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Metabolic Coordination Structures Contribute to Diabetic Myocardial Dysfunction.

Teng Wu1,2,3, Tongsheng Huang1,2, Honglin Ren1,2

  • 1Guangdong Engineering & Technology Research Center for Disease-Model Animals, Laboratory Animal Center (T.W., T.H., H.R., C.S., J.Q., X.F., J.W., S.X., Y.J., M.L., H.Z., Y.Z., K.L., Maoquan Yang, Z.S., X. Li, Y.W., Ming Yang, H.L., X.H., J.T., W.C.), Sun Yat-sen University, Guangzhou, China.

Circulation Research
|April 7, 2025
PubMed
Summary

Acyl-coenzyme A-binding protein (ACBP) exacerbates cardiac dysfunction in type 2 diabetes by disrupting cardiomyocyte structure and metabolism. Targeting ACBP offers a potential therapeutic strategy for diabetic heart disease.

Keywords:
diabetic cardiomyopathieslipid metabolismmyocardial contractionmyocytes, cardiac

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Area of Science:

  • Cardiology
  • Metabolic Disorders
  • Molecular Biology

Background:

  • Diabetes mellitus is a significant risk factor for cardiac dysfunction and heart failure.
  • Diabetic cardiomyopathy involves metabolic disturbances and structural remodeling of the heart.
  • The interplay between metabolic and structural changes in diabetic heart disease remains poorly understood.

Purpose of the Study:

  • To investigate the role of acyl-coenzyme A-binding protein (ACBP) in the metabolic and structural coupling of diabetic cardiac dysfunction.
  • To elucidate the underlying mechanisms by which ACBP influences cardiac structure and function in type 2 diabetes.

Main Methods:

  • Utilized mouse models of type 2 diabetes (T2DM) to analyze cardiac metabolism and structure.
  • Screened public datasets to identify ACBP as a potential mediator of T2DM-associated heart disease.
  • Employed in vivo loss-of-function and gain-of-function studies, metabolomics, co-immunoprecipitation, and ChIP sequencing to investigate ACBP's role and mechanisms.

Main Results:

  • Diabetic hearts showed altered lipid metabolism, impaired ultrastructure, and systolic/diastolic dysfunction.
  • ACBP expression was upregulated in diabetic hearts and associated with disease severity.
  • ACBP knockout attenuated T2DM-induced cardiac remodeling and dysfunction, while overexpression exacerbated it.
  • ACBP was found to interact with MyBPC3, potentially impairing myocardial contraction, and its transcription is regulated by PPARγ.

Conclusions:

  • ACBP plays a critical role in the bidirectional regulation of cardiomyocyte metabolism and structure in T2DM.
  • ACBP represents a potential therapeutic target for mitigating cardiac dysfunction in diabetic patients.