H. Pasantes‐Morales

Instituto Nacional de Cardiología

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Julio Morán

Universidad Nacional Autónoma de México

Roberto Sánchez‐Olea

Autonomous University of San Luis Potosí

O. Quesada

Universidad Nacional Autónoma de México

P. Mandel

Université Libre de Bruxelles

J Klethi

Centre National de la Recherche Scientifique

Ana María López‐Colomé

Universidad Nacional Autónoma de México

Rocı́o Salceda

Universidad Nacional Autónoma de México

Sandra Morales‐Mulia

Weatherford College

Arne Schousboe

University of Copenhagen

Carlos Cruz

Escola Universitária Vasco da Gama

Cooperative Institutions

Universidad Nacional Autónoma de México

Instituto Nacional de Cardiología

Pediatric Nephrology of Alabama

Catholic University of Korea

Kyoto University

Center for Research and Advanced Studies of the National Polytechnic Institute

University of Tsukuba

Hirosaki University

Inserm

Centre National de la Recherche Scientifique

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Are Membrane Tyrosine Kinase Receptors Involved in Osmotransduction?

Springer eBooks (2006)

H. Pasantes‐Morales Ruth Lezama Rodrigo Franco

Cell surface receptor

Second messenger system

10.1007/0-387-23752-6_27

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Citations (0)

Taurine binding to membranes from rat brain regions

Journal of Neuroscience Research (1981)

Ana María López‐Colomé H. Pasantes‐Morales

Abstract [ 3 H]‐taurine binding to membranes from different regions from rat brain was studied. Binding to membranes from cerebral cortex and its subcellular fractions, hypothalamus, olfactory bulb and cerebellum was measured. Binding to membranes from dorsal root ganglion was also determined. Na + ‐dependent taurine binding was consistently observed in all the membranes except those from dorsal root ganglion. A K D = 4.06 μM was obtained for binding to membranes from cerebral cortex. Na + ‐dependent taurine binding was displaced by 20 μM strychnine or bicuculline. Na + ‐independent taurine binding with properties corresponding to a postsynaptic interaction could not be detected in any of the regions studied. The possibility of Na + ‐dependent taurine binding, representing binding to uptake sites or to postsynaptic receptors for GABA and glycine, is discussed.

Dorsal root ganglion

10.1002/jnr.490060405

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Evidence for two mechanisms of amino acid osmolyte release from hippocampal slices

Pflügers Archiv - European Journal of Physiology (2001)

Rodrigo Franco M. Torres-M x E rquez H. Pasantes‐Morales

Chelerythrine

Niflumic acid

Wortmannin

10.1007/s004240100604

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Citations (57)

Effect of X537A on the release of amino acids in retina

Biochemical and Biophysical Research Communications (1974)

H. Pasantes‐Morales Rocı́o Salceda A. Gómez-Puyou

10.1016/s0006-291x(74)80494-8

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Citations (16)

Subject Index Vol. 86, 2000

The Nephron journals/Nephron journals (2000)

Yoshihiro Matsumoto Izumi Amano Eun Jung Jun Young Ok Kim Ayşegül Zumrutdal

10.1159/000045876

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Protective effect of taurine and zinc on peroxidation‐induced damage in photoreceptor outer segments

Journal of Neuroscience Research (1984)

H. Pasantes‐Morales Carlos Cruz

Abstract Exposure of isolated frog rod outer segments (ROS) to ferrous sulfate in a Krebsbicarbonate medium causes a time‐dependent disruption of the membrane organization of the discs. Ferrous sulfate also causes ROS swelling and aggregation. Addition of taurine (5–20 mM) and zinc sulfate (250 μM) to the incubation medium markedly protected ROS from the disrupting effect of ferrous sulfate. Of other amino acids tested, only β‐alanine had a protective effect on ROS structure. Ferrous sulfate caused an increase in lipid peroxidation, measured by malonaldehyde formation. The protective effect of taurine and zinc is not accompanied by a reduction of lipid peroxidation. Water accumulation occurs as a consequence of the peroxidative action of ferrous sulfate, and this effect was counteracted by taurine and zinc. Ferrous sulfate did not cause damage to ROS structure when incubation was carried out in sucrose‐HEPES. Sodium, chloride, and bicarbonate ions caused ferrous sulfate to disrupt ROS structure. It is concluded that taurine and zinc protect ROS membranes from ion and/or water entry occurring as a consequence of membrane lipid peroxidation.

