Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.

ABSTRACT: The mechanism underlying asthenozoospermia in male infertility has been a prominent topic in reproductive medicine research. Human sperm function is modified by various protein post-translational modifications (PTMs). Among these, lactylation modification, a relatively novel PTM, has not been previously reported in the context of the male reproductive system. Comparative analyses between asthenozoospermic and normal sperm have revealed a significant down-regulation in the level of lysine lactylation (Kla) in proteins from asthenozoospermic sperm. Based on proteomic studies of protein Kla, 220 lactylated proteins were identified in sperm. Bioinformatics results showed that these lactylated proteins were highly enriched in the glycolytic pathway. Phosphoglycerate kinase 2 (PGK2), a key glyco

SUBMITTER: Yan M 

PROVIDER: S-EPMC12702358 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature