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At least 865 records · Page 48Linked to original sources
PubMed2000

Assembly of the Heparin Removal Device for patients with suspected adverse reaction to protamine sulphate.

Protamine sulphate is routinely used after cardiopulmonary bypass (CPB) to restore the patient's baseline coagulatory state. However, adverse reactions are encountered, and alternative means to neutralize heparin are, therefore, necessary. The Heparin Removal Device (HRD) constitutes an extracorporeal circuit that allows ex vivo deheparinization by mean of a polycationic ligand that binds heparin molecules. This paper presents the setup of the HRD circuit. It is illustrated by the report of a 68-year-old man with a known severe crustacean allergy. The patient (78 kg, 170 cm) was admitted for elective coronary artery bypass graft surgery. It was decided that the HRD would be used as a precaution in order to avoid the risks of using protamine sulphate. The CPB time and aortic crossclamp time were 70 and 40 min, respectively. At the end of CPB, the device was inserted and processing started. Activated coagulation time values were monitored over a 130 min period and diminished from 480 to 300 s after 45 min, 220 s after 90 min, and settled at 150 s. Haemostasis was acceptable and processing stopped. The operation was terminated and the patient transferred to the intensive care unit. Clinical evolution was excellent, with minimal postoperative bleeding. The HRD presents an alternative to protamine sulphate when this drug is contraindicated for a certain patient population who might have a suspected, known or emergency adverse reaction.

Aged↗
PubMed1993

Complement (C3, C4) and C-reactive protein responses to cardiopulmonary bypass and protamine administration.

Complement activation has been deemed responsible for the damaging effects of cardiopulmonary bypass (CPB) in patients undergoing open heart surgery. We studied C3, C4 and C-reactive protein (CRP) in 22 patients undergoing CPB. In Group 1 (11 patients), protamine was given intravenously and in Group 2 (11 patients), via the aortic root after CPB. Significant decreases were observed in C3 and C4 during CPB in both groups indicating complement activation primarily by the classic pathway. Protamine did not lead to further activation of the complement system. In both groups, C3 levels gradually returned toward baseline within 24 hours but C4 levels were still lower than baseline 24 hours postoperatively. CPB and protamine administration did not cause any significant changes in CRP levels, but CRP increased abruptly 24 hours after operation. Although activation of complement system during CPB is expected to invoke an acute phase response, we conclude that this period is not long enough to induce an increased production of CRP in response to tissue injury or inflammation.

Adult↗
PubMed1977

The anatomy of cooperative binding between protamines and DNA.

DNA was titrated with protamine under equilibrium conditions while binding was simultaneously followed by electron microscopy and the fluorescamine technique. Positive cooperativity concluded from the binding assays was shown to be correlated with an aligned association of DNA fibres. Subsequent structural modifications, dependent upon the protamine/DNA ratio, suggests a mechanism for DNA compaction by protamines. In the framework of this model, protamine phosphorylation appears to promote formation of DNA interstrand links yielding a very pronounced filigree structure.

Clupeine↗
PubMed1989

Determination of soluble fibrin by turbidimetry of its protamine sulphate-induced paracoagulation.

Protamine sulphate-induced aggregation of soluble fibrin causes an increase of turbidity in the plasma sample, which can be measured by means of kinetic turbidimetry. A method was developed which is sufficiently sensitive for the determination of soluble fibrin in plasma without interfering with the sensitivity for fibrinogen. The performance of the assay was studied by analysing plasma samples with high concentrations of fibrinogen and soluble fibrin at different pH values, at different concentrations of plasma and protamine sulphate, and using different wavelengths and analysis times. Measurement of thrombin-induced fibrinogen-fibrin-transformation by the developed turbidimetric method, gave results that correlated well with the release of fibrinopeptide A. The new protamine sulphate method for turbidimetric determination of soluble fibrin is characterized by its practicability, rapid availability of reproducible, quantitative results, and its economy of reagents and time in single and serial analysis. Therefore it seems well-suited for the routine diagnosis of hypercoagulability with increased fibrinogen turnover.