Bicarbonate

10.1002/jnr.490110310

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Citations (86)

Distribution of taurine and other free amino acids in the visual pathway of the crayfish Procambarus clarkii

Comparative Biochemistry and Physiology Part B Comparative Biochemistry (1992)

Arturo Picones R.L. Escalera H. Pasantes‐Morales

Procambarus clarkii

Eyestalk

Medulla

10.1016/0305-0491(92)90350-z

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Citations (3)

Volume changes and whole cell membrane currents activated during gradual osmolarity decrease in C6 glioma cells: contribution of two types of K⁺ channels

AJP Cell Physiology (2004)

Benito Ordaz Luis Vaca Rodrigo Franco H. Pasantes‐Morales

Volume changes and whole cell ionic currents activated by gradual osmolarity reductions (GOR) of 1.8 mosM/min were characterized in C6 glioma cells. Cells swell less in GOR than after sudden osmolarity reductions (SOR), the extent of swelling being partly Ca 2+ dependent. In nominally Ca 2+ -free conditions, GOR activated predominantly whole cell outward currents. Cells depolarized from the initial −79 mV to a steady state of −54 mV reached at 18% osmolarity reduction [hyposmolarity of −18% (H-18%)]. Recordings of Cl − and K + currents showed activation at H-3% of an outwardly rectifying Cl − current, with conductance of 1.6 nS, sensitive to niflumic acid and 5-nitro-2-(3-phenylpropylamino)benzoic acid, followed at H-18% by an outwardly rectifying K + current with conductance of 4.1 nS, inhibited by clofilium but insensitive to the typical K + channel blockers. With 200 nM Ca 2+ in the patch pipette, whole cell currents activated at H-3% and at H-13% cells depolarized from −77 to −63 mV. A K + current activated at H-1%, showing a rapid increase in conductance, suppressed by charybdotoxin and insensitive to clofilium. These results show the operation of two different K + channels in response to GOR in the same cell type, activated by Ca 2+ and osmolarity and with different osmolarity activation thresholds. Taurine and glutamate efflux, monitored by labeled tracers, showed delayed osmolarity thresholds of H-39 and H-33%, respectively. This observation clearly separates the Cl − and amino acid osmosensitive pathways. The delayed amino acid efflux may contribute to counteract swelling at more stringent osmolarity reductions.

Osmotic concentration

Niflumic acid

Reversal potential

Chloride channel

Efflux

Pipette

10.1152/ajpcell.00198.2003

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Citations (30)

Higher susceptibility of taurine-deficient rats to seizures induced by 4-aminopyridine

Neuropharmacology (1987)

H. Pasantes‐Morales M. E. Arzate O. Quesada Ryan J. Huxtable

4-Aminopyridine

Convulsion

Tonic (physiology)

10.1016/0028-3908(87)90123-7

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Citations (22)

Taurine release associated to volume regulation in rabbit lymphocytes

Journal of Cellular Biochemistry (1991)

Jesse Garcia Roberto Sánchez‐Olea H. Pasantes‐Morales

Rabbit lymphocytes exposed to hyposmotic media first swell and then recover their initial volume within 6 min. During volume recovery, free amino acids (FAA) decrease from 451.1 to 208 nmoles/mg protein. Taurine was the dominating FAA, accounting for 70% of the FAA pool. The time course of 3H-taurine release induced by hyposmolarity followed that of volume recovery. Efflux of 3H-taurine in an 8 min period was 17.8% (of total labeled taurine accumulated during loading) in an isosmotic medium. Reducing osmolarity to 0.87, 0.75, 0.62, and 0.5 increased this release to 24.8%, 38.1%, 56.4% and 70.9%, respectively. The volume-sensitive release of 3H-taurine was unaffected by omission of external Na+ or Ca++ and was reduced by 23% in the absence of Cl-. It was unaffected by agents disrupting the cytoskeleton or by tetraethylammonium, barium, quinidine, and gadolinium, but was 26% reduced by DIDS. Taurine release was inhibited at 4 degrees C, but was unchanged at 15 degrees C or 25 degrees C. An involvement of FAA, particularly taurine, in lymphocyte volume regulation is suggested.

DIDS

Osmotic concentration

10.1002/jcb.240450212

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Citations (27)