Glucose-6- Phosphate Dehydrogenase Activity in Newborn in Jos: A Necessary Evaluation for Icteric Neonates

Ed Jatau,Ob Toma,Tv Ma'An,Z Ayuba,Jo Ewuga,Oj Egesie,Do Damulak

doi:10.46912/jbrcp.v2i42019.127

Abstract

Red blood cell glucose-6-phosphate dehydrogenase (G6PD) is a key regulatory enzyme with the major role of meeting the cellular need for reductive biosynthesis and maintenance of redox status. G6PD deficiency is a common inherited enzyme defect associated with severe neonatal hyperbilirubinaemia that can result in permanent neurologic damage or death. This study was aimed at estimating the level of G6PD activity among icteric neonates to assess its usefulness in the evaluation of icteric neonates in Jos. One hundred and fifty icteric neonates (92 males and 58 females) whose parents consented were consecutively enrolled as they presented at the Special Care Baby Units (SCBU) of the Jos University Teaching Hospital (JUTH), Bingham University Teaching Hospital (BhUTH), and the Plateau State Specialist Hospital (PSSH), Jos. These subjects had their G6PD activity levels assayed using the Pointe Quantitative Diagnostic Kit (USA) while other relevant clinical information was obtained using a questionnaire. G6PD activity of the icteric neonates ranged between 0.54 and 24.18 IU/gHb with a mean of 8.02 ± 4.87 IU/gHb. Sixty-one (40.7 %), comprising 45 males and 16 female neonates were G6PD deficient with mean G6PD activity of 3.79 ± 1.37 IU/gHb while eighty-nine (59.3%) were G6PD normal with a mean G6PD activity of 10.92 ± 4.24 IU/gHb. G6PD activity in icteric neonates in Jos varies widely with a relatively high proportion of these neonates being G6PD deficient. Determination of G6PD activity in icteric neonates should therefore form an important evaluation tool for identification and intervention in those with the deficiency.

Highlights

Glucose-6-phosphate dehydrogenase (G6PD) is a cytoplasmic enzyme distributed in all cells and catalyses glucose-6-phosphate oxidation to 6phosphogluconolactone, converting the co-enzyme nicotinamide adenine dinucleotide phosphate (NADP) to its reduced form (NADPH)
This is corroborated by the report that in African populations, three different G6PD genotypes are recognised in males (GdA+, GdB and GdA−) whilst in females six genotypes are recognised (GdB/GdB, GdA+/GdB, GdA+/GdA+, GdB/GdA−, GdA−/GdA− and GdA+/GdA−).13Ademowo et al in a study in Nigeria, demonstrated that each of these genotypes expresses varying levels of enzyme activity ranging from 9.5 ± 3.7 IU/gHb in GdB in males to 1.7 ± 1.1 IU/gHb in GdA−/GdA− genotype in females.[13]
The proportion of icteric neonates with G6PD deficiency in this study is similar to the finding in Zaria, North West and Ilorin, North Central Nigeria where Ahmed et al, and Amiwero et al reported a prevalence of 40 % and 43 % respectively.[14,15]

Summary

Introduction

Glucose-6-phosphate dehydrogenase (G6PD) is a cytoplasmic enzyme distributed in all cells and catalyses glucose-6-phosphate oxidation to 6phosphogluconolactone, converting the co-enzyme nicotinamide adenine dinucleotide phosphate (NADP) to its reduced form (NADPH).

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Conclusion