ArticleScientific reports2025
Homeostatic response of phospholipid pathways to PCYT2 deficiency and impaired de Novo synthesis of phosphatidylethanolamine.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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10 authors.
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Abstract
PCYT2 is the key regulatory enzyme in the biosynthesis of phosphatidylethanolamine (PE) via the CDP-ethanolamine Kennedy pathway. Deficiencies in this gene have been linked to metabolic, neurological, and cardiac disorders; however, most studies report that PE levels remain unchanged. This study aimed to identify the metabolic mechanisms that preserve PE levels when its synthesis is impaired in PCYT2-knockdown human fibroblasts. We investigated alternative pathways that could compensate for reduced PE synthesis, including phosphatidylcholine (PC) and PE base-exchange to phosphatidylserine (PS), followed by PE resynthesis via PS decarboxylation. These pathways were individually assessed using [14 C]-ethanolamine, [3 H]-choline, and [3 H]-serine, and correlated with the expression and activity of the base-exchange genes PTSS1, PTSS2, and the PS decarboxylase PISD. The base-exchange activity was not significantly altered and mitochondrial PS decarboxylation was inhibited, indicating that these routes do not compensate for reduced PE synthesis in PCYT2-deficient cells. Chronic choline treatment increased ethanolamine and choline transport and upregulated the choline/ethanolamine transporter CTL1, yet PC synthesis and base-exchange activity remained unchanged, demonstrating that choline supplementation does not affect PE sythesis. Instead, PE homeostasis was maintained through reduced degradation and extensive phospholipid remodeling via the Lands' cycle, as evidenced by broad changes in fatty acid composition and increased phospholipid unsaturation. Remodeling extended beyond PC, PE, and PS to include phosphatidylinositol and sphingomyelin. These metabolic adaptations led to elevated reactive oxygen species production and enhanced mitochondrial fusion without significantly affecting autophagy or cell viability. Our findings suggest that in the absence of PCYT2 activity, PE levels are preserved primarily through reduced degradation and remodeling, rather than through alternative biosynthetic pathways.
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