{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kawaguchi R"],"funding":["Japan Science and Technology Agency","Japan Society for the Promotion of Science"],"pagination":["BSR20253768"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12905485"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["46(1)"],"pubmed_abstract":["Hyperhomocysteinemia is a risk factor of cardiovascular disease (CVD). High-density lipoprotein (HDL) plays an important role in anti-atherosclerosis, with its anti-atherogenic function attributed to HDL-associated proteins such as apolipoprotein A-I (apoA-I) and paraoxonase 1 (PON1). Homocysteine (Hcy) thiolactone modifies lysine residues in proteins, thereby altering their function. Although dysfunction of apoA-I and PON1 has been reported, the precise modification sites and underlying mechanisms have remained unclear. In this study, we aimed to identify Hcy-thiolactone modification sites on apoA-I and PON1. In addition, we sought to clarify the effects of Hcy-thiolactone on PON1 activity and its distribution. Modification sites were analyzed using MALDI-TOF MS. The effects of Hcy-thiola"],"journal":["Bioscience reports"],"pubmed_title":["Homocysteine thiolactone affects paraoxonase 1 activity via altered paraoxonase 1 distribution on high-density lipoprotein particles."],"pmcid":["PMC12905485"],"funding_grant_id":["22K07466, 25K10657","JPMJSP2120"],"pubmed_authors":["Kugii Y","Ohkawa R","Hosoya S","Suzuki N","Kawaguchi R","Sasaki T","Miyakoshi T","Yoshimoto A"],"additional_accession":[]},"is_claimable":false,"name":"Homocysteine thiolactone affects paraoxonase 1 activity via altered paraoxonase 1 distribution on high-density lipoprotein particles.","description":"Hyperhomocysteinemia is a risk factor of cardiovascular disease (CVD). High-density lipoprotein (HDL) plays an important role in anti-atherosclerosis, with its anti-atherogenic function attributed to HDL-associated proteins such as apolipoprotein A-I (apoA-I) and paraoxonase 1 (PON1). Homocysteine (Hcy) thiolactone modifies lysine residues in proteins, thereby altering their function. Although dysfunction of apoA-I and PON1 has been reported, the precise modification sites and underlying mechanisms have remained unclear. In this study, we aimed to identify Hcy-thiolactone modification sites on apoA-I and PON1. In addition, we sought to clarify the effects of Hcy-thiolactone on PON1 activity and its distribution. Modification sites were analyzed using MALDI-TOF MS. The effects of Hcy-thiola","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-07-15T16:28:58.944Z","creation":"2026-07-07T03:08:11.901Z"},"accession":"S-EPMC12905485","cross_references":{"pubmed":["41496561"],"doi":["10.1042/BSR20253768"]}}