on fibrin degradation and binding of endogenous plasma proteases. Electrophoresis (8.5% SDS-PAGE) revealed that fibrin formed in the presence of ACP demonstrated characteristic gamma-gamma dimers (90-kDa) and beta-monomers (55-kDa), but resisted spontaneous fibrinolysis (72 h, 37 degrees C) or degradation by plasminogen activators (uPA, tPA). Casein zymography revealed an ACP-dependent decrease in fibrin binding of a low molecular weight (Mw) protease triplet (47-, 43-, 42-kDa) and increased fibrin binding of two high Mw proteases (94- and 84-kDa). The low Mw triplet also possessed gelatinolytic activity, but was not an MMP since 1,10-phenanthroline was ineffective as an inhibitor. Fibrin-binding proteases were inhibited to some degree by the serine protease inhibitor aprotinin. Competition/dissociation experiments with epsilon-aminocaproic acid revealed that the low Mw triplet lacked kringle regions whereas the 94- and 84-kDa proteases were tentatively identified and glu-/lys-plasmin(ogen)s. The triplet may, however, represent one or more kringle deficient mini-plasminogen(s), since electrophoretic mobility and substrate specificity was similar to elastase-generated mini-plasminogen. To explore these findings in a clinically relevant setting, a series of plasma samples was collected from a patient with unstable angina prior to, during, and post coronary artery bypass graft (CABG) surgery. Fibrin formed from plasma collected during and immediately post CABG was associated with increased fibrinolytic capacity and enhanced binding of a) MMP-9, b) the low Mw protease triplet (described above), and c) PA (as putative 110-kDa tPA:PAI-1 complex). The relevance of these findings to pathologic calcification of atherosclerotic plaques is discussed.

Aged↗
PubMed2002

Increasing paracellular porosity by E-cadherin peptides: discovery of bulge and groove regions in the EC1-domain of E-cadherin.

PURPOSE: The objective of this work is to evaluate the ability of peptides derived from the bulge (HAV-peptides) and groove (ADT-peptides) regions of E-cadherin EC1-domain to increase the paracellular porosity of the intercellular junctions of Madin-Darby canine kidney (MDCK) cell monolayers. METHODS: Peptides were synthesized using a solid-phase method and were purified using semi-preparative HPLC. MDCK monolayers were used to evaluate the ability of cadherin peptides to modulate cadherin-cadherin interactions in the intercellular junctions. The increase in intercellular junction porosity was determined by the change in transepithelial electrical resistance (TEER) values and the paracellular transport of 14C-mannitol. RESULTS: HAV- and ADT-peptides can lower the TEER value of MDCK cell monolayers and enhance the paracellular permeation of 14C-mannitol. HAV- and ADT-decapeptides can modulate the intercellular junctions when they are added from the basolateral side but not from the apical side; on the other hand. HAV- and ADT-hexapeptides increase the paracellular porosity of the monolayers when added from either side. Conjugation of HAV- and ADT-peptides using omega-aminocaproic acid can only work to modulate the paracellular porosity when ADT-peptide is at the N-terminus and HAV-peptide is at the C-terminus; because of its size, the conjugate can only modulate the intercellular junction when added from the basolateral side. CONCLUSIONS: Peptides from the bulge and groove regions of the EC1 domain of E-cadherin can inhibit cadherin-cadherin interactions, resulting in the opening of the paracellular junctions. These peptides may be used to improve paracellular permeation of peptides and proteins. Furthermore, this work suggests that both groove and bulge regions of EC-domain are important for cadherin-cadherin interactions.

Animals↗
PubMed2001

Binding of Amadori glucose-modified albumin by the monocytic cell line MonoMac 6 activates protein kinase C epsilon protein tyrosine kinases and the transcription factors AP-1 and NF-kappaB.

An affinity purification procedure is employed for the isolation of FL-specific binding proteins from MM6 cell membranes using magnetobeads coated with glycated polylysine and elution with FL and glycated 6-aminocaproic acid. Two main binding proteins were identified as membrane-bound nucleolin and cellular myosin heavy chain, which are glycosylated. This study shows that in these cells binding of short-term glycated albumin leads to activation of PKC, especially its isoform epsilon and this is linked to translocation of AP-1 and NF-kappaB into the nucleus. Consequently, an increased formation of IL-1ss mRNA is observed. The PKC inhibitor GO6976 prevents all these effects. Glycated albumin also stimulates activation of PTK. The PTK inhibitor genistein prevents activation of AP-1 indicating that PTK is also involved in this process, whereas NF-kappaB translocation is only dependent on PKC activation.

