Associations of Circulating ANGPTL3, C-Terminal Domain-Containing ANGPTL4, and ANGPTL3/8 and ANGPTL4/8 Complexes with LPL Activity, Diabetes, Inflammation, and Cardiovascular Mortality.

angiopoietin-like proteins cardiovascular mortality diabetes inflammation lipoprotein lipase

Journal

Circulation
ISSN: 1524-4539
Titre abrégé: Circulation
Pays: United States
ID NLM: 0147763

Informations de publication

Date de publication:
11 Oct 2024
Historique:
medline: 11 10 2024
pubmed: 11 10 2024
entrez: 11 10 2024
Statut: aheadofprint

Résumé

ANGPTL3/4/8 (angiopoietin-like proteins 3, 4, and 8) are important regulators of LPL (lipoprotein lipase). ANGPTL8 forms complexes with ANGPTL3 and ANGPTL4. ANGPTL4/8 complex formation converts ANGPTL4 from a furin substrate to a plasmin substrate, and both cleavages generate similar C-terminal domain-containing (CD)-ANGPTL4 fragments. Whereas several studies have investigated associations of free ANGPTL proteins with cardiovascular risk, there are no data describing associations of the complexes and CD-ANGPTL4 with outcomes or describing the effects of the complexes on LPL bound to GPIHBP1 (glycosylphosphatidylinositol HDL-binding protein 1). Recombinant protein assays were used to study ANGPTL protein and complex effects on GPIHBP1-LPL activity. ANGPTL3/8, ANGPTL3, ANGPTL4/8, and CD-ANGPTL4 were measured with dedicated immunoassays in 2394 LURIC (Ludwigshafen Risk and Cardiovascular Health) study participants undergoing coronary angiography and 6188 getABI study (German Epidemiological Trial on Ankle Brachial Index) participants undergoing ankle brachial index measurement. There was a follow-up for cardiovascular death with a median (interquartile range) duration of 9.80 (8.75-10.40) years in the LURIC study and 7.06 (7.00-7.14) years in the getABI study. ANGPTL3/8 potently inhibited GPIHBP1-LPL activity and showed positive associations with LDL-C (low-density lipoprotein cholesterol) and triglycerides (both ANGPTL3/8 potently inhibited GPIHBP1-LPL enzymatic activity, consistent with its positive association with serum lipids. However, ANGPTL3/8, LDL-C, and triglyceride levels were not associated with cardiovascular death in the LURIC and getABI cohorts. In contrast, concentrations of ANGPTL4/8 and particularly CD-ANGPTL4 were positively associated with inflammation, the prevalence of diabetes, and cardiovascular mortality.

Sections du résumé

BACKGROUND UNASSIGNED
ANGPTL3/4/8 (angiopoietin-like proteins 3, 4, and 8) are important regulators of LPL (lipoprotein lipase). ANGPTL8 forms complexes with ANGPTL3 and ANGPTL4. ANGPTL4/8 complex formation converts ANGPTL4 from a furin substrate to a plasmin substrate, and both cleavages generate similar C-terminal domain-containing (CD)-ANGPTL4 fragments. Whereas several studies have investigated associations of free ANGPTL proteins with cardiovascular risk, there are no data describing associations of the complexes and CD-ANGPTL4 with outcomes or describing the effects of the complexes on LPL bound to GPIHBP1 (glycosylphosphatidylinositol HDL-binding protein 1).
METHODS UNASSIGNED
Recombinant protein assays were used to study ANGPTL protein and complex effects on GPIHBP1-LPL activity. ANGPTL3/8, ANGPTL3, ANGPTL4/8, and CD-ANGPTL4 were measured with dedicated immunoassays in 2394 LURIC (Ludwigshafen Risk and Cardiovascular Health) study participants undergoing coronary angiography and 6188 getABI study (German Epidemiological Trial on Ankle Brachial Index) participants undergoing ankle brachial index measurement. There was a follow-up for cardiovascular death with a median (interquartile range) duration of 9.80 (8.75-10.40) years in the LURIC study and 7.06 (7.00-7.14) years in the getABI study.
RESULTS UNASSIGNED
ANGPTL3/8 potently inhibited GPIHBP1-LPL activity and showed positive associations with LDL-C (low-density lipoprotein cholesterol) and triglycerides (both
CONCLUSIONS UNASSIGNED
ANGPTL3/8 potently inhibited GPIHBP1-LPL enzymatic activity, consistent with its positive association with serum lipids. However, ANGPTL3/8, LDL-C, and triglyceride levels were not associated with cardiovascular death in the LURIC and getABI cohorts. In contrast, concentrations of ANGPTL4/8 and particularly CD-ANGPTL4 were positively associated with inflammation, the prevalence of diabetes, and cardiovascular mortality.

