Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023473 (chronic myeloid leukemia)
 18,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Actin, myosin, and a high molecular weight actin-binding protein were purified from chronic myelogenous leukemia (CML) leukocytes. CML leukocyte actin resembled skeletal muscle and other cytoplasmic actins by its subunit molecular weight, by its ability to polymerize in the presence of salts, and to activate the Mg2+-ATPase activity of rabbit skeletal muscle myosin. CML leukocyte myosin was similar to other vertebrate cytoplasmic myosins in having heavy chains and two light subunits. However, its apparent heavy-chain molecular weight and Stokes radius suggested that it was variably degraded during purification. Purified CML leukocyte myosin had average specific EDTA- AND Ca2+-activated ATPase activities of 125 and 151 nmol Pi released/mg protein per min, respectively and low specific Mg2+-ATPase activity. The Mg2+-ATPase activity of CML myosin was increased 200-fold by rabbit skeletal muscle F-actin, but the specific activity relative to that of actin-activated rabbit skeletal muscle myosin was low. CML leukocyte myosin, like other vertebrate cytoplasmic myosins, formed filaments in 0.1 M KCl solutions. Reduced and denatured CML leukocyte-actin-binding protein had a single high molecular weight subunit like a recently described actin-binding protein of rabbit pulmonary macrophages which promotes the polymerization and gelation of actin. Cytoplasmic extracts of CML leukocytes prepared with ice-cold 0.34-M sucrose solutions containing Mg2+-ATP, dithiothreitol, and EDTA at pH 7.0 underwent rapid gelation when warmed to 25 degrees C. Initially, the gel could be liquified by cooling to ice-bath temperature. With time, warmed cytoplasmic extract gels shrunk ("contracted") into aggregates. The following findings indicated that CML leukocyte actin-binding protein promoted the temperature-dependent gelation of actin in the cytoplasmic extracts and that CML leukocyte myosin was involved in the contraction of the actin gels: (a) Cytoplasmic extract gels initially contained actin as their major polypeptide component and consistent of tangled thin filaments; (b) Contracted aggregates of cytoplasmic extract gels contained by large quantities of myosin as well as actin; (c) Purified actin-binding protein underwent a temperature-dependent, reversible aggregation and caused low concentrations of purified muscle or CML leukocyte actins to gel in sucrose solutions; (d) The gels formed from purified actin plus purified actin-binding protein slowly contracted in the presence but not in the absence of purified CML leukocyte myosin; (e) Rabbit antiserum against purified CML leukocyte actin-binding protein but not against purified CML leukocyte myosin inhibited the gelation of warmed CML leukocyte extracts. Antiserum against CML leukocyte myosin had no effect on the gelation of CML leukocyte extracts but partially curtailed the contraction of the CML leukocyte extract gels and of gels formed from purified CML leukocyte actin-binding protein plus rabbit skeletal muscle actin.
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PMID:Interactions of actin, myosin, and an actin-binding protein of chronic myelogenous leukemia leukocytes. 13 21

Because of recent developments in the study of vitamin B12-binding proteins, the levels of the three serum binders were compared in serum and plasma samples from subjects with various disorders. The results allow the following conclusions: (1) As previously reported, transcobalamin (TC) III and to a lesser extent TC I are artifactually elevated in serum. The appear to be released in vitro during the clotting process, presumably from granulocytes. (2) Blood cells of patients with polycythemia vera release exceedingly large amounts of TC I and TC III in vitro. (3) The above findings support, but do not prove, at least a partial granulocytic source of TC I. Nevertheless, factors other than granulocytes influence TC I levels, as disorders characterized by increased TC I (most prominently chronic myelogenous leukemia but also several cases of cancer) manifest relatively little cellular release of TC I in vitro. (4) Despite the serum artifact, the serum abnormalities described in various conditions were seen in plasma also, even though the actual values of themselves were lower in plasma. The chief exception was TC III, which was elevated in plasma only in polycythemia vera (and in a few cases of leukocytosis). (5) EDTA-NaF anticoagulant is not suitable, as it causes plasma dilution, thus explaining previous reports of TC II level differences between serum and plasma. EDTA is therefore a preferable anticoagulant for vitamin B12-binding protein studies, although it too may not be ideal.
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PMID:Vitamin B12-binding proteins in serum and plasma in various disorders. Effect of anticoagulants. 41 9

