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Your search keyword '"Pelech, Steven L."' showing total 171 results
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171 results on '"Pelech, Steven L."'

4. Networking with mitogen-activated protein kinases

Author

Pelech, Steven L., Charest, David L., Mordret, Guy P., Siow, Yaw Loong, Palaty, Chrystal, Campbell, Donna, Charlton, Lorin, Samiei, Mitra, Sanghera, Jasbinder S., Dhalla, Naranjan S., editor, Khandelwal, R. L., editor, and Wang, J. H., editor

Published
1993
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9. In vivo regulation of protein-serine kinases by insulin in skeletal muscle of fructose-hypertensive rats

Author

Bhanot, Sanjay, Salh, Baljinder S., Verma, Subodh, McNeill, John H., and Pelech, Steven L.

Subjects
Hypertension -- Physiological aspects, Insulin -- Physiological aspects, Muscles -- Physiological aspects, Protein kinases -- Physiological aspects, Rats -- Physiological aspects, Serine -- Physiological aspects, Threonine -- Physiological aspects, Biological sciences
Abstract

The effects of tail-vein insulin injection on the regulation of protein-serine kinases in hindlimb skeletal muscle were studied in hyperinsulinemic hypertensive fructose-fed (FF) rats that had been fasted overnight. Basal protein kinase B (PKB) activity increased about twofold in FF rats and was not further stimulated by insulin. Findings showed that the phosphatidylinositol 3-kinase (PI3K) -> PKB -> S6 kinase (S6K) pathway was upregulated under basal conditions. Also, insulin stimulation of PI3K and S6K activities was enhanced.

Published
1999

11. Amyotrophic lateral sclerosis: the involvement of intracellular Ca2+ and protein kinase C

Author

Krieger, Charles, Lanius, Ruth A., Pelech, Steven L., and Shaw, Christopher A.

Subjects
Amyotrophic lateral sclerosis -- Physiological aspects, Calcium channels -- Physiological aspects, Protein kinases -- Physiological aspects, Biological sciences, Chemistry, Pharmaceuticals and cosmetics industries
Abstract

The neurodegenerative disease, amyotrophic lateral sclerosis (ALS), is characterized by the selective death of motoneurones and corticospinal tract neurones. Abnormalities in excitatory amino acids and their receptors, as well as disordered function of voltage-dependent [Ca.sup.2+] channels and superoxide dismutase have been reported in ALS patients. Furthermore, the activity of protein kinase C (PKC), a [Ca.sup.2]+, phospholipid-dependent enzyme, is also substantially increased in tissue from ALS patients, suggesting that alterations in intracellular free [Ca.sup.2+] may be central to many of the diverse pathogenic mechanisms potentially responsible for ALS as discussed here by Charles Krieger and colleagues. Increased PKC activity, in turn, may have direct or indirect effects on neuronal viability and influence the pathogenic process in ALS by modifying the phosphorylation of voltage-dependent [Ca.sup.2+] channels, neurotransmitter receptors and structural proteins.

Published
1996

13. The malignant connection: when its molecular 'nervous system' goes awry, a cell can turn cancerous

Author

Pelech, Steven L.

Subjects
Sarcoma -- Research, Carcinogenesis -- Research, Cancer cells -- Research, Oncogenes -- Research, Virus research -- Observations -- Research, Science and technology, Observations, Research
Abstract

The Rous Sarconia Virus, now known to induce malignant tumors in chickens, has proved to be something of a ticket to a Nobel prize. In 1966 an award in physiology [...]

Published
1993

14. Raf-1 and p21v-ras cooperate in the activation of mitogen-activated protein kinase

Author

Williams, Nidhi G., Paradis, Helene, Agarwal, Sadhana, Charest, David L., Pelech, Steven L., and Roberts, Thomas M.

Subjects
Protein kinases -- Physiological aspects, Science and technology
Abstract

Researchers used a bacilovirus/Sf9 insect cell system to discover the regulatory relationships between pp60v-src, p21v-ras, MAP kinase (p44erk1/mapk) and Raf-1. The results indicate that stimulation of p44erk1/mapk by p21v-ras could happen through Raf-1 dependent and Raf-1-independent pathways.

