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At least 253 records · Page 14Linked to original sources
PubMed1999

Oligonucleotide therapeutics for hematologic disorders.

During the last decade, the catalogue of known genes responsible for cell growth, development, and neoplastic transformation has expanded dramatically. Attempts to translate this information into new therapeutic strategies for both hematologic and non-hematologic diseases have accelerated at a rapid pace as well. Inserting genes into cells which either replace, or counter the effects of disease causing genes has been one of the primary ways in which scientists have tried to exploit this new knowledge. Strategies to directly downregulate gene expression have developed in parallel with this approach. The latter include triple helix forming oligonucleotides (ODN) and 'antisense' ODN. The latter have already entered clinical trials for a variety of disorders. In this monograph, we review the use of these materials in the treatment of hematologic diseases, particularly myelogenous leukemias. Problems and possible solutions associated with the use of ODN will be discussed as well.

Animals↗
PubMed1975

The erythrocyte sedimentation rate, rouleaux formation and hyperviscosity syndrome. Theory and fact.

Uncomplicated hyperviscosity syndrome secondary to hypergammaglobulinemic states seems to be associated with rouleaux formation on the peripheral blood film and a normal or near normal erythrocyte sedimentation rate. Conversely, the concomitant finding of rouleaux formation with a normal erythrocyte sedimentation rate is highly suggestive of the hyperviscosity syndrome. The theoretical and factual justifications for this hypothesis are presented.

Adult↗
PubMed1978

Factor VIII activity and antigen in sick newborns with pathological proteolysis in blood.

Factor VIII clotting activity (VII:C) and factor VIII related antigen (VIII:R:AG) were determined in 12 sick newborn infants with pathological proteolysis in their circulation. A marked discrepancy was noted between VIII:R:AG and VIII:C, the ratio in sick infants being, on average, 2:1, while no discrepancy was seen in healthy newborns. The finding in the sick infants resembled a low grade plasminogen activation, which was studied experimentally. It is concluded that demonstration of a marked discrepancy between VIII:R:AG and VIII:C is a useful indication of pathologic proteolysis in sick newborns.

Antigens↗
PubMed1971

Functional evaluation of an inherited abnormal fibrinogen: fibrinogen "Baltimore".

The rate of clotting and the rate of development and degree of turbidity after addition of thrombin to plasma or purified fibrinogen from a patient with fibrinogen Baltimore was delayed when compared with normal, especially in the presence of low concentrations of thrombin. Optimal coagulation and development of translucent, rather than opaque, clots occurred at a lower pH with the abnormal fibrinogen than with normal. Development of turbidity during clotting of the abnormal plasma or fibrinogen was less than normal at each pH tested, but was maximal in both at approximately pH 6.4. The physical quality of clots formed from fibrinogen Baltimore was abnormal, as demonstrated by a decreased amplitude on thromboelastography. The morphologic appearance of fibrin strands formed from fibrinogen Baltimore by thrombin at pH 7.4 was abnormal when examined by phase contrast or electron microscopy, but those formed by thrombin at pH 6.4 or by thrombin and calcium chloride were similar to, though less compact, than normal fibrin. The periodicity of fibrin formed from fibrinogen Baltimore was similar to normal and was 231-233 A.A study of the release of the fibrinopeptides from the patient's fibrinogen and its chromatographic subfractions verified the existence of both a normally behaving and a defective form of fibrinogen in the patient's plasma. The defective form differed from normal in three functionally different ways: (a) the rate of release of fibrinopeptides A and AP was slower than normal; (b) no visible clot formation accompanied either partial or complete release of the fibrinopeptides from the defective form in 0.3 M NaCl at pH 7.4; and (c) the defective component possessed a high proportion of phosphorylated, relative to nonphosphorylated, fibrinopeptide A, while the coagulable component contained very little of the phosphorylated peptide (AP). The high phosphate content of the defective component did not appear to be the cause of the abnormality, but may be the result of an associated metabolic or genetic phenomenon.

Blood Coagulation↗
PubMed1975

Defective alpha-polymerization in the conversion of fibrinogen Baltimore to fibrin.

The subunit structure of fibrinogen Baltimore and fibrin formed from this inherited dysfibrinogenemia was analyzed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. The molecular weights of the alpha-, b- and gamma-chains of fibrinogen Baltimore were found to be identical to those of normal fibrinogen. Noncross-linked fibrin formed from both purified fibrinogen Baltimore as well as normal fibrinogen contained two alpha-monomers (alpha1 and alpha2). alpha2 was presumed to be alpha-monomer from which fibrinopeptide A had been released. The evolution of alpha2 during clotting of fibrinogen Baltimore was delayed and appeared to be quantitatively reduced when compared to normal. Crosslinked fibrin formed from fibrinogen Baltimore possessed an abnormal subunit structure. alpha-polymers were not generated in thrombin-induced, factor XIII-rich clots of fibrinogen Baltimore under conditions of pH and calcium concentration suitable for complete alpha-polymerization in normal fibrin. If clotting was carried out with calcium concentrations twice that required for normal clots or at pH 6.4, fibrin from fibrinogen Baltimore was completely cross-linked. These structural analyses of fibrin formed from fibrinogen Baltimore substantiate earlier findings that indicate a defect in the alpha-chain of this dysfibrinogenemia.

Blood Coagulation Disorders↗
PubMed1994

Activation of the plasma clotting, fibrinolytic, and kinin-kallikrein system in preterm infants with severe idiopathic respiratory distress syndrome.

We studied the activation pattern of clotting, fibrinolysis, and kinin-kallikrein during the first 5 d of life in 10 preterm infants with signs of severe idiopathic respiratory distress syndrome (IRDS) after birth (IRDS group) and in 12 healthy preterm infants (reference group). We found systemic activation of clotting, fibrinolysis, and kinin-kallikrein in the IRDS infants within 12 to 24 h of birth, represented by increased median thrombin-antithrombin III complex formation (90 ng/mL versus 10 ng/mL in the reference group, p < 0.05), increased mean tissue-type plasminogen activator plasma concentrations (11.8 ng/mL versus 3.5 ng/mL in the reference group, p < 0.05), and increased mean plasma kallikrein activity (182.6% versus 162.0% of maximal activated human plasma in the reference group, p < 0.05), respectively. Clotting activation was accompanied by a significant decrease of the platelet count. Clotting and fibrinolytic activity decreased in the IRDS group during the first 2 to 3 d of life. Kinin-kallikrein activation was accompanied by decreased plasma kallikrein inhibitor activity values and did not change throughout the study period. Plasma factor XII activity was not significantly increased in the IRDS infants during the first 2 d of life but did significantly increase thereafter. The cause of simultaneous activation of clotting, fibrinolysis, and kinin-kallikrein in our IRDS infants has not yet been clarified. However, this activation process may contribute to lung injury such as that described in the adult respiratory distress syndrome.

Antithrombin III↗