Determination of the percentage of cells in clumps on a stained smear of human peripheral blood porvided a useful, accurate technique for measuring cell adhesiveness. Smears of human peripheral blood drawn with EDTA were prepared on a blood slide centrifuge, stained, and examined under a light microscope. Statistical analysis showed that the method resulted in a Poisson distribution of particles on the slide, where a particle was considered to be a simple cell, or two or more cells which appeared to be touching, Analysis of the distributions of erythrocytes and leukocytes showed that clumps were formed before the cells were deposited on the slide. When adhesiveness of erythrocytes or leukocytes was increased by incubation with antiserum to the corresponding cell type, the percentage of that cell type in clumps increased proportionately, Preliminary results using the method showed that normal human donors had similar to 1% of their erythrocytes and 1-5% of their leukocytes in clumps. In chronic myelocytic leukemia, as many as 60% of the leukocytes were in clumps.
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PMID:A measurement technique for cell adhesiveness. 80 13

A solid-phase radioimmunoassay is described for measuring lactoferrin levels in normal human plasma. The sensitivity of the assay was 6 ng. per milliliter with an intraassay coefficient of variation of 4 per cent and an interassay value of 9 per cent. Healthy adult males had a mean plasma level of 1.62 mug per milliliter which was significantly higher than adult females, 1.07 mug per milliliter. Postmenopausal females had levels similar to men, 1.74 mug per milliliter, while younger women had a significantly lower mean value, 0.75 mug per milliliter. Two menstruating women and 2 pregnant women had moderately elevated levels. Consistently elevated levels were found in patients with untreated or relapsing chronic myeloid leukemia--all over 12.0 mug per milliliter, while patients on marrow suppressant therapy tended to have subnormal levels. The collection of serum specimens as opposed to plasma, resulted in inconsistently elevated levels: EDTA was the anticoagulant of choice, as heparin interfered in the radioimmunoassay system.
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PMID:A solid-phase radioimmunoassay for the measurement of lactoferrin in human plasma: variations with age, sex, and disease. 106 75

A retrospective analysis of evidence of platelet clumping, an in vitro phenomenon in blood samples anticoagulated by EDTA, was performed in 49 patients with myeloproliferative diseases other than chronic myeloid leukaemia. Evidence of platelet clumping was provided by the H6000 picture, which in the presence of platelet aggregates yields a characteristic "whisk" in a defined region. Out of the 49 patients, 17 (35%) had evidence of platelet clumping which, however, occurred in an unpredictable manner from time to time. Platelet clumping thus provides a confounding factor when automated platelet counts are used to monitor effects of cytotoxic treatment in this type of disorders. In a prospective study, it was shown that the problem can be overcome by optimizing the hospital routine to secure minimum delay between sampling and analysis.
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PMID:Platelet clumping in Ph-negative myeloproliferative syndromes. 342 99

A solid-phase, one-step radioimmunoassay was developed for the determination of plasma lactoferrin concentration. The detection limit of the assay is 150 micrograms/l. Leakage of cellular lactoferrin was minimal when EDTA was used as anticoagulant, while results obtained from serum and from heparinized plasma were not reproducible. The plasma lactoferrin concentration of 35 female and 44 male healthy adults was measured in order to determine normal values. The geometric mean of lactoferrin levels in men is about 10% higher than in women: 483 (200-1500) micrograms/l in men and 446 (200-870) micrograms/l in women. Patients with acute and chronic leukaemias were also studied. In 38 patients with chronic myeloid leukaemia plasma lactoferrin levels were increased by three times while the neutrophil count was ten times higher than normal. Normal lactoferrin concentrations were measured in plasma samples from 15 patients with chronic lymphocytic leukaemia in incomplete remission while no detectable lactoferrin was found in samples from those in relapse (10 patients). In the untreated patients or those in relapse (19 cases) of both acute lymphocytic and myeloid leukaemias, plasma lactoferrin concentrations were undetectable while they seemed to return to normal during remission (3 cases). The data obtained indicate that the determination of plasma lactoferrin concentration might play an important role in facilitating the assessment of total blood granulocyte pool (TBGP).
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PMID:Plasma lactoferrin levels in leukaemias. 347 35

