Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.4.4 (adenosine deaminase)
 5,136 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A fusion between a selectable multidrug resistance (MDR1) cDNA and an adenosine deaminase (ADA) cDNA concomitantly confers multidrug resistance and ADA activity on transfected cells. We have produced a Harvey murine sarcoma virus-derived, replication-defective, recombinant retrovirus to transduce this chimeric MDR-ADA gene efficiently into a great variety of cells. Infection with the MDR-ADA retrovirus conferred the multidrug resistance phenotype on drug-sensitive cells, therefore allowing selection in the presence of colchicine. Colchicine-resistant cells synthesized large amounts of a membrane-associated 210-kDa MDR-ADA fusion protein that preserved both MDR and ADA functional activities. To monitor expression of the chimeric gene in vivo, Kirsten virus-transformed NIH cells were infected with the MDR-ADA retrovirus, and after drug-selection, injected into athymic nude mice. Tumors developed that contained the bifunctionally active MDR-ADA fusion protein. When these mouse tumor cells were placed in tissue culture without the selecting drug, they did not lose the bifunctionally active MDR-ADA fusion protein. The replication-defective, recombinant MDR-ADA retrovirus should be useful to stably introduce the chimeric MDR-ADA gene into a variety of cell types for biological experiments in vitro and in vivo.
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PMID:Retroviral transfer of a chimeric multidrug resistance-adenosine deaminase gene. 196 8

Colchicine and its less toxic derivatives (demecolcine and deacetyl colchicine), in dependence on the concentration in the incubation medium, inhibited the activity of adenosine deaminase in the lymphocytes. All the three substances increased the level of cyclic adenosine monophosphate which has the ability of influencing the proliferation of T-lymphocytes. Colchicine and its derivates also inhibited the activity of purine nucleooxidophosphorylase, which, similarly as adenosine deaminase, is a marker enzyme of T-lymphocytes. The results obtained lead to the assumption that the mentioned preparations inhibit the function of T-lymphocytes.
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PMID:[The effect of colchicine and its derivatives on the activity of enzyme markers of T-lymphocytes]. 255 78

Colchicine is taken up by isolated cerebral tissues incubated in glucose-salt solutions and is maintained in the tissues when they are superfused with colchicine-free solutions. Most of the colchicine in such tissues remains uncombined after an hour's incubation; up to 20% is combined with tubulin of cytosolic and particulate fractions. Adenosine, and conditions of stimulation or depolarization which release adenosine, diminish the uptake of colchicine and less appears in combined forms. Uptake is diminished also by 2-chloroadenosine and by cyclic AMP; is increased by theophylline and by adenosine deaminase but unaffected by dipyridamole. Adenylate cyclase complexes, with their known tubulin association, are suggested as involved in a route of colchicine-entry and so could give a means whereby environmental changes modify colchicine toxicity, and colchicine-attachment to cerebral preparations.
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PMID:Adenosine modifies colchicine-uptake into tissues from the mammalian brain. 2050 Oct 76