Identifiants

pubmed: 39392008
doi: 10.1161/CIRCULATIONAHA.124.069272
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Auteurs

Günther Silbernagel (G)

Division of Angiology, Department of Internal Medicine, Medical University of Graz, Austria. (G.S.).

Yan Q Chen (YQ)

Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN (Y.Q.C., H.L., D.L., Y.W., E.Y.Z., Y.Q., R.J.K.).

Hongxia Li (H)

Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN (Y.Q.C., H.L., D.L., Y.W., E.Y.Z., Y.Q., R.J.K.).

Deven Lemen (D)

Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN (Y.Q.C., H.L., D.L., Y.W., E.Y.Z., Y.Q., R.J.K.).

Yi Wen (Y)

Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN (Y.Q.C., H.L., D.L., Y.W., E.Y.Z., Y.Q., R.J.K.).

Eugene Y Zhen (EY)

Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN (Y.Q.C., H.L., D.L., Y.W., E.Y.Z., Y.Q., R.J.K.).

Martin Rief (M)

Anaesthesiology and Intensive Care Medicine, Medical University of Graz, Austria. (M.R.).

Marcus E Kleber (ME)

Vth Department of Medicine, Medical Faculty Mannheim, Heidelberg University, Mannheim, Germany (W.M., M.E.K.).
Synlab MVZ Humangenetik Mannheim, GmbH, Germany (M.E.K.).

Mark A Sarzynski (MA)

Department of Exercise Science, University of South Carolina, Columbia (M.A.S.).

Yue-Wei Qian (YW)

Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN (Y.Q.C., H.L., D.L., Y.W., E.Y.Z., Y.Q., R.J.K.).

Boerge Schmidt (B)

Institute for Medical Informatics, Biometry and Epidemiology, University Hospital Essen, University Duisburg-Essen, Germany (A.S., B.S.).

Ulrike Trampisch (U)

Department of Medical Informatics, Biometry and Epidemiology, Ruhr University, Bochum, Germany (U.T., H.J.T.).

Angela P Moissl (AP)

Institute of Nutritional Sciences Friedrich Schiller University and Competence Cluster for Nutrition and Cardiovascular Health, Halle-Jena-Leipzig, Jena, Germany (A.P.M.).

Henrik Rudolf (H)

Institute for Biostatistics and Informatics in Medicine and Ageing Research, Rostock University, Germany (H.R.).

Heribert Schunkert (H)

Department of Cardiology, German Heart Center Munich, Technical University of Munich and Partner Site Munich Heart Alliance, German Center for Cardiovascular Disease, Germany (H.S.).

Andreas Stang (A)

Institute for Medical Informatics, Biometry and Epidemiology, University Hospital Essen, University Duisburg-Essen, Germany (A.S., B.S.).
School of Public Health, Department of Epidemiology, Boston University, MA (A.S.).

Winfried März (W)

Clinical Institute of Medical and Chemical Laboratory Diagnostics, Medical University of Graz, Austria. (W.M., H.S.).
Vth Department of Medicine, Medical Faculty Mannheim, Heidelberg University, Mannheim, Germany (W.M., M.E.K.).
Synlab Academy, Synlab Holding Germany, Mannheim (W.M.).

Hans J Trampisch (HJ)

Department of Medical Informatics, Biometry and Epidemiology, Ruhr University, Bochum, Germany (U.T., H.J.T.).

Hubert Scharnagl (H)

Clinical Institute of Medical and Chemical Laboratory Diagnostics, Medical University of Graz, Austria. (W.M., H.S.).

Robert J Konrad (RJ)

Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN (Y.Q.C., H.L., D.L., Y.W., E.Y.Z., Y.Q., R.J.K.).

Classifications MeSH