Carrier Proteins↗
PubMed1998

Binding of latent matrix metalloproteinase 9 to fibrin: activation via a plasmin-dependent pathway.

The binding of two matrix metalloproteinases (MMP) to fibrin was evaluated. MMP-2 (72-kDa) and MMP-9 (92-, 130-, and 225-kDa) were selected since both contain a fibronectin-like region and fibronectin binds fibrin. Gelatin zymography indicated selective and dose dependent binding of MMP-9 to fibrin. No MMP-2 binding to fibrin occurred. Densitometry revealed that the 130- and 225-kDa forms demonstrated similar sigmoidal binding profiles whereas 92-kDa uptake was hyperbolic. Fibronectin and TIMP-1 competition studies indicated that the fibronectin and C-terminal MMP-9 domains, respectively, were not involved with fibrin binding. The MMP-9 collagen-like region may be of regulatory significance since type I and II fibrillar and type IV basement membrane collagens demonstrated fibrin binding. During fibrinolysis, latent fibrin-bound MMP-9 was processed to lower molecular weight forms consistent with proteolytic activation. This process was inhibited by epsilon-aminocaproic acid, indicating a plasmin-dependent pathway. The significance of these findings to procoagulant activity and MMP-mediated extracellular matrix destruction during inflammation and tumor invasion and metastasis is discussed.

Collagenases↗
PubMed1999

[Chronic, hemorrhage-induced iron deficiency anemia in Osler disease].

We report the history of a 77-year-old man with Osler-Weber-Rendu disease (hereditary hemorrhagic telangiectasia) who suffered from recurrent epistaxis and chronic bleeding anemia for many years. Hereditary hemorrhagic telangiectasia is a rare congenital disease, that is characterized by telangiectases of the nasal and oral mucosa, the gastrointestinal tract and the skin. Arteriovenous malformations of the lung and the brain may be present. The genetic and pathologic features, the clinical manifestations and the differential diagnosis are shortly presented. The management is not validated by controlled studies and is mainly based on clinical experience. It involves supportive therapy with iron supplementation and erythrocyte transfusions, if needed, for chronic bleeding anemia, aminocaproic acid, tranexamic acid or oestrogen-progesterone therapy to prevent mucosal bleeding, cauterisation, photocoagulation, transcatheter embolotherapy or surgery to treat the vascular abnormalities.

Aged↗
PubMed1996

Development and clinical application of a new ELISA assay to determine plasmin-alpha2-antiplasmin complexes in plasma.

Plasmin-alpha2-antiplasmin complexes (PAP) are considered good markers of fibrinolytic activation in vivo. The presence of neoantigens in these complexes offers the possibility to develop specific immunoassays to determine PAP levels. We have developed a sensitive PAP purification method in vitro by adding urokinase to fresh plasma followed by affinity chromatography to lysine-sepharose and elution with epsilon-aminocaproic acid. This material, characterized by SDS-PAGE and Western blotting, was used to raise monoclonal antibodies (MoAbs). We describe a new enzyme linked immunosorbent assay (ELISA) to quantify PAP complexes in plasma. The assay follows the sandwich principle and is based on two MoAbs, CPL12 and CPL15, that bind to the modified alpha2-antiplasmin moiety and the plasmin moiety of the complex respectively. The calibration curve was constructed with definite concentrations of purified PAP. The lower limit of the assay is 75 ng/ml and the variation coefficients are 3.5% (intra-assay) and 10-6% (interassay). A mean value of 573.5+/-131.4 ng/ml was obtained from PAP concentration in a healthy population (n = 30). Significantly higher PAP levels were observed under diverse clinical conditions in which fibrinolysis is activated: clinical sepsis, acute myocardial infarction (AMI), malignancy, diabetes, pregnancy, elderly people and thrombolytic therapy. From our results we conclude that this ELISA is suitable to measure in vivo plasma PAP levels.

Antibodies, Monoclonal↗
PubMed2003

Effect of various stabilizing agents on Imperata cylindrica grass pollen allergen extract.