Blood Coagulation↗
PubMed1990

Immunocytochemical localization of nuclear protamine in boar spermatozoa during epididymal transit.

Protamine was specifically demonstrated in boar spermatozoa collected from the rete testis, caput, corpus and cauda epididymidis and the ejaculate by immunoelectron microscopy, using anti-boar or anti-ram protamine antisera and an indirect post-embedding immunogold technique. Spermatozoa from all collection sites stained after incubation although with different degrees of labelling. Controls were negative. Labelling increased from the rete testis towards the epididymal corpus, where it was most intense, decreasing sharply thereafter. The weakest binding of the assayed antibodies was obtained in the ejaculated spermatozoa but it could be reversed by in-vitro induction of chromatin decondensation with sodium dodecyl sulphate and the metal-chelating EDTA. The finding of a significant decrease in the immunolabelling detected from the corpus epididymidis onwards indicates a critical point for the interaction between DNA and the protamines in boar spermatozoa during the epididymal maturation.

Animals↗
PubMed1976

Comparison between a modified ethanol gelation test and protamine sulfate test. Experimental studies.

A comparative experimental study has been made to correlate the protamine sulfate test and a modified ethanol gelation test, based on clinical observations of the solubility of a gel formed at 20 degrees C (Godal and Abildgaard procedure) when it was transferred to a bath at 37 degrees C. Two different results were obtained: the gel remained insoluble at 37 degrees C or it became completely soluble, with intermediate degrees of partial solubility. Our studies indicate that this is due to the amount of fibrin monomers formed and the level of fibrinogen: the first are responsible for the insolubility of the gel and the second for its solubility. This furnishes us with useful information for diagnostic purposes. We found the protamine sulfate test more sensitive than the ethanol gelation test, and its sensitivity increased when fibrinogen level decreased. An insoluble gelation test is a sure indication of the presence of fibrin monomers, but a soluble gel calls for the protamine sulfate test to confirm this or the existence of high fibrinogen level.

Ethanol↗
PubMed2000

[Catastrophic pulmonary vasoconstriction associated with protamine reversal of heparin].

Administration of protamine intravenously to neutralize the anticoagulant effects of heparin may be associated with hypotension. These adverse cardiovascular responses to protamine fall into three distinct types: transient hypotension related to rapid drug administration; anaphylactic responses: and catastrophic pulmonary vasoconstriction. We recently observed three patients who had catastrophic pulmonary vasoconstriction, which were treated with the assist circulation and intraaortic balloon pumping. The two patients were survived except one who was dead due to the cerebral ischemic damage which was introduced by delayed establishment of circulatory assist device. We conclude that meticulous longstanding observation of the hemodynamic condition is important after administration of protamine under the unremoved cannulations.

Aged↗
PubMed1975

Heparin therapy during extracorporeal circulation. II. The use of a dose-response curve to individualize heparin and protamine dosage.

Because the administration of heparin and protamine according to a set protocol will fail to anticoagulate safely or neutralize appropriately a significant number of patients, a method of monitoring heparin therapy during cardiopulmonary bypass is presented. A dose response curve relating heparin dosage to its effect on the activated coagulation time (ACT) can be determined with sufficient accuracy for clinical purposes from three ACT's. Preparation of such a curve makes it possible to maintain anticoagulation in a safe range during bypass and minimizes the number of monitoring tests of coagulation required. At the conclusion of bypass, this curve can be used to predict the precise amount of protamine needed for neutralization. Freed from the confusing effects of hyperheparinemia or protamine excess, the physician can diagnose and treat postoperative bleeding problems much more readily.

Blood Coagulation Tests↗
PubMed1976

Assay of protamine messenger RNA from rainbow trout testis.

