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PORPHOBILINOGEN DEAMINASE AND ADENOSINE DEAMINASE ACTIVITY AS A POSSIBLE DIAGNOSTIC AID IN LYMPHATIC LEUKEMIAS.

ABSTRACT: It has been demonstrated recently that in addition to morphologic and immunologic methods, enzyme characterisation of lymphoid cells is useful in the study and classification of lympho proliferative disorders. Heme biosynthetic pathway and purine metabolism are reported to be disturbed in such patients, this study was an attempt to estimate two enzymes Adenosine Deaminase (ADA) and Porphobilinogen Deaminase (PBGD) and correlate them with cytological and morphological parameters in lymphatic leukemias. Fasting heparinized venous blood samples were collected from 40 patients and 20 controls. Porphobilinogen Deaminase (PBGD) and Adenosine Deaminase (ADA) assays were carried out in peripheral mononuclear cells. Both enzyme activities were significantly elevated in ALL. In CLL, while PBGD activity was elevated, ADA remained in normal limits. Our study indicates that PBGD and ADA Assays will be useful adjuncts to cytomorphological studies in differentiating ALL from CLL.

SUBMITTER: Sontakke AN

PROVIDER: S-EPMC5531728 | biostudies-other | 1999 Jan

REPOSITORIES: biostudies-other

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Project description:BACKGROUND:Human adenosine deaminase 2 (ADA2) is an extracellular enzyme that negatively regulates adenosine-mediated cell signaling by converting adenosine to inosine. Altered ADA2 enzyme activity has been associated with some viral infections and rheumatic diseases. The potential utility of ADA2 as a biomarker is, however, limited by the absence of established ranges of ADA2 concentration and enzyme activity in the healthy population. It is known that ADA2 enzyme activity is lower in adults, but when (and why) this decline happens is not known. The purpose of this study was to establish normative ranges of ADA2 enzyme activity and protein concentration in the healthy pediatric population. METHODS:We modified a commercially available ADA2 enzyme activity assay to enable higher throughput analysis of fresh, frozen and hemolyzed blood samples. With this assay and ADA2 protein immunoblotting, we analyzed ADA2 enzyme activity and protein concentration in blood plasma from a cohort of children and adolescents (n?=?94) aged 5?months to 18?years. One-way ANOVA with subsequent Tukey multiple comparison test was used to analyze group differences. Reference intervals were generated using the central 95% of the population (2-97.5 percentiles). RESULTS:ADA2 enzyme activity was consistent in fresh, frozen, and hemolyzed sera and plasma as measured by our modified assay. Analysis of plasma samples from the healthy pediatric cohort revealed that ADA2 enzyme activity is significantly lower in older children than in younger children (p?<?0.0001). In contrast, there was no significant correlation between ADA2 protein concentration and either age or ADA2 enzyme activity. CONCLUSION:We observed that ADA2 enzyme activity, but not ADA2 protein concentration, negatively correlates with age in a cohort of children and adolescents. Our findings stress the importance of appropriate age-matched controls for assessing ADA2 enzyme activity in the clinical setting.

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PORPHOBILINOGEN DEAMINASE AND ADENOSINE DEAMINASE ACTIVITY AS A POSSIBLE DIAGNOSTIC AID IN LYMPHATIC LEUKEMIAS.

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