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Regulation of Blood Pressure by Targeting CaV1.2-Galectin-1 Protein Interaction
Zhenyu Hu1, Guang Li2, Jiong-Wei Wang1,3,4
1Department of Physiology, Yong Loo Lin School of Medicine (Z.Y.H., J.-W.W., D.Y., M.C.L., Y.P.W., T.W.S.), National University of Singapore.
Circulation
|April 14, 2018
Summary
Galectin-1 (Gal-1) promotes proteasomal degradation of L-type CaV1.2 channels by disrupting CaVβ binding, influencing blood pressure. Targeting this interaction offers a potential therapeutic strategy for hypertension.
Area of Science:
- Cardiovascular Physiology
- Molecular Cell Biology
- Biochemistry
Background:
- L-type CaV1.2 channels are critical for blood pressure regulation.
- Galectin-1 (Gal-1) binds CaV1.2 channels, reducing current density, but the mechanism and blood pressure role are unclear.
Purpose of the Study:
- To elucidate the molecular mechanism of Gal-1-mediated CaV1.2 channel downregulation.
- To investigate the direct role of Gal-1 in blood pressure regulation.
Main Methods:
- In vitro: Co-immunoprecipitation, Western blot, patch-clamp, immunohistochemistry, pressure myography.
- In vivo: Peptide (Tat-e9c) and viral vector (AAV5-Gal-1) delivery in rats to assess blood pressure effects.
Main Results:
- Gal-1 induces CaV1.2 proteasomal degradation by allosterically competing with CaVβ, leading to polyubiquitination.
- Hypertension in rats and patients correlates inversely with Gal-1 and directly with CaV1.2 levels.
- Disrupting Gal-1 interaction increased blood pressure; overexpressing Gal-1 reduced it.
Conclusions:
- Gal-1 promotes CaV1.2 degradation by displacing CaVβ and masking export signals, clarifying its role in blood pressure.
- Targeting the CaV1.2-Gal-1 interaction is a potential therapeutic strategy for hypertension.
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