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General Medicine · Haematology: lead poisoning
Sample itemA 6-year-old child living near an informal battery-recycling unit has colicky abdominal pain, constipation, irritability and anaemia. The blood film shows coarse basophilic stippling of red cells, and blood lead is markedly raised. Which pair of haem synthesis enzymes is inhibited by lead?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
C. Delta-aminolevulinic acid dehydratase and ferrochelatase
Lead inhibits ALA dehydratase and ferrochelatase, so delta-aminolevulinic acid and free erythrocyte protoporphyrin accumulate and haem synthesis falls. It also inhibits pyrimidine 5'-nucleotidase, which causes basophilic stippling from retained ribosomal RNA. Lead lines on the gums, wrist drop and encephalopathy are other features, and chelation with succimer or calcium EDTA is used.
Option by option
A. Porphobilinogen deaminase and uroporphyrinogen III synthase
Porphobilinogen deaminase deficiency causes acute intermittent porphyria and uroporphyrinogen III synthase deficiency causes congenital erythropoietic porphyria.
B. Heme oxygenase and biliverdin reductase
Haem oxygenase and biliverdin reductase belong to haem degradation, not synthesis.
C. Delta-aminolevulinic acid dehydratase and ferrochelatase (correct)
Correct. Inhibition of these two enzymes explains raised ALA and protoporphyrin with anaemia.
D. Delta-aminolevulinic acid synthase and uroporphyrinogen decarboxylase
ALA synthase is the rate-limiting step and is regulated by haem; uroporphyrinogen decarboxylase is deficient in porphyria cutanea tarda.
Source note: Original NextPrep sample item — pending expert review. This item is original practice material awaiting independent expert review, so confirm important facts in a standard textbook.
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