A low molecular weight RNA fraction possessing protamine mRNA activity was prepared from rainbow trout testis polysomes. Addition of low molecular weight RNA to a Krebs II ascites S-30 cell-free protein synthesis system strongly stimulated [14C]arginine incorporation into acid-insoluble material. This stimulation was completely abolished by 10-4 M aurintricarboxylic acid, an inhibitor of eukaryotic protein synthesis at the level of initiation. Starch gel electrophoresis showed that labeled arginine was incorporated in vitro into products identical with both authentic protamine and histones as found previously (Gilmour, R. S., and Dixon, G. H. (1972) J. Biol. Chem. 247, 4621-4627). The 4 to 6 S RNA fraction, isolated from the polysomal low molecular weight RNA by sucrose gradient fractionation, enhanced the incorporation of [14C]arginine into acid-insoluble material and when this product was examined by starch gel electrophoresis, it co-migrated with authentic rainbow trout protamine.

Animals↗
PubMedDate not supplied

[Properties of protamine-heparin complexes].

Protamine-heparin complexes have a considerable resistance to physical factors of the environment such as a high ion strength and acid or alkaline pH. Free protamine is digested by plasmin giving products with a greatly decreased ability to form complexes with heparin and lower antiheparin action. Bound protamine, on the other hand, is resistant to the action of plasmin as a result of which the enzyme does not release heparin from the complexes.

Fibrinolysin↗
PubMed2006

[Structure and role of protamines 1 and 2 in spermatogenesis and male infertility].

In the last decade the abnormalities in male infertility became the main problem of more than 50% couples. The main reasons of male infertility are abnormal gonadotropin releasing hormone (GnRH) secretion, pituitary gland diseases and presence of testicular genetic defects. The male infertility also may result from chemotherapy, radiotherapy and viral infections. The main genetic factors responsible for male infertility encompass the mutations of genes, which encode important factors of spermatogenesis. Recently mRNAs of numerous genes have been identified in spermatozoa. The first transcripts found in spermatozoa included protamine 1 and 2 (PRM1 and PRM2). Protamines are basic polypeptides, which form complex with DNA in spermatids and spermatozoa. Structure of PRM1 and PRM2 genes and function of these proteins suggest the possible relationship between of protamines expression disorders and male infertility. The PRM1, PRM2 and transition proteins 1 and 2 (TP1 and TP2) play important role in DNA condensation. We attempted to present current knowledge regarding structure and expression regulation of PRM1 and PRM2 genes. We also discussed the effect of disorders of PRM1 and PRM2 expression on male infertility.

Amino Acid Sequence↗
PubMedDate not supplied

[Comparison of two schemes of administering the Russian protamine sulfate after extracorporeal circulation in cardiosurgical patients].

The paper presents data of a study comparing two schemes (Scheme 1: a heparin/protamine ratio of 1:2; Scheme 2: a heparin/protamine ratio of 1:3) for administering protamine sulfate to neutralize heparin in patients after extracorporeal circulation. A larger dose of protamine sulfate is shown to induce significant thrombocytic dysfunction, resulting in increased postoperative hemorrhage. To minimize protamine sulfate doses required for neutralization of the anticoagulant effect of heparin is a way of preventing these complications.

Blood Platelets↗
PubMedDate not supplied

[Protamine as a specific inhibitor of electron transport between cytochromes c and a on the outer surface of the mitochondrial membrane].

The basic protein protamine is found to be a potent inhibitor of mitochondrial cytochrome c oxidase, while the oxidase activity of the "inside out" submitochondrial particles is only slightly affected by this polycation. The site of inhibition of mitochondrial respiration by protamine is localized between cytochromes c and a, protamine combining with cytochrome oxidase competitively to cytochrome, c, Ki=2,5 x 10(-6) M. The data obtained suggest that it is the outer side of the mitochondrial membrane where oxidation of cytochrome c by cytochrome a occurs.

Animals↗
PubMedDate not supplied

A protamine-mediated heparin sensing device.