Published
1993

15. Mitogen-activated protein kinases: versatile transducers for cell signaling

Author

Pelech, Steven L. and Sanghera, Jasbinder S.

Subjects
Mitogens -- Physiological aspects, Protein kinases -- Physiological aspects, Cellular signal transduction -- Physiological aspects, Biological sciences, Chemistry
Abstract

Mitogen-activated protein (MAP) kinases are stimulated by growth factors that bind to tyrosine kinases, lymphokines and phosphatidylinositide agonists. This leads to MAP activation of protein kinase C, inhibitors of protein-serine/threonine phosphatases, protein-tyrosine phosphatases and microtubule assembly. MAP kinases serve as common signaling components in distinct transduction pathways which are initiated by numerous stimuli.

Published
1992

17. Supplementary Methods from Insights into the roles of CMK-1 and OGT-1 in interstimulus interval-dependent habituation in Caenorhabditis elegans

Author

Ardiel, Evan L., McDiarmid, Troy A., Timbers, Tiffany A., Lee, Kirsten C. Y., Safaei, Javad, Pelech, Steven L., and Rankin, Catharine H.

Abstract

Habituation is a ubiquitous form of non-associative learning observed as a decrement in responding to repeated stimulation that cannot be explained by sensory adaptation or motor fatigue. One of the defining characteristics of habituation is its sensitivity to the rate at which training stimuli are presented—animals habituate faster in response to more rapid stimulation. The molecular mechanisms underlying this interstimulus interval (ISI)-dependent characteristic of habituation remain unknown. In this article, we use behavioural neurogenetic and bioinformatic analyses in the nematode Caenorhabiditis elegans to identify the first molecules that modulate habituation in an ISI-dependent manner. We show that the Caenorhabditis elegans orthologues of Ca2+/calmodulin-dependent kinases CaMK1/4, CMK-1 and O-linked N-acetylglucosamine (O-GlcNAc) transferase, OGT-1, both function in primary sensory neurons to inhibit habituation at short ISIs and promote it at long ISIs. In addition, both cmk-1 and ogt-1 mutants display a rare mechanosensory hyper-responsive phenotype, i.e. larger mechanosensory responses than wild-type. Overall, our work identifies two conserved genes that function in sensory neurons to modulate habituation in an ISI-dependent manner, providing the first insights into the molecular mechanisms underlying the universally observed phenomenon that habituation has different properties when stimuli are delivered at different rates.

Published
2018
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18. Supplementary Figures from Insights into the roles of CMK-1 and OGT-1 in interstimulus interval-dependent habituation in Caenorhabditis elegans

Author

Ardiel, Evan L., McDiarmid, Troy A., Timbers, Tiffany A., Lee, Kirsten C. Y., Safaei, Javad, Pelech, Steven L., and Rankin, Catharine H.

Abstract

Habituation is a ubiquitous form of non-associative learning observed as a decrement in responding to repeated stimulation that cannot be explained by sensory adaptation or motor fatigue. One of the defining characteristics of habituation is its sensitivity to the rate at which training stimuli are presented—animals habituate faster in response to more rapid stimulation. The molecular mechanisms underlying this interstimulus interval (ISI)-dependent characteristic of habituation remain unknown. In this article, we use behavioural neurogenetic and bioinformatic analyses in the nematode Caenorhabiditis elegans to identify the first molecules that modulate habituation in an ISI-dependent manner. We show that the Caenorhabditis elegans orthologues of Ca2+/calmodulin-dependent kinases CaMK1/4, CMK-1 and O-linked N-acetylglucosamine (O-GlcNAc) transferase, OGT-1, both function in primary sensory neurons to inhibit habituation at short ISIs and promote it at long ISIs. In addition, both cmk-1 and ogt-1 mutants display a rare mechanosensory hyper-responsive phenotype, i.e. larger mechanosensory responses than wild-type. Overall, our work identifies two conserved genes that function in sensory neurons to modulate habituation in an ISI-dependent manner, providing the first insights into the molecular mechanisms underlying the universally observed phenomenon that habituation has different properties when stimuli are delivered at different rates.

Published
2018
Full Text
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