Ponce-Coria José | UNAM Universidad Nacional Autónoma de México (original) (raw)

Papers/Scientific publications by Ponce-Coria José

Background: WNK4 acts upstream of SPAK/OSR1 in the regulation of Na-K-2Cl cotransporters. Results... more Background: WNK4 acts upstream of SPAK/OSR1 in the regulation of Na-K-2Cl cotransporters. Results: Here we show that WNK4 directly binds to NKCC1, and in the presence of Cab39 it stimulates NKCC1 activity. Conclusion: WNK4 regulates NKCC1 through SPAK/OSR1-dependent and SPAK/OSR1-independent pathways. Significance: We uncovered a novel mode of Na-K-2Cl cotransporter activation which involves a direct interaction of WNK4 with the cation-chloride cotransporter.

The K-Cl cotransporter (KCC) functions in maintaining chloride and volume homeostasis in a variet... more The K-Cl cotransporter (KCC) functions in maintaining chloride and volume homeostasis in a variety of cells. In the process of cloning the mouse KCC3 cDNA, we came across a cloning mutation (E289G) that rendered the cotransporter inactive in functional assays in Xenopus laevis oocytes. Through biochemical studies, we demonstrate that the mutant E289G cotransporter is glycosylation-deficient, does not move beyond the endoplasmic reticulum or the early Golgi, and thus fails to reach the plasma membrane. We establish through co-immunoprecipitation experiments that both wild-type and mutant KCC3 with KCC2 results in the formation of hetero-dimers. We further demonstrate that formation of these hetero-dimers prevents the proper trafficking of the cotransporter to the plasma membrane, resulting in a significant decrease in cotransporter function. This effect is due to interaction between the K-Cl cotransporter isoforms, as this was not observed when KCC3-E289G was co-expressed with NKCC1. Our studies also reveal that the glutamic acid residue is essential to K-Cl cotransporter function, as the corresponding mutation in KCC2 also leads to an absence of function. Interestingly, mutation of this conserved glutamic acid residue in the Na(+)-dependent cation-chloride cotransporters had no effect on NKCC1 function in isosmotic conditions, but diminished cotransporter activity under hypertonicity. Together, our data show that the glutamic acid residue (E289) is essential for proper trafficking and function of KCCs and that expression of a non-functional but full-length K-Cl cotransporter might results in dominant-negative effects on other K-Cl cotransporters.

X-ray crystallography of the catalytic domain of oxidative stress response 1 (OSR1) has provided ... more X-ray crystallography of the catalytic domain of oxidative stress response 1 (OSR1) has provided evidence for dimerization and domain swapping. However, the functional significance of dimer formation or domain swapping has yet to be addressed. In this study, we used nine glutamine residues to link the carboxyl end of one SPAK (related Ste20 kinase) monomer to the amino end of another SPAK monomer to assess the role of kinase monomers versus dimers in Na-K-2Cl cotransporter 1 (NKCC1) activation. Transport studies in Xenopus laevis oocytes show that forcing dimerization of two wild-type SPAK molecules results in cotransporter activation when calcium-binding protein 39 (Cab39) is coexpressed, indicating that the presence of Cab39 can bypass the upstream phosphorylation requirement of SPAK normally associated with kinase activation. We determined that monomers are the functional units of the kinase as concatamers consisting of an active and various inactive monomers were still functional. Furthermore, we found that two different nonfunctional SPAK mutants could be linked together in a concatamer and activated, presumably by domain swapping, indicating that dimerization and domain swapping are both important components of kinase activation. Finally, we demonstrate rescue of a nonfunctional SPAK mutant by domain swapping with wild-type OSR1, indicating that heterodimers of the two Ste20-related kinases are possible and therefore potentially relevant to the regulation of NKCC1 activity.

