Publications by authors named "Pedro J Del Rivero Morfin"

L-type Ca channels (Ca1.2/1.3) convey influx of calcium ions that orchestrate a bevy of biological responses including muscle contraction, neuronal function, and gene transcription.

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  • The study investigates how the protein Rad influences heart function during stress by affecting calcium ion influx and contraction strength.
  • It focuses on specific phosphorylation sites on Rad (Ser272 and Ser300) that modulate its interaction with voltage-gated calcium channels, which are crucial for increasing cardiac output.
  • The findings suggest that Rad's ability to detach from the membrane is essential for enhancing calcium currents during sympathetic nervous system activation, especially when the heart is responding to threats.
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Voltage-dependent and Ca2+-dependent inactivation (VDI and CDI, respectively) of CaV channels are two biologically consequential feedback mechanisms that fine-tune Ca2+ entry into neurons and cardiomyocytes. Although known to be initiated by distinct molecular events, how these processes obstruct conduction through the channel pore remains poorly defined. Here, focusing on ultrahighly conserved tryptophan residues in the interdomain interfaces near the selectivity filter of CaV1.

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L-type Ca channels (Ca 1.2/1.3) convey influx of calcium ions (Ca ) that orchestrate a bevy of biological responses including muscle contraction and gene transcription.

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Voltage-dependent and Ca-dependent inactivation (VDI and CDI, respectively) of Ca channels are two biologically consequential feedback mechanisms that fine-tune Ca entry into neurons and cardiomyocytes. Although known to be initiated by distinct molecular events, how these processes obstruct conduction through the channel pore remains poorly defined. Here, focusing on ultra-highly conserved tryptophan residues in the inter-domain interfaces near the selectivity filter of Ca1.

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Calcium influx through voltage-gated calcium channels, Ca1.2, in cardiomyocytes initiates excitation-contraction coupling in the heart. The force and rate of cardiac contraction are modulated by the sympathetic nervous system, mediated substantially by changes in intracellular calcium.

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Acylation, a reversible post-translational lipid modification of proteins, controls the properties and function of various proteins, including ion channels. Large conductance Ca-activated potassium (BK) channels are acylated at two sites that impart distinct functional effects. Whereas the enzymes that attach lipid groups are known, the enzymes mediating lipid removal ( deacylation) are largely unknown.

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Article Synopsis
  • The study investigates how cardiac Ca1.2 channels, crucial for heart function, are regulated under different conditions like normal activity, sympathetic activation, and heart failure.
  • Researchers created specific transgenic mice to analyze the effects of mutations and splice variants on the channel's behavior and response to β-adrenergic stimulation.
  • Findings reveal that the α I-II loop plays a key role in modulating the activity of Ca1.2 channels, with variations impacting both the channel's open probability and its responsiveness to stimulating signals.
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Background: Documenting the patterns of oral anticoagulation therapy (OAT) is essential to prevent thromboembolic complications of nonvalvular atrial fibrillation (NVAF).

Objective: To report the patterns of OAT according to age and thromboembolic risk in patients included in CARMEN-AF, a nationwide registry of NVAF in Mexico, an upper middle-income country.

Material And Methods: There were 1,423 consecutive patients ≥18 years old and with at least one thromboembolic risk factor enrolled in the CARMEN-AF Registry at their regular clinical visit during a three-year period.

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