Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023418 (leukemia)
 93,477 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The gene for the receptor for ecotropic murine leukemia virus (Rev) has been assigned to mouse chromosome 5. This determination was made possible by an analysis of somatic cell hybrids between mouse and Chinese hamster cells. The parents of these hybrids were A/HeJ or Mus poschiavinus peritoneal exudate cells or BALB/c primary embryo fibroblasts and E36, a Chinese hamster lung fibroblast deficient in hypoxanthine guanine phosphoribosyltransferase. Segregation of mouse chromosomes in these hybrids was analyzed by chromosome banding and isozyme expression. Cells were tested for their ability to absorb and replicate vesicular stomatitis virus (murine leukemia virus [MuLV]) pseudotype particles and ecotropic MuLV as measured by the XC test. The presence of chromosome 5 was essential for receptor expression as determined by three statistical procedures. Segregation of the receptor for ecotropic murine leukemia virus was also followed in two series of subclones. In both, receptor expression was syntenic with phosphoglucomutase-1, an isozyme which has been mapped to mouse chromosome 5.
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PMID:Assignment of the receptor for ecotropic murine leukemia virus to mouse chromosome 5. 21 1

By means of an approach that combined the techniques of somatic cell genetics and Mendelian breeding studies, the inducibility locus, designated Cv, for ecotropic murine leukemia virus in BALB/c mice, was mapped to chromosome 5, 23 units from the locus for phosphoglucomutase-1, with gene order Cv-Pgm-1-Gus. This low-efficiency inducibility locus is therefore not allelic with the chromosome 7 loci previously described for two other mouse strains with high virus inducibility. These studies provide further evidence that endogenous ecotropic viruses represent viral genomes inserted at different chromosomal sites in the various mouse strains.
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PMID:Genetic mapping of the ecotropic murine leukemia virus-inducing locus of BALB/c mouse to chromosome 5. 21 75

Five hybrids reactive with monoclonal antibodies against human leukocyte common antigen (T-200) and/or lymphocyte function-associated antigen 1 (LFA-1) beta subunit were obtained from the fusion of human blood lymphocytes or T-cell chronic lymphocytic leukemia cells with BW5147 mouse T-cell leukemia cells. Chromosome analyses of 20 clones showed concordance between the presence of human chromosomes 1 and 21 and the expression of T-200 and LFA-1 beta subunit, respectively. Confirmation of human chromosomes in the hybrids was made by the electrophoretic analyses of phosphoglucomutase for chromosome 1 and superoxide dismutase for chromosome 21. The results suggested that the presence of human chromosomes 1 and 21 was essential for the expression of T-200 and LFA-1 beta subunit, respectively.
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PMID:Chromosomal assignments of genes coding for human leukocyte common antigen, T-200, and lymphocyte function-associated antigen 1, LFA-1 beta subunit. 295 27

We report an effective follow-up of the establishment of bone-marrow function after an allogeneic bone-marrow transplantation in a patient with acute lymphoblastic leukemia, by means of a suitable genetic marker, phosphoglucomutase-1 (EC 5.4.2.2) isoenzyme. A patient with acute lymphoblastic leukemia received allogeneic bone-marrow graft from a sibling who was of the same sex and blood group, HLA-identical, and mixed-lymphocyte-culture nonreactive. To monitor the bone-marrow engraftment and the type and degree of chimerism established, we used a genetic marker, the phosphoglucomutase-1 isoenzyme system, to reveal the difference between the bone-marrow host and donor. We did phosphoglucomutase-1 isoenzyme subtyping of the host's and donor's erythrocytes before transplantation, and isoenzyme phenotyping of the host's erythrocytes during a year after transplantation. Establishment of bone-marrow graft function, a period of temporary mixed chimerism with a population of both host's and donor's erythrocytes, a period of the exclusive presence of donor's erythrocytes, and the resumed appearance of host's erythrocytes after eight months, with no signs of relapse of leukemia, were all observed by analysis of phenotypes. These isoenzymes served as a significant and practical genetic marker, which could be successfully used in studies on bone-marrow transplantation.
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PMID:Subtyping of erythrocyte phosphoglucomutase-1 as a genetic marker for bone-marrow engraftment and hematopoietic chimerism after allogeneic bone-marrow transplantation in a patient with acute lymphoblastic leukemia. 297 48

Synthesis of ferritin, a constitutive protein, is increased by iron. This protein is well recognized as a protein which detoxifies, stores and transports iron. The 24 subunits of ferritin assemble to form a protomer of Mr 480,000. This protein shell can sequester up to 4500 g atoms of iron as ferrichydroxyphosphate. Ferritin in vitro and in vivo binds other metal ions such as Cu, Zn, Cd, Pb, Be and Al. Next to Fe it binds large quantities of Be. Therefore, in vitro ferritin protects against and reverses the inhibition by Be of enzymes susceptible to this metal ion. Also, rats pretreated with Fe survive otherwise toxic levels of either pulmonary or intravenous exposure of Be. Liver ferritin from rats injected with Zn contains some of the injected metal ion. Incubation of such ferritin-zinc complex with zinc-requiring apoenzymes restores their activity. Fe(III) of ferritin is released only after its reduction to Fe(II) by a reductant. Incubation of phosphoglucomutase, a phosphoserine containing enzyme with ferritin and a reductant causes irreversible inactivation of the enzyme and removes 70% of its phosphate. Some other phosphoproteins are similarly inactivated but without the loss of the bound phosphate. Thus, uncontrolled release of iron from ferritin, in the presence of a reductant and oxygen can modify several biomolecules and can affect metabolic processes. A subclass of ferritin, acidic isoferritins, have been implicated in leukemia-associated inhibitory activity and has been suggested to inhibit production of Ia+ macrophage progenitors.
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PMID:Ferritin: an expanded role in metabolic regulation. 327 34