A convenient, protamine mediated strip assay for heparin was developed. The assay is established on the specific interaction between heparin and protamine, and the metachromatic color change of methylene blue dye from blue to purple in the presence of heparin. The device consists of a fibrin cup fabricated with a cellulose paper strip containing immobilized protamine. To analyze plasma heparin levels, a fixed volume of the test sample is placed in the fibrin cup and allowed to migrate through the strip in a descending manner until exhaustion. The region to which heparin binds is then visualized as purple in color by spraying methylene blue dye onto the strip. The heparin level in the sample is estimated from the length of the purple region using a preconstructed standard curve. This device proved to be capable of detecting and differentiating heparin in clinically relevant concentrations.

Heparin↗
PubMed1991

[Blood lipoproteins in modeling of atherosclerosis and administration of protamine].

The influence of protamine on the HDL, LDL, VLDL species concentration variation as well as on their cholesterol and protein content in respect to total blood serum cholesterol in different periods (1 and 7 months) of hypercholesteremia in rabbits is investigated. Daily administration of protamine (10 mg/kg) during 30 days to intact animals did not change the investigated parameters. In the early period of hypercholesteremia protamine considerably increased the content of all lipoprotein fractions. Under the conditions of prolonged hypercholesteremia the LDL and VLDL concentrations decreased by 23 and 60 per cent, respectively; HDL increased by 101 per cent.

Animals↗
PubMed1991

Adducts in sperm protamine and DNA vs. mutation frequency.

In mammals, variability in the genetic sensitivity of different germ-cell stages to mutagens could be the result of how much chemical reaches the different stages, what molecular targets may be affected in the different stages and whether or not repair of lesions occurs. In the mouse, several chemical mutagens have been found that cause their greatest genetic damage in late-spermatid and early-spermatozoa stages and that also bind very strongly to the protamine in these stages. Chemicals which are less genetically damaging to these stages have been found to have much less affinity for protamine. Furthermore, the level of chemical binding to DNA in late-spermatid and early-spermatozoa stages has not been correlated with the level of induced genetic damage, although DNA breakage in these sensitive stages has been shown to increase. This DNA damage is believed to indirectly result from chemical binding to sulfhydryl groups in protamine which prevents normal chromatin condensation within the sperm nucleus.

Acrylamide↗
PubMed1977

[Influence of hemodialysis, heparin and protamin on the pre-beta fraction of lipoproteins in patients with chronic kidney failure].

The spectrum of lipoproteins in the serum and the blood clotting time was examined in 19 dialyzed and 5 non-dialyzed patients with chronic renal failure. Compared were the values obtained in hemodialysis with intermittent and regional heparinization and the changes after the application of heparin in hemodialysis and beside it. In non-dialyzed and dialyzed patients in interdialyzation period were studied the changes of given parameters which occur after heparin and protamin application. Out of the results of this examination it follows that: 1. the most significant factor causing the changes of lipoprotein spectrum in the serum during hemodialysis is heparin. 2. the effect of protamin upon the lipoprotein spectrum during hemodialysis cannot be explained only by the neutralisation of heparin effect. 3. beside heparin and protamin in the spectrum changes of lipoproteins during hemodialysis also other factors are participant that are concerned with hemodialysis.

Blood Coagulation↗
PubMedDate not supplied

In vitro and in vivo effect of heparin, chondroitin, dextran and protamine on the virulence of pseudorabies virus (Suid herpesvirus 1).

The possible antiherpetic effect of three polyanions (heparin, chondroitin sulfate and dextran sulfate), as well as one polycation (protamine sulfate) was tested in vitro and in vivo against pseudorabies virus (Suid herpesvirus 1). The in vitro experiments revealed that heparin, dextran sulfate and protamine sulfate significantly reduced the number of lytic plaques. Chondroitin sulfate only caused a decrease in mean plaque size. Experiments in vivo disclosed that heparin injected subcutaneously before the experimental infection, was the only polyanion that protected mice against pseudorabies virus. Protamine sulfate had a paradoxic effect: whereas in vitro it reduced the number of lytic plaques, in vivo it increased the lethality of pseudorabies virus. Chondroitin sulfate and dextran sulfate did not modify the virulence of the virus in mice.

Animals↗