3 edition of Mammalian TRP channels as molecular targets found in the catalog.
|Statement||[editors, Derek J. Chadwick and Jamie A. Goode].|
|Series||Novartis Foundation symposium -- 258|
|Contributions||Chadwick, Derek., Goode, Jamie., Novartis Foundation