BACKGROUND: Allergen extracts are unstable, heat labile or susceptible to proteases. Stability of allergen extracts is important for proper diagnosis and therapy of allergic disorders. OBJECTIVE: The present study was undertaken to determine the preservation and stabilization conditions of Imperata cylindrica (Ic) grass pollen extract. METHODS: The Ic extract was kept with 0.1 mepsilon-aminocaproic acid (EACA), 0.75 m sucrose, 5% glycerol, 0.03% human serum albumin (HSA) or 0.4% phenol for different time periods. The extracts were stored for 3, 6 and 12 months each at 4 degrees C, 4 degrees C with daily exposure to room temperature (RT) for 1 h, and RT. The quality of extracts was analysed by SDS-PAGE, Western blot, ELISA, ELISA inhibition and skin test. RESULTS: Extracts kept with EACA and sucrose retained most of the protein bands followed by glycerol as determined by SDS-PAGE and Western blot during all storage periods and conditions in comparison with standard extracts. The extracts kept with HSA, phenol and without preservative (WP) showed protein degradation below 33 kDa after 3 months storage at all conditions. However, a 67-kDa allergen was stable in these extracts. EACA extract required 75 to 120 ng of protein for 50% inhibition in IgE binding under different conditions, whereas standard extract required 70 ng for the same. ELISA also demonstrated high allergenic reactivity of EACA extract. ID test on allergy patients with EACA extract demonstrated same allergenic potency as that of standard extract. CONCLUSION: EACA is the best preservative/stabilizing agent of Ic pollen extract, followed by sucrose and glycerol. Ic extract kept with phenol, HSA and without preservative showed degradation within 3 months. EACA preserved extract is equally potent as that of standard extract up to 1 year's storage.

Allergens↗
PubMed2001

Heart transplant in a factor VIII-deficient patient with a high-titre inhibitor: perioperative management using high-dose continuous infusion factor VIII and recombinant factor VIIa.

Four years prior to transplantation, a 14-year-old boy with severe haemophilia A and a high-responding factor VIII (FVIII) inhibitor developed an anteroseptal myocardial infarct while receiving high doses of an activated prothrombin complex concentrate (PCC). Cardiac transplantation was required for survival because of the ensuing cardiomyopathy. At surgery, the patient's inhibitor titre was 1.8 Bethesda units (BU). High-dose bolus therapy, followed by a continuous infusion of FVIII provided excellent operative and initial postoperative haemostasis without additional blood-product support. Once anamnaesis developed on day 6 postoperatively, recombinant factor VIIa (rFVIIa) therapy was initiated. Haemostasis remained excellent, except for the transient increase in chest-tube bleeding that was noted on day 7. epsilon-Aminocaproic acid was added and haemostasis was re-established. On day 15, rFVIIa was replaced with alternate day infusions of prothrombin complex concentrates (PCCs). On day 21 following the transplant, the patient was discharged, remaining on daily FVIII immune tolerance and thrice-weekly PCC prophylaxis. He remains well 24 months after transplant with an inhibitor titre of 39 BU. This paper describes the second case of cardiac transplantation complicated by haemophilia and an inhibitor, and discusses preoperative planning and operative and postsurgical haemostasis management.

Adolescent↗
PubMed2003

Painless urethral bleeding: an unusual presentation of Von Willebrand disease.

Von Willebrand disease (vWD) is the most common bleeding disorder, and usually presents with either easy bruising or mucus membrane bleeding. Many patients are also diagnosed as a result of abnormal pre-operative laboratory tests. In this report, we describe two patients presenting with painless, persistent urethral bleeding as their initial manifestation of vWD. The first patient began bleeding after a Foley catheter was placed during a hospital admission for status epilepticus. A urologic examination demonstrated a wound in the posterior urethra. Despite repeated attempts at controlling the bleeding with cautery, the bleeding persisted. The second patient presented with spontaneous urethral bleeding and a normal urologic examination. Due to persistent bleeding, both patients underwent a coagulation evaluation that demonstrated the presence of type 1 vWD. The first patient had resolution of his bleeding following 5 weeks of Alphanate, a von Willebrand factor containing factor VIII concentrate, and aminocaproic acid. The second patient initially responded to desmopressin, but subsequently required Humate-P to achieve complete resolution. These cases illustrate the importance of an evaluation for bleeding disorders in patients with persistent bleeding from any site.

Adolescent↗
PubMed2001

Utilization of technologies to reduce allogeneic blood transfusion in the United States.

