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DIP2A functions as a FSTL1 receptor.

Noriyuki Ouchi1, Yasuhide Asaumi, Koji Ohashi

  • 1Molecular Cardiology/Whitaker Cardiovascular Institute, Boston University School of Medicine, Boston, Massachusetts 02118, USA.

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Follistatin-like 1 (FSTL1) uses DIP2A as its receptor to protect the heart and vasculature. This discovery reveals DIP2A

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Area of Science:

  • Cardiovascular Biology
  • Molecular Cell Biology
  • Biochemistry

Background:

  • Follistatin-like 1 (FSTL1) is an extracellular glycoprotein with incompletely understood roles in physiological and pathological conditions.
  • Previous research indicated FSTL1, a muscle-derived factor, benefits the heart and vasculature, particularly under ischemic stress.
  • Identifying the FSTL1 receptor is crucial for understanding its mechanism of action.

Purpose of the Study:

  • To identify the specific receptor mediating the cellular effects of FSTL1.
  • To investigate the interaction between FSTL1 and its potential receptor in cardiovascular cells.
  • To elucidate the role of this receptor in FSTL1's protective functions.

Main Methods:

  • Utilized co-immunoprecipitation assays to detect FSTL1-binding partners.
  • Investigated FSTL1 binding to endothelial cells with and without DIP2A knockdown via small interfering RNA (siRNA).
  • Assessed FSTL1-stimulated endothelial cell survival, migration, network formation, and Akt phosphorylation following DIP2A knockdown.
  • Examined FSTL1's protective effects against hypoxia/reoxygenation-induced apoptosis and Akt phosphorylation in cardiac myocytes with DIP2A ablation.

Main Results:

  • Identified Diver-interacting protein homolog A (DIP2A) as a novel FSTL1-binding partner on the membrane of endothelial cells.
  • Confirmed a direct physical interaction between FSTL1 and DIP2A.
  • Demonstrated that DIP2A is present on the surface of endothelial cells and mediates FSTL1 binding.
  • Showed that DIP2A knockdown diminished FSTL1-induced endothelial cell survival, migration, network differentiation, and Akt phosphorylation.
  • Revealed that DIP2A ablation reduced FSTL1's protective effects against cardiac myocyte apoptosis and suppressed FSTL1-induced Akt phosphorylation.

Conclusions:

  • DIP2A functions as a novel cell surface receptor for FSTL1.
  • DIP2A mediates the cardiovascular protective effects of FSTL1 in both endothelial cells and cardiac myocytes.
  • This finding provides a key mechanistic insight into FSTL1's beneficial actions in the cardiovascular system.