Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adenosine deaminase (EC 3.5.4.4, ADA) has been assayed in lymphocytes, granulocytes and erythrocytes from 45 patients with haematological malignancies. Activities were uniformly low in lymphocytes from patients with chronic lymphocytic leukaemia. Variable, but abnormal activities were frequently found in multiple myeloma, untreated lymphoma and leukaemic reticuloendotheliosis. High values were observed in lymphocytes from patients with lymphoma during intensive combination chemotherapy. ADA levels in lymphocytes were not correlated with levels in granulocytes or erythrocytes. ADA was elevated in blasts of patients with acute lymphocytic and myelogenous leukaemias but the ranges of activities per cell were so similar that ADA assay is unlikely to be of major help in distinguishing the two diseases.
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PMID:Adenosine deaminase activity in peripheral blood cells of patients with haematological malignancies. 106 90

Adenosine deaminase (ADA) has been assayed in plasma, erythrocytes, and lymphocytes from 29 patients with haematological and autoimmune diseases. ADA activity was uniformly low in erythrocytes and lymphocytes from patients with non-Hodgkin lymphoma and multiple myeloma (p less than 0.001). High levels of ADA activity was found in plasma, erythrocytes, and lymphocytes from patients with myeloid leukemia (p less than 0.001). ADA was high in plasma but low in erythrocytes and lymphocytes from patients with autoimmune diseases treated with immunosuppressive drugs (p less than 0.05). 4 adults with congenital immunodeficiency showed decreased ADA activity. In the control group of normal blood donors we found a 34-year-old female with low ADA activity in plasma, erythrocytes, and lymphocytes without any immunological abnormalities. This is the 3rd case of a healthy individual deficient for ADA. 1 patient with Osler's disease and high ADA activity in erythrocytes showed the importance of the purine salvage enzyme not only in lymphocytes.
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PMID:Adenosine deaminase activity in plasma and blood cells of patients with haematological and autoimmune diseases. 678 72

Adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4; ADA) activity is widely distributed in human tissues and is highest in lymphoid tissues. Two ADA isozymes are known as ADA1 and ADA2. Human tissue extracts contained ADA1 predominantly. Meanwhile, ADA2 was the main component of serum ADA. ADA activity was significantly elevated in the sera from patients with hepatic diseases, hematological malignancies and infectious diseases. Serum concentrations of ADA1 were high in patients with acute leukemias, chronic myeloid blast crisis leukemia and acute liver injury. Serum ADA2 levels were raised in patients with adult T-cell leukemia, multiple myeloma (B-J type), infectious mononucleosis, rubella, acquired immunodeficiency syndrome, chronic hepatic diseases and tuberculosis. It is supposed that ADA1 is derived mainly from injured tissues or cells while ADA2 comes from stimulated T-cells.
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PMID:[Adenosine deaminase]. 760 76

We have examined the cytotoxic effects of cyclic adenosine-3', 5'-monophosphate (cAMP) derivatives on multiple myeloma cells lines and determined that the 8-Chloro substituted derivative (8Cl-cAMP) is one of the most potent. We report here that 8Cl-cAMP is cytotoxic to both steroid sensitive and insensitive myeloma cells with a half maximal concentration of approximately 3 micromol/L. 8Cl-cAMP toxicity in myeloma cells is dependent on phosphodiesterase activity in the serum of cell culture medium. A metabolite of 8Cl-cAMP, 8-Chloro-adenosine (8Cl-AD), kills myeloma cells as effectively as 8Cl-cAMP. Adenosine deaminase (ADA) converts 8Cl-AD into 8Cl-inosine and abrogates the cytotoxic effects of 8Cl-cAMP, 8Cl-AMP, and 8Cl-AD, as does 5-(p-Nitrobenzyl)-6-Thio-Inosine (NBTI), an inhibitor of nucleoside uptake. These data suggest that 8Cl-cAMP must be converted to 8Cl-AD and that 8Cl-AD is the compound that enters the cell. Contrary to glucocorticoid-mediated cell death in myeloma cells, the pathway of 8Cl-AD-mediated cell death appears to be independent of interleukin-6 (IL-6) actions. Although the exact mode of action for this agent is currently unknown, its ability to kill steroid sensitive and insensitive multiple myeloma cells in an IL-6 independent fashion may offer exciting new therapeutic options.
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PMID:8Cl-cAMP cytotoxicity in both steroid sensitive and insensitive multiple myeloma cell lines is mediated by 8Cl-adenosine. 976 75