SNII Área II FISIOLOGÍA HUMANA 55 PEREZ CORNEJO, GLORIA PATRICIA
PEREZ CORNEJO, GLORIA PATRICIA

PEREZ CORNEJO, GLORIA PATRICIA

CIENCIAS DE LA VIDA · Nivel 1

Chloride channels Electrophysiology Purinergic receptors

Desde 1996 es Profesor-Investigador en Universidad Autonoma de San Luis Potosi

RESEARCH My work is focused on two topics: TMEM16A channels and P2X7 purinergic receptors. TMEM16A channels The calcium-activated chloride channels...

RESEARCH

My work is focused on two topics: TMEM16A channels and P2X7 purinergic receptors.

TMEM16A channels

The calcium-activated chloride channels TMEM16A and TMEM16B play a role in numerous physiological processes such as: water and electrolyte secretion, sensory transduction, regulation of vascular tone, cardiac excitability and neuronal excitability. The genes ANO1 and ANO2 that code for these channels were identified in 2008. I am interested in learning about the activation and regulatory mechanisms that allow the TMEM16A channel to function in a cellular context. Thus far we have learned that TMEM16A displays complex chloride current kinetics since channel gating involves interactions between the intracellular calcium concentration, membrane depolarization, extracellular Cl−, permeant anions and binding of extracellular protons to glutamic acid 623 and intracellular protons to the calcium-pocket. In addition, cytosolic factors, cytoskeletal proteins, and membrane lipids modulate channel activity. For example, we found that cAMP down regulates CaCC through a dual mechanism involving PKA and CFTR; downregulating the expression of moesin in HEK-293 cells changes channel activity; PI(4,5)P2 is required for TMEM16A activity while cholesterol regulate channel function but is not essential. We also found that exogenous stearic, arachidonic, oleic, docosahexaenoic, and eicosapentaenoic fatty acids inhibit TMEM16A in a dose- and voltage-dependent manner.

P2X7 purinergic receptors

Purinergic receptors belong to the P2X receptor family composed of seven members that function as cationic channels when activated by extracellular ATP. These receptors are expressed in the central nervous system, immune system and other tissues. We have studied the crossregulation of P2X4 and P2X7 receptors. Until 2007 it was believed that P2X7 did not interact with other purinergic receptors. We showed that P2X4 and P2X7 interact with each other through protein-protein contacts. This interaction is relevant for the physiological function of mouse macrophages. Also, we have documented the importance of P2X7 in the phagocytosis of yeast and bacteria.

TEACHING

I devote some of my time to learn about the effectiveness of different teaching interventions to help my students learn more effectively. I am also interested in applying the Item Response Theory for item banking and test equating.

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Perfil académico

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Contenido de ORCID y Scopus 50/50
ORCID: identificador válido 7/7
ORCID: biografía 343 palabras 8/8
ORCID: palabras clave 3 palabras clave 4/4
Scopus: identificador válido 5/5
Publicaciones visibles Fuente: ORCID 26/26
Redes académicas 2/23
Google Académico Aún no registrado 0/8
ResearchGate / Academia.edu Aún no registrado 0/8
Redes especializadas (Web of Science, Loop o SciProfiles) 2/2
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Clasificación disciplinar 5/27
Especialidad válida Aún no registrado 0/22
Institución y entidad de acreditación válidas 5/5

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Nombre GLORIA PATRICIA PEREZ CORNEJO
Área BIOLOGÍA Y QUÍMICA
Campo CIENCIAS DE LA VIDA
Disciplina FISIOLOGÍA HUMANA
Especialidad OTRAS
CVU 16847
Institución
Tipo de institución Pública
Dependencia FACULTAD DE MEDICINA
Entidad SAN LUIS POTOSI
Nivel 1
Vigencia Inicio: 01/01/2024
Fin: 31/12/2028

Evolución en el SNII

  • Candidato: 1997–1999
  • Nivel I: 2000–2008
  • Nivel I: 2010–2016
  • Nivel II: 2017–2020
  • Nivel I: 2021–2026

Publicaciones ORCID

2022
Gating and anion selectivity are reciprocally regulated in TMEM16A (ANO1) Journal of General Physiology
Function and Regulation of the Calcium-Activated Chloride Channel Anoctamin 1 (TMEM16A) Handbook of Experimental Pharmacology · ISSN 0171-2004
Oleic acid blocks the calcium-activated chloride channel TMEM16A/ANO1 Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · ISSN 1388-1981
2021
Nutrition education on obesity and diabetes to medical students Advances in Physiology Education · ISSN 1043-4046
2020
Voltage-Dependent Protonation of the Calcium Pocket Enable Activation of the Calcium-Activated Chloride Channel Anoctamin-1 (TMEM16A) Scientific Reports · ISSN 2045-2322
Regulation of the Ca2+-activated chloride channel Anoctamin-1 (TMEM16A) by Ca2+-induced interaction with FKBP12 and calcineurin Cell Calcium · ISSN 0143-4160
2018
Phosphatidylinositol 4,5-bisphosphate, cholesterol, and fatty acids modulate the calcium-activated chloride channel TMEM16A (ANO1) Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · ISSN 1388-1981
2017
Extracellular protons enable activation of the calcium-dependent chloride channel TMEM16A The Journal of Physiology · ISSN 0022-3751
2016
P2X7 from j774 murine macrophages acts as a scavenger receptor for bacteria but not yeast Biochemical and Biophysical Research Communications
Revealing the activation pathway for TMEM16A chloride channels from macroscopic currents and kinetic models Pflügers Archiv - European Journal of Physiology · ISSN 0031-6768