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Reduced thiamine binding is a novel mechanism for TPK deficiency disorder.

Wenjie HuangJiao QinDingdong LiuYan WangXiaofei ShenNa YangHui ZhouXiao-Tang CaiZhi-Ling WangDan YuRong LuoQingxiang SunYong-Mei XieDa Jia
Published in: Molecular genetics and genomics : MGG (2018)
Thiamine pyrophosphokinase (TPK) converts thiamine (vitamin B1) into thiamine pyrophosphate (TPP), an essential cofactor for many important enzymes. TPK1 mutations lead to a rare disorder: episodic encephalopathy type thiamine metabolism dysfunction. Yet, the molecular mechanism of the disease is not entirely clear. Here we report an individual case of episodic encephalopathy, with familial history carrying a novel homozygous TPK1 mutation (p.L28S). The L28S mutation leads to reduced enzymatic activity, both in vitro and in vivo, without impairing thiamine binding and protein stability. Thiamine supplementation averted encephalopathic episodes and restored the patient's developmental progression. Biochemical characterization of reported TPK1 missense mutations suggested reduced thiamine binding as a new disease mechanism. Importantly, many disease mutants are directly or indirectly involved in thiamine binding. Thus, our study provided a novel rationale for thiamine supplementation, so far the major therapeutic intervention in TPK deficiency.
Keyphrases
  • early onset
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