Wanders Ronald J A, Groothoff Jaap W, Deesker Lisa J, Salido Eduardo, Garrelfs Sander F
Department of Pediatric Nephrology, Emma Children's Hospital, Amsterdam, The Netherlands.
Department of Laboratory Medicine, Laboratory Genetic Metabolic Diseases, Amsterdam UMC, Amsterdam, The Netherlands.
J Inherit Metab Dis. 2025 Jan;48(1):e12817. doi: 10.1002/jimd.12817. Epub 2024 Nov 24.
Glyoxylate is a toxic metabolite because of its rapid conversion into oxalate, as catalyzed by the ubiquitous enzyme lactate dehydrogenase. This requires the presence of efficient glyoxylate detoxification systems in multiple subcellular compartments, as glyoxylate is produced in peroxisomes, mitochondria, and the cytosol. Alanine glyoxylate aminotransferase (AGT) and glyoxylate reductase/hydroxypyruvate reductase (GRHPR) are the key enzymes involved in glyoxylate detoxification. Bi-allelic mutations in the genes coding for these enzymes cause primary hyperoxaluria type 1 (PH1) and 2 (PH2), respectively. Glyoxylate is derived from various sources, including 4-hydroxyproline, which is degraded in mitochondria, generating pyruvate and glyoxylate, as catalyzed by the mitochondrial enzyme 4-hydroxy-2-oxoglutarate aldolase (HOGA); however, counterintuitively, a defect in HOGA1 is the molecular basis of primary hyperoxaluria type 3 (PH3). Irrespective of its underlying cause, hyperoxaluria in humans leads to nephrocalcinosis, recurrent urolithiasis, and kidney damage, which may culminate in kidney failure requiring combined liver-kidney transplantation in severely affected patients. In the past few years, therapeutic options, especially for primary hyperoxaluria type 1 (PH1), have greatly been improved thanks to the introduction of two RNAi-based therapies that inhibit either the production of glycolate oxidase (lumasiran) or lactate dehydrogenase (nedosiran). While lumasiran only targets PH1 patients, nedosiran was specifically developed to target all three subtypes of PH. Inspired by the findings reported in the literature that nedosiran effectively reduced urinary oxalate excretion in PH1 patients but not in PH2 or PH3 patients, we have now revisited glyoxylate metabolism in humans and performed a thorough literature study which revealed that glyoxylate/oxalate metabolism is not confined to the liver but instead involves multiple different organs. This new view on glyoxylate/oxalate metabolism in humans may well explain the disappointing results of nedosiran in PH2 and PH3, and provides new clues for the future generation of new therapeutic strategies for PH2 and PH3.
乙醛酸是一种有毒代谢物,因为它能在普遍存在的乳酸脱氢酶催化下迅速转化为草酸盐。这就需要在多个亚细胞区室中存在有效的乙醛酸解毒系统,因为乙醛酸在过氧化物酶体、线粒体和细胞质中产生。丙氨酸乙醛酸氨基转移酶(AGT)和乙醛酸还原酶/羟基丙酮酸还原酶(GRHPR)是参与乙醛酸解毒的关键酶。编码这些酶的基因发生双等位基因突变分别导致1型原发性高草酸尿症(PH1)和2型原发性高草酸尿症(PH2)。乙醛酸有多种来源,包括4-羟基脯氨酸,它在线粒体中被降解,在线粒体酶4-羟基-2-氧代戊二酸醛缩酶(HOGA)的催化下生成丙酮酸和乙醛酸;然而,与直觉相反的是,HOGA1缺陷是3型原发性高草酸尿症(PH3)的分子基础。无论其潜在原因如何,人类高草酸尿症都会导致肾钙质沉着、复发性尿路结石和肾损伤,在严重受影响的患者中,最终可能导致肾衰竭,需要进行肝肾联合移植。在过去几年中,由于引入了两种基于RNAi的疗法,即抑制乙醇酸氧化酶(鲁马西冉)或乳酸脱氢酶(奈多西冉)的产生,治疗选择,尤其是针对1型原发性高草酸尿症(PH1)的治疗选择有了很大改善。虽然鲁马西冉仅针对PH1患者,但奈多西冉是专门为针对所有三种PH亚型而开发的。受文献报道的奈多西冉能有效降低PH1患者尿草酸排泄但对PH2或PH3患者无效这一发现的启发,我们现在重新审视了人类乙醛酸代谢,并进行了全面的文献研究,结果表明乙醛酸/草酸盐代谢不仅限于肝脏,而是涉及多个不同器官。这种关于人类乙醛酸/草酸盐代谢的新观点很可能解释了奈多西冉在PH2和PH3中令人失望的结果,并为未来开发针对PH2和PH3的新治疗策略提供了新线索。