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)

The activity and properties of acid alpha-mannosidase were studied in normal granulocytes and in two types of myeloid cells from patients with chronic myeloid leukemia. The activity of the enzyme in leukemic cells was 2-fold higher than that in normal granulocytes and in morphologically matured myeloid cells. Two latter types of cells did not differ in alpha-mannosidase activity. Kinetic properties, thermo- and pH stability of alpha-mannosidase from normal and leukemic cells were similar. alpha-mannosidase in leukemic and normal cells existed in two forms (A and B), which were easily separated on DEAE-cellulose column. These two forms differed in molecular mass (300 and 290 kD, respectively) and in the degree of sialylation. The quantitative ratios of A and B forms in normal and leukemic cells were different. In normal granulocytes and in mature cells from patients this ratio was 0.60 and 0.67, respectively. In leukemic cells the ratio was found to be 1.31. Thus, in leukemic cells form A of alpha-mannosidase predominanted, whereas in normal cells the predominance of form B was observed. It was suggested therefore that in leukemic cells the enhanced synthesis of alpha-mannosidase occurred in parallel with the accumulation of the B form. This accumulation was assumed as the cause of enhanced activity of the enzyme in immature leukemic cells.
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PMID:[Acid alpha-D-mannosidase of human leukocytes in the norm and during chronic myeloid leukemia]. 316 90

Mixed leukocyte suspensions were prepared from heparinized blood collected from healthy subjects and from patients with chronic myeloid leukemia (CML). In all the suspensions determinations were made for: zinc, by atomic absorption; granulocyte alkaline phosphatase (GAP), using the method with p-nitrophenylphosphatase; granulocyte LDH, by means of the enzymatic autoanalyser LKD 8,600. In the patients with CML, the values of zinc and of granulocyte alkaline phosphatase activity were very low while the granulocyte LDH values were higher than normal. The chromatogram of the granulocyte LDH isoenzymes on DEAE-Sephadex A50 minicolumn (0.5 X 12 cm) showed an "alpha type abnormality" revealed by the increased activity of the isoenzymes with high electrophoretic mobility LDH2 and LDH1 specific for tissues with intense oxidative phosphorylation. In the normal subjects the chromatogram of the leukocyte LDH isoenzymes showed a type M (skeletal muscle) prevalence denoting intense anaerobic glycolysis. Therefore the low zinc concentrations (0.55 micrograms mg N2 as compared with the normal 1.24 micrograms mg N2) in these patients cause the decrease of GAP activity by the lack of zinc in the active center of the enzyme and the decrease of cellular permeability thus allowing the extracellular release of granulocyte LDH.
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PMID:Study of the relationship between the granulocyte LDH, alkaline phosphatase and Zn at the level of the leukocyte in patients with chronic myeloid leukemia. 346 14

Serum from a patient with chronic myelogenous leukemia was subjected to anion-exchange chromatography on DEAE-Sepharose CL-6B. High-affinity binding of [3H]folate to front effluent, eluted at a low salt gradient, was studied in equilibrium-dialysis experiments (37 degrees C, pH 7.4). As suggested by the data, folate binding displayed positive cooperativity. Dilution of the binder solution resulted in a shift to a simple non-cooperative binding type and increased binding affinity. Furthermore, binding was inhibited at pH 5.0 and at low temperature (7 degrees C). This study demonstrates important similarities between high-affinity folate binding in milk and serum: positive cooperativity and dependence of binding affinity on concentration of binder. Identical mechanisms may underly these phenomena in milk and serum. The apparent relationship between binding type and concentration of binder shown herein seems to agree fairly well with recent observations on sera from groups of healthy persons.
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PMID:High-affinity binding of folate to a serum protein in chronic myelogenous leukemia: effect of binder concentration, pH, and temperature. 693 95

Although vitamin B12 is an essential coenzyme for DNA synthesis, humans, like other mammals, are incapable of synthesizing it. The role of intrinsic factor (IF) in B12 absorption is widely known, but, in fact there exists a much more intricate and complex mechanism for the effective assimilation of this important trace element in humans. B12 binding proteins play important roles in all stages of vitamin B12 metabolism. They are involved not only in its absorption, but also in its transport in serum, uptake to cells, storage in organs, enterohepatic circulation, and elimination of its analogues. Besides IF, well-known as a vitamin B12 binding protein found in gastric juice, there are other kinds of binding proteins found in human serum which are composed to transcobalamin (TC) I, II and III. Elevation of the vitamin B12 level in chronic myelogenous leukemia was first reported in the 1950s. Since then, B12 elevation has been found to occur in other kinds of chronic myeloproliferative disorders (CMPDs) as well and to be caused by an increase of serum TC. In CMPDs, either TCI or TCIII increases, but, the degree of elevation and the type of TC involved differs for each disorder. This article describes the changes in TC of CMPD patients. With the induction of the developed radioimmunoassay for R-type B12 binding protein, many cases have been examined. In addition, detailed qualitative analysis using DEAE cellulose column chromatography has been included for conditions not previously reported.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Vitamin B12 and transcobalamin in chronic myeloproliferative disorders]. 829 40

A novel mannose-binding lectin (designated CML) was isolated from Clematis montana Buch.-Ham stem (Ranunculaceae) using ion exchange and gel filtration chromatographies on DEAE-Sepharose and Sephacryl S-100. The purified C. montana lectin was a homodimer of 11,968.9 Da subunits as determined by gel filtration and MS. The hemagglutinating activity of CML was inhibited by branched oligomannosides. The N-terminal 15-amino acid sequence of CML, DNVKYSGQVKNTGSA, has not been reported for other lectins. Also, the peptide mass fingerprinting assay confirmed that there is no match result of similar plant lectins for CML, indicating CML may be a novel plant lectin. CML showed marked antiviral activity against various viruses in cell culture. Subsequently, CML was also found to exhibit remarkable inhibitory effect on L929, HeLa, MCF7 and HepG2 cells. Furthermore, CML specially induced L929 cell apoptosis in dose-dependent manner as evidenced by MTT, fluorescent microscopy, LDH activity-based cytotoxicity assays and DNA ladder. Moreover, due to both caspase inhibitors and Western blot analyses, caspase was also found to play the important role in the potential apoptotic mechanism of CML. When the carbohydrate-binding site was fully inhibited by sugars, cytotoxicity was abruptly decreased and apoptotic phenomenon in L929 cells was not observed, suggesting a significant correlation between mannose-binding-specific activity and the antineoplastic mechanism.
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PMID:Clematis montana lectin, a novel mannose-binding lectin from traditional Chinese medicine with antiviral and apoptosis-inducing activities. 1957 2


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