A folate binding protein purified from the cytoplasm of human chronic myelogenous leukemia cells and saturated with [3H]pteroylglutamic acid, and the same protein labeled with 125I and saturated with pteroylglutamic acid, binds to the nuclear fraction of rat liver. EDTA inhibits this binding and this inhibition is reversed by Ca2+ but not by Mg2+. The nuclear fraction binds very little free [3H]pteroylglutamic acid, and the cytoplasm from which the nuclei have been removed does not bind the protein-folate complex. A Kd of 0.7 nM and a value of 1000 unsaturated binding sites per nucleus were obtained by Scatchard analysis. The translocation of folate to the nuclear membrane or nucleus by this soluble cytoplasmic folate binder may be the mechanism for the induction of enzyme(s) required for the metabolism of the folate ligand attached to the protein.
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PMID:Rat liver nuclei contain receptors for a folate binding protein. 632 Feb 2

Platelet satellitism to basophil granulocytes was observed in a patient with chronic myelocytic leukaemia. This phenomenon occurred with peripheral basophil cells obtained from venous blood anticoagulated with EDTA. Previous reports have demonstrated platelet satellitism to polymorphonuclear neutrophils and monocytes but not to other types of white blood cells. The cause of the platelet satellitism in this CML case remains unclear. It is suggested that this rare phenomenon should be considered in evaluating the platelet number in CML.
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PMID:Platelet satellitism to basophils in a patient with chronic myelocytic leukaemia. 695 40

The molecular weights of EDTA-mercaptoethanol-soluble Fc gamma-affined proteins isolated from chronic lymphocytic leukemia of the B type, prolymphocytic leukemia of the B type, chronic myeloid leukemia and hairy-cell leukemia were compared. SDS polyacrylamide gel electrophoresis of the Fc gamma-binding material obtained from all six cases of B type leukemia revealed a single peak with an apparent molecular weight of 28,000. The Fc gamma-affined material isolated from the cells of two cases of chronic myeloid leukemia showed two peaks, one with an apparent molecular weight of 42,600 and one with an apparent molecular weight of 18,800. The Fc gamma-affined material isolated from the cells of two cases of hairy-cell leukemia electrophoresed in the form of a closely spaced double peak. One component of the double peak had an apparent molecular weight of 28,000 and thus corresponds to the Fc gamma-binding material of leukemic B cells. The second component had a slightly lower molecular weight. The latter component is not present on either leukemic B cells or myeloid cells. The results indicate that the EDTA-mercaptoethanol-soluble Fc gamma-affined proteins of different types of cells differ in molecular weight, and thus in molecular structure.
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PMID:Molecular weight analysis of Fc gamma-binding proteins of lymphoid leukemia, myeloid leukemia, and hairy-cell leukemia. 697 74

We report a highly sensitive time-resolved immunofluorometric method for quantification of polymerase chain reaction (PCR)-amplified mRNA sequences. The PCR primers are labeled at their 5' ends, one with biotin and the other with a hapten. The modified primers are incorporated, during PCR, in the amplified product. The PCR product is captured, through its biotin moiety, to a streptavidin-coated solid phase and subsequently is detected with an alkaline phosphatase-labeled antibody. The phosphate ester of fluorosalicylic acid is used as a substrate. The fluorosalicylate produced forms a highly fluorescent ternary complex with Tb(3+)-EDTA, which is measured by time-resolved fluorometry. We chose the determination of PCR-amplified chronic myelogenous leukemia-specific mRNA as a model system. mRNA molecules corresponding to 0.1 leukemic cell in the presence of 0.5 million normal cells may be detected (signal-to-background ratio of 1.5). The method provides a sensitive and rapid nonisotopic alternative to Southern blot and hybridization with radioactive probes.
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PMID:Time-resolved immunofluorometric determination of specific mRNA sequences amplified by the polymerase chain reaction. 784 30


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