Transforming growth factor-beta (TGF-beta) is a key mediator in the pathogenesis of renal disease... more Transforming growth factor-beta (TGF-beta) is a key mediator in the pathogenesis of renal diseases. Betaglycan, also known as the type III TGF-beta receptor, regulates TGF-beta action by modulating its access to the type I and II receptors. Betaglycan potentiates TGF-beta; however, soluble betaglycan, which is produced by the shedding of the membrane-bound receptor, is a potent antagonist of TGF-beta. In the present work, we have used a recombinant form of soluble betaglycan (SBG) to prevent renal damage in genetically obese and diabetic db/db mice. Eight-wk-old db/db or nondiabetic (db/m) mice were injected intraperitoneally with 50 mug of SBG or vehicle alone three times a wk for 8 wk. The db/db mice that received vehicle presented albuminuria and increased serum creatinine, as well as glomerular mesangial matrix expansion. The db/db mice treated with SBG exhibited a reduction in serum creatinine, albuminuria, and structural renal damage. These effects were associated with lower kidney levels of mRNAs encoding TGF-beta1, TGF-beta2, TGF-beta3, collagen IV, collagen I, fibronectin, and serum glucocorticoid kinase as well as a reduction in the immunostaining of collagen IV and fibronectin. Our data indicate that SBG is a renoprotective agent that neutralized TGF-beta actions in this model of nephropathy. Because SBG has a high affinity for all TGF-beta isoforms, in particular TGF-beta2, it is found naturally in serum and tissues and its shedding may be regulated. We believe that SBG shall prove convenient for long-term treatment of kidney diseases and other pathologies in which TGF-beta plays a pathophysiological role.

Microbial flavohaemoglobins are proteins with homology to haemoglobins from higher organisms, but... more Microbial flavohaemoglobins are proteins with homology to haemoglobins from higher organisms, but clearly linked to nitric oxide (NO) metabolism by bacteria and yeast. hmp mutant strains of several bacteria are hypersensitive to NO and related compounds and hmp genes are up-regulated by the presence of NO. The regulatory mechanisms involved in hmp induction by NO and the superoxide-generating agent, methyl viologen (paraquat; PQ), are complex, but progressively being resolved. Here we show for the first time that, in Salmonella enterica serovar Typhimurium, hmp transcription is increased on exposure to PQ and demonstrate that RamA, a homologue of MarA is responsible for most of the hmp paraquat regulation. In addition we demonstrate NO-dependent elevation of Salmonella hmp transcription and Hmp accumulation. In both Escherichia coli and Salmonella modest transcriptional repression of hmp is exerted by the iron responsive transcriptional repressor Fur. Finally, in contrast to previous reports, we show that in E. coli and Salmonella, hmp induction by both paraquat and sodium nitroprusside is further elevated in a fur mutant background, indicating that additional regulators are implicated in this control process.

WNK kinases [with no lysine (K) kinase] are emerging as regulators of several membrane transport ... more WNK kinases [with no lysine (K) kinase] are emerging as regulators of several membrane transport proteins in which WNKs act as molecular switches that coordinate the activity of several players. Members of the cation-coupled chloride cotransporters family (solute carrier family number 12) are one of the main targets. WNK3 activates the Na(+)-driven cotransporters NCC, NKCC1, and NKCC2 and inhibits the K(+)-driven cotransporters KCC1 to KCC4. WNK4 inhibits the activity of NCC and NKCC1, while in the presence of the STE20-related proline-alanine-rich kinase SPAK activates NKCC1. Nothing is known, however, regarding the effect of WNK4 on the K(+)-Cl(-) cotransporters. Using the heterologous expression system of Xenopus laevis oocytes, here we show that WNK4 inhibits the activity of the K(+)-Cl(-) cotransporters KCC1, KCC3, and KCC4 under cell swelling, a condition in which these cotransporters are maximally active. The effect of WNK4 requires its catalytic activity because it was lost by the substitution of aspartate 318 for alanine (WNK4-D318A) that renders WNK4 catalytically inactive. In contrast, three different WNK4 missense mutations that cause pseudohypoaldosteronism type II do not affect the WNK4-induced inhibition of KCC4. Finally, we observed that catalytically inactive WNK4-D318A is able to bypass the tonicity requirements for KCC2 and KCC3 activation in isotonic conditions. This effect is enhanced by the presence of catalytically inactive SPAK, was prevented by the presence of protein phosphatase inhibitors, and was not present in KCC1 and KCC4. Our results reveal that WNK4 regulates the activity of the K(+)-Cl(-) cotransporters