Concern over safety of the blood supply has led to the use of technologies to reduce allogeneic blood transfusion. The objective of this research was to determine the utilization of these technologies in the United States. We evaluated the following techniques: preoperative autologous donation (PAD), cell salvage (CS) and acute normovolemic haemodilution (ANH); and the following pharmaceuticals: aprotinin (APR), epsilon-aminocaproic acid (EACA), tranexamic acid (TXA), desmopressin (DDAVP) and recombinant human erythropoietin (EPO). In 1997, we conducted a cross-sectional mail survey of service chiefs at 1000 US hospitals randomly selected and stratified by status as a provider of open-heart surgery, geographical location and hospital bed size. Sixty-nine per cent (690) of hospitals responded to at least one of the four surveys sent to each hospital. Hospitals reported use of techniques more than pharmaceuticals (P < 0.001); PAD (83%, n = 206) and CS (82% n = 420) were used most frequently. Lack of familiarity was the most common reason cited for infrequent use of pharmaceuticals. Organizational characteristics (e.g. provision of open-heart surgery, size, geographical location, teaching status and type of hospital) were differentially associated with technology use. There is greater use of techniques than pharmaceuticals in US hospitals to reduce the need for allogeneic blood in the peri-operative setting. Providing open-heart surgery is strongly associated with the utilization of these technologies.

Biomedical Technology↗
PubMed2006

Renal dysfunction after thoracic aortic surgery requiring deep hypothermic circulatory arrest: definition, incidence, and clinical predictors.

OBJECTIVE: The purpose of this study was to evaluate renal dysfunction (RD) after thoracic aortic surgery (TAS) requiring deep hypothermic circulatory arrest (DHCA), to determine the influence of definition on RD after TAS-DHCA, to determine univariate predictors of RD after TAS-DHCA, and to determine multivariate predictors for RD TAS-DHCA. RD was defined in 3 ways: (1) >25% reduction in creatinine clearance, (2) >50% increase in serum creatinine, and (3) >50% increase in serum creatinine with an abnormal peak serum creatinine (>1.3 mg/dL for men and >1.0 mg/dL for women). STUDY DESIGN: Retrospective and observational. STUDY SETTING: Single large university hospital. PARTICIPANTS: All adults requiring TAS-DHCA in 2000 and 2001. MAIN RESULTS: The cohort size was 144. Antifibrinolytic exposure was 100%: aprotinin 66% and aminocaproic acid 34%. The incidence of RD TAS-DHCA was 22.9% to 38.2%, depending on the definition. The incidence of renal replacement therapy was 2.8%. Multivariate predictors for RD after TAS-DHCA were sepsis, aprotinin exposure, preoperative hypertension, age, and donor exposures. CONCLUSIONS: Although RD after TAS-DHCA varies substantially because of definition, it is still very common. Its multivariate predictors merit further focused research to enhance perioperative protection of the kidney.

Adult↗
PubMed2001

Blood loss in elective coronary artery surgery: a comparison of centrifugal versus roller pump heads during cardiopulmonary bypass.

OBJECTIVES: To compare the effects of centrifugal pumps versus roller pumps for cardiopulmonary bypass (CPB) in routine cardiac surgery on hematologic parameters in the context of modern practice. DESIGN: Prospective, randomized, partially blinded. SETTING: University teaching hospital. PARTICIPANTS: Elective coronary artery surgery patients (n = 113) INTERVENTION: Patients were randomized to be perfused with either a roller head (group R, n = 56) or a centrifugal head (group C, n = 57) pump. Patients received epsilon-aminocaproic acid before and during CPB. Core body temperatures were allowed to drift down to approximately 32 degrees C. MEASUREMENTS AND MAIN RESULTS: Postoperative chest tube blood loss, blood product requirements, hemoglobin, and platelet counts were assessed. There were no significant differences in preoperative or intraoperative parameters, including CPB time, complexity of procedure, and minimum core temperature. There were the expected reductions in hemoglobin and platelet levels post-CPB in both groups to a similar extent. Chest tubes remained in situ for similar durations, and the final volume of drainage was not significantly different (group C, 1300 +/- 92 mL; group R 1117 +/- 83 mL; p = 0.14). Allogeneic blood was given to 23% of patients in group C and 18% in group R (p = 0.63). Aspirin was associated with an increase in early chest tube drainage. CONCLUSIONS: In this surgical and perfusion environment, the authors were unable to show an advantage, from the hematologic point of view, in the routine use of a centrifugal pump head in elective coronary artery surgical patients. The use of antifibrinolytic agents and mild hypothermia may have effects on hemostasis that overshadow the influence of pump head design in this type of surgery.

Aged↗