Two members of a recently discovered family of protein kinases are the cause of an inherited dise... more Two members of a recently discovered family of protein kinases are the cause of an inherited disease known as pseudohypoaldosteronism type II (PHAII). These patients exhibit arterial hypertension together with hyperkalemia and metabolic acidosis. This is a mirror image of Gitelman disease that is due to inactivating mutations of the SLC12A3 gene that encodes the thiazide-sensitive Na(+):Cl(-) cotransporter. The uncovered genes causing PHAII encode for serine/threonine kinases known as WNK1 and WNK4. Physiological and biochemical studies have revealed that WNK1 and WNK4 modulate the activity of several transport pathways of the aldosterone-sensitive distal nephron, thus increasing our understanding of how diverse renal ion transport proteins are coordinated to regulate normal blood pressure levels. Observations discussed in the present work place WNK1 and WNK4 as genes involved in the genesis of essential hypertension and as potential targets for the development of antihypertensive drugs.

Apical bumetanide-sensitive Na(+)-K(+)-2Cl(-) cotransporter (NKCC2), the kidney-specific member o... more Apical bumetanide-sensitive Na(+)-K(+)-2Cl(-) cotransporter (NKCC2), the kidney-specific member of a cation-chloride cotransporter superfamily, is an integral membrane protein responsible for the transepithelial reabsorption of NaCl. The role of NKCC2 is essential for renal volume regulation. Vasopressin (AVP) controls NKCC2 surface expression in cells of the thick ascending limb of the loop of Henle (TAL). We found that 40-70% of Triton X-100-insoluble NKCC2 was present in cholesterol-enriched lipid rafts (LR) in rat kidney and cultured TAL cells. The related Na(+)-Cl(-) cotransporter (NCC) from rat kidney was distributed in LR as well. NKCC2-containing LR were detected both intracellularly and in the plasma membrane. Bumetanide-sensitive transport of NKCC2 as analyzed by (86)Rb(+) influx in Xenopus laevis oocytes was markedly reduced by methyl-beta-cyclodextrin (MbetaCD)-induced cholesterol depletion. In TAL, short-term AVP application induced apical vesicular trafficking along with a shift of NKCC2 from non-raft to LR fractions. In parallel, increased colocalization of NKCC2 with the LR ganglioside GM1 and their polar translocation were assessed by confocal analysis. Apical biotinylation showed twofold increases in NKCC2 surface expression. These effects were blunted by mevalonate-lovastatin/MbetaCD-induced cholesterol deprivation. Collectively, these findings demonstrate that a pool of NKCC2 distributes in rafts. Results are consistent with a model in which LR mediate polar insertion, activity, and AVP-induced trafficking of NKCC2 in the control of transepithelial NaCl transport.

Loss of physiological regulation of the renal thiazide-sensitive Na+-Cl- cotransporter (NCC) by m... more Loss of physiological regulation of the renal thiazide-sensitive Na+-Cl- cotransporter (NCC) by mutant WNK1 or WNK4 results in pseudohypoaldosteronism type II (PHAII) characterized by arterial hypertension and hyperkalemia. WNK4 normally inhibits NCC, but this effect is lost by eliminating WNK4 catalytic activity or through PHAII-type mutations. In contrast, another member of the WNK family, WNK3, activates NCC. The positive effect of WNK3 on NCC also requires its catalytic activity. Because the opposite effects of WNK3 and WNK4 on NCC were observed in the same expression system, sequences within the WNKs should endow these kinases with their activating or inhibiting properties. To gain insight into the structure-function relationships between the WNKs and NCC, we used a chimera approach between WNK3 and WNK4 to elucidate the domain of the WNKs responsible for the effects on NCC. Chimeras were constructed by swapping the amino or carboxyl terminus domains, which flank the central kinase domain, between WNK3 and WNK4. Our results show that the effect of chimeras toward NCC follows the amino-terminal domain. Thus the amino terminus of the WNKs contains the sequences that are required for their activating or inhibiting properties on NCC.

"OBJECTIVES: Screening for variants in SLC12A1 and SLC12A3 genes, encoding the renal Na:Cl (NCC) ... more "OBJECTIVES: Screening for variants in SLC12A1 and SLC12A3 genes, encoding the renal Na:Cl (NCC) and Na:K:2Cl (NKCC2) cotransporters, respectively, in 3125 members of the Framingham Heart Study (FHS) revealed that carrying a rare mutation in one of these genes was associated with a significant reduction in blood pressure, in the risk of arterial hypertension, and of death due to cardiovascular disease. Because near 60% of the rare mutations identified have not been related to Bartter's or Gitelman's disease, the consequence of such mutations on cotransporter activity is unknown.

METHODS: We used the heterologous expression system of Xenopus laevis oocytes, microinjected with wild-type or mutant NCC or NKCC2 cRNAs, to examine the effect of these inferred NCC and NKCC2 mutations on the cotransporters' functional properties. Cotransporter activity was defined as the diuretic-sensitive radioactive tracer uptake and response to known modulators was assessed.

RESULTS: Basal NCC activity was significantly reduced in all NCC mutants and, excluding NCC-S186F, response to WNK3, WNK4, or intracellular chloride depletion was conserved. Similarly, basal activity was reduced in six out of nine NKCC2 mutants and response to WNK3 was maintained. No effect on protein expression was seen, except for NCC-S186F, which was significantly reduced.

CONCLUSIONS: The rare NCC or NKCC2 mutations found in the FHS significantly reduced the basal activity of the cotransporters. This observation supports that even a small, but chronic reduction of NCC or NKCC2 function results in a lower blood pressure and decreased risk of hypertension in otherwise healthy individuals in the general population."

Proceedings of the …, Jan 1, 2008

The Na(+):K(+):2Cl(-) cotransporter (NKCC2) is the target of loop diuretics and is mutated in Bar... more The Na(+):K(+):2Cl(-) cotransporter (NKCC2) is the target of loop diuretics and is mutated in Bartter's syndrome, a heterogeneous autosomal recessive disease that impairs salt reabsorption in the kidney's thick ascending limb (TAL). Despite the importance of this cation/chloride cotransporter (CCC), the mechanisms that underlie its regulation are largely unknown. Here, we show that intracellular chloride depletion in Xenopus laevis oocytes, achieved by either coexpression of the K-Cl cotransporter KCC2 or low-chloride hypotonic stress, activates NKCC2 by promoting the phosphorylation of three highly conserved threonines (96, 101, and 111) in the amino terminus. Elimination of these residues renders NKCC2 unresponsive to reductions of [Cl(-)](i). The chloride-sensitive activation of NKCC2 requires the interaction of two serine-threonine kinases, WNK3 (related to WNK1 and WNK4, genes mutated in a Mendelian form of hypertension) and SPAK (a Ste20-type kinase known to interact with and phosphorylate other CCCs). WNK3 is positioned upstream of SPAK and appears to be the chloride-sensitive kinase. Elimination of WNK3's unique SPAK-binding motif prevents its activation of NKCC2, as does the mutation of threonines 96, 101, and 111. A catalytically inactive WNK3 mutant also completely prevents NKCC2 activation by intracellular chloride depletion. Together these data reveal a chloride-sensing mechanism that regulates NKCC2 and provide insight into how increases in the level of intracellular chloride in TAL cells, as seen in certain pathological states, could drastically impair renal salt reabsorption.

Conference Presentations/Scientific talks by Ponce-Coria José

Constancia a José Ponce Coria por su participación como Ponente del tema: Papel de los cotranspor... more Constancia a José Ponce Coria por su participación como Ponente del tema: Papel de los cotransportadores de sodio potasio dos cloruros (NKCCs) en la salud humana, realizado en las instalaciones de la Facultad de Estudios Superiores Zaragoza el 9 de septiembre del 2015.

"Screening of more than 3 thousand members of the Framingham Heart Study for variations in the re... more "Screening of more than 3 thousand members of the Framingham Heart Study for variations in the renal NaCl cotransporter, NCC, revealed that subjects with rare independent mutations in one allele have a significantly lower blood pressure and are protected against hypertension (Ji et al, Nature Gen, 2008). Although some of the mutations were previously reported as cause of Gitelman’s disease, others have not been shown to be associated with this inherited disease and thus, the consequence of such mutations in NCC activity is not known. We have introduced five independent mutations in the rat NCC sequence to find out the consequences upon NCC functional properties. The analyzed mutations were L153F, S186F, A230T, F493L, and G777E. Xenopus laevis oocytes were injected with 20 ng ofwild type or mutants NCC cRNA and three days later the basal activity and response to regulators was assessed by measuring the thiazide-sensitive 22Na+ Uptake. To assess the effect of modulators, oocytes were co-injected with WNK3 or WNK4 cRNA, or were exposed to intracellular chloride depletion maneuvers (ICD) known to activate NCC (Pacheco-Alvarez et al, JBC 2006). The activity of wild type NCC was taken as 100% and data from all groups was normalized accordingly.
The basal NCC activity was significantly reduced in four out of the five mutants NCCs. The percentage of activity was 60 %, 10%, 45 %, and 63 % for L153F, S186F, A230T, and F493L mutants, respectively. The S186F mutant not only exhibited a dramatic decrease in activity, but also showed no response to WNK3 or to ICD. In contrast, although basal activity was reduced in L153F, A230T, and F493L mutants, the response to WNK3, WNK4,
and ICD was similar to wild type NCC. Interestingly, the basal activity of mutant G777E was similar to NCC. This mutant, however, exhibited a 40 % reduction of WNK3-induced activation, while response to ICD was conserved. We conclude that reduction of NCC activity or response to WNK3 is the mechanism by which these rare independent mutations in NCC protect against arterial hypertension."

"Activation of the renal Na+:K+:2Cl- cotransporter by the kinase WNK3 requires interaction betwee... more "Activation of the renal Na+:K+:2Cl- cotransporter by the kinase WNK3 requires interaction between WNK3 and a serine/threonine kinase known as SPAK (Ponce-Coria et al, PNAS 2008), recently shown to be associated with hypertension in a genome wide association study (Wang et al, PNAS 2009). The direct role of SPAK and its closely related homologue kinase OSR1 in the modulation of NKCC2 activity, however, is not known. The effect of wild type SPAK (WT-SPAK) or OSR1 (WT-OSR1) or catalytically inactive SPAK (KI-SPAK) or OSR1 (KI-OSR1) upon the renal specific NKCC2 and the ubiquitously expressed NKCC1 was assessed in Xenopus laevis oocytes. To this end, oocytes were microinjected with 10 ng of NKCC2 or NKCC1 cRNA alone or together with 10 ng of WT or KI SPAK and/or OSR1 cRNA. Three days later NKCC function was determined as the bumetanide-sensitive 86Rb+ uptake. The activity of NKCC2 and NKCC1 was not affected by WT-SPAK, but was decreased by KI-SPAK, suggesting that endogenous SPAK is required to sustain basal activity. Consistent with these observations, elimination of the unique SPAK binding motif of NKCC2 (NKCC2-F17A) resulted in reduction of NKCC2 function. In addition, basal activity of NKCC2-F17A was not further affected by KI-SPAK. Interestingly, activity of NKCC1 was not affected by WT-OSR1, but was decreased by KI-OSR1, while activity
of NKCC2 was decreased by both WT- or KI-OSR1. Reduction of NKCC2 by KI-OSR1 was prevented by WT-SPAK cRNA. Since oocytes express SPAK, but not OSR1, these observations suggest that NKCC1 can be regulated by SPAK and OSR1, while NKCC2 is only modulated by SPAK, and the negative effect of OSR1 is probably of the dominant negative type. Finally, the positive effect of WNK3 or intracellular chloride depletion upon the cotransporter activity was conserved for NKCC2 in the presence of KI-SPAK and for the mutant NKCC2-F17A. Our data suggest that SPAK-NKCC2 interaction is required to sustain basal activity of NKCC2, but not for activation of the cotransporter by WNK3, in which the critical interaction occurs between WNK3 and SPAK (Ponce-Coria, et al. PNAS 2008). Finally, OSR1 is a positive regulator of NKCC1, but not of NKCC2."

Course certificates by Ponce-Coria José

"Nutrition and Lifestyle in Pregnancy" online course authorized by Ludwig-Maximilians-Universitä... more "Nutrition and Lifestyle in Pregnancy"

online course authorized by Ludwig-Maximilians-Universität München (LMU) and offered through Coursera

Verify at coursera.org/verify/M2Q2TB9NFZK5 Coursera has confirmed the identity of José Ponce Coria and his participation in the course.

Jose Ponce Coria has successfully completed with honors: " "Introduction to the Biology of Cancer... more Jose Ponce Coria has successfully completed with honors: "
"Introduction to the Biology of Cancer"
an online non-credit course authorized by Johns Hopkins University and offered
through Coursera
Kenneth J. Pienta, M.D.
The Donald S. Coffey Professor of Urology
Professor of Oncology
The James Buchanan Brady Urological Institute
The Johns Hopkins University School of Medicine
Verify at coursera.org/verify/3DKEK2M7PX6Y
Coursera has confirmed the identity of this individual and
their participation

Por este conducto se informa que el Dr. José Ponce Coria, fue aceptado para cursar el "Diplomado ... more Por este conducto se informa que el Dr. José Ponce Coria, fue aceptado para cursar el "Diplomado en Docencia Universitaria" El diplomado tiene un valor curricular de 240 horas.

La Facultad de Estudios Superiores Zaragoza UNAM a través de la Dirección General de Asuntos del ... more La Facultad de Estudios Superiores Zaragoza UNAM a través de la Dirección General de Asuntos del Personal Académico otorga la constancia a:

José Ponce Coria

por cumplir con los objetivos del curso-taller Recuperación de Evidencias Científicas en Medios Electrónicos, llevado a cabo del 17 al 18 de julio del 2015. Duración: 20 horas.

Firma: Dr. Víctor Manuel Mendoza Núñez Director de la FES-Z

Curso impartido por: Dr. Mario Rodriguez León. Jefe de la carrera Médico Cirujano FES-Z UNAM

Proceedings of the …, Jan 1, 2008

"Nutrition and Lifestyle in Pregnancy" online course authorized by Ludwig-Maximilians-Universitä... more "Nutrition and Lifestyle in Pregnancy"

online course authorized by Ludwig-Maximilians-Universität München (LMU) and offered through Coursera

Verify at coursera.org/verify/M2Q2TB9NFZK5 Coursera has confirmed the identity of José Ponce Coria and his participation in the course.

José Ponce Coria

por cumplir con los objetivos del curso-taller Recuperación de Evidencias Científicas en Medios Electrónicos, llevado a cabo del 17 al 18 de julio del 2015. Duración: 20 horas.

Firma: Dr. Víctor Manuel Mendoza Núñez Director de la FES-Z

Curso impartido por: Dr. Mario Rodriguez León. Jefe de la carrera Médico Cirujano FES-Z UNAM

Jose Ponce Coria has succesfully completed "Introduction to Dental Medicine" a 7 week online n... more Jose Ponce Coria has succesfully completed "Introduction to Dental Medicine"

a 7 week online non-credit course authorized by University of Pennsylvania and offered
through Coursera

course imparted by:

Uri Hangorsky, DDS, MS, Thomas Sollecito, DMD, Eric Stoopler, DMD,

University of Pennsylvania School of Dental Medicine

Jose Ponce Coria has succesfully completed "Introductory Human Physiology" a 10 week online non-c... more Jose Ponce Coria has succesfully completed "Introductory Human Physiology" a 10 week online non-credit course authorized by Duke University and offered through Coursera.

Course imparted by:

Jennifer Carbrey, Ph.D. Assistant Research Professor Cell Biology Department School of Medicine Duke University

Emma R. Jakoi, Ph.D. Associate Research Professor
Cell Biology Department School of Medicine Duke University

an online non-credit course authorized by Duke University and offered through Coursera

Verify at coursera.org/verify/G2VH4E58UDNL
Coursera has confirmed the identity of this individual and
their participation in the course.

José Ponce Coria has succesfully completed " Genes and the Human Condition (From Behaviour to Bio... more José Ponce Coria has succesfully completed " Genes and the Human Condition (From Behaviour to Biothechnology)" a 10 week online non-credit course authorized by University of Maryland and offered through Coursera.

Course imparted by:

Distinguished Professor Raymond J St. Leger, PhD from the Department of Entomology University of Maryland

Tammatha O´Brien, PhD
Department of Entomology
University of Maryland

an online non-credit course authorized by University of Maryland, College Park and offered through Coursera

Verify at coursera.org/verify/K67MBMAXHPW3
Coursera has confirmed the identity of this individual and
their participation in the course

Jose Ponce Coria has succesfully completed with distinction Bacteria and Chronic Infections cou... more Jose Ponce Coria has succesfully completed with distinction
Bacteria and Chronic Infections

course imparted by:

Professor Thomas Bjarnsholt Costerton Biofilm Center
University of Copenhagen

a 6 week online non-credit course authorized by University of Copenhagen and offered through Coursera

Jose Ponce Coria has succesfully completed The addicted brain course imparted by Professor M... more Jose Ponce Coria has succesfully completed

The addicted brain

course imparted by

Professor Michael Kuhar, PhD Yerkes/Emory Pharmacology and Neuroscience Emory University

an online non-credit course authorized by Emory University and offered through Coursera

Verify at coursera.org/verify/GNFMGV5UY96M
Coursera has confirmed the identity of this individual and
their participation in the course.

La Universidad La Salle Nezahualcoyotl otorga la constancia a José Ponce Coria por su participa... more La Universidad La Salle Nezahualcoyotl otorga la constancia a José Ponce Coria

por su participación en el curso presencial:

"Impartición de cursos de formación de capital humano de manera presencial grupal" Con una duración de 30 h

Constancia firmada por el rector Mtro. Raúl Valadez García

Reconocimiento a José Ponce Coria por el apoyo brindado al impartir la teoría y seminario de Morf... more Reconocimiento a José Ponce Coria por el apoyo brindado al impartir la teoría y seminario de Morfofisiología en el módulo "Sistema nervioso y órganos de los sentidos", del 24 de agosto al 25 de septiembre del 2015, a los alumnos del grupo 1303 de la carrera de Médico Cirujano.

Graduate Student Travel Award by the American Physiological Society-Epithelial Transport Group

La Comisión Coordinadora de Institutos Nacionales de Salud y Hospitales de Alta Especialidad otor... more La Comisión Coordinadora de Institutos Nacionales de Salud y Hospitales de Alta Especialidad otorga el TERCER PREMIO EN EL AREA DE INVESTIGACION BIOMEDICA

a los investigadores

Pedro San Cristobal, José Ponce-Coria, Norma Vázquez y Gerardo Gamba

Second best work in the biomedical research field, award granted by the MEXICAN MINISTRY OF HEALTH to:

José Ponce-Coria, Pedro San Cristobal, Norma Vázquez y Gerardo Gamba

La Comisión Coordinadora de Institutos Nacionales de Salud y Hospitales de Alta Especialidad otor... more La Comisión Coordinadora de Institutos Nacionales de Salud y Hospitales de Alta Especialidad otorga el SEGUNDO PREMIO EN EL AREA DE INVESTIGACION BIOMEDICA

a los investigadores

José Ponce-Coria, Pedro San Cristobal, Norma Vázquez y Gerardo Gamba

Second best work in the biomedical research field, award granted by the MEXICAN MINISTRY OF HEALTH to:

José Ponce-Coria, Pedro San Cristobal, Norma Vázquez y Gerardo Gamba

José Ponce Coria Coordinador Académico en el Seminario de Investigación en la FES Zaragoza Fecha... more José Ponce Coria Coordinador Académico en el Seminario de Investigación en la FES Zaragoza

Fecha de realización: 9 de septiembre 2015

Nombramiento a José Ponce Coria como Presidente del IV Encuentro académico, cultural y deportivo ... more Nombramiento a José Ponce Coria como Presidente del IV Encuentro académico, cultural y deportivo de la carrera de Médico Cirujano en la Facultad de Estudios Superiores Zaragoza. Universidad Nacional Autónoma de México

José Ponce Coria

por su participación como PROFESOR TITULAR del curso:

Nociones Generales de la Medicina de Precisión

organizado por la carrera de Medico Cirujando del 22 de junio al 30 de julio, con 22 horas y media de duración.

Firma: Dr. Víctor Manuel Mendoza Núñez Director de la FES-Z

Curso impartido por:

PhD. José Ponce-Coria. Profesor titular asociado C de tiempo completo - Carrera de Médico Cirujano - FES-Z UNAM

C.D. Natalia Arreguín Lobera - Profesor de asignatura "A" carrera de Médico Cirujano - FES-Z UNAM

José Ponce Coria

por haber impartido el curso:

"Principios de Genética"

llevado a cabo del 24 de noviembre al 5 de diciembre del 2014. Duración: 20 horas.

Firma: Dr. Víctor Manuel Mendoza Núñez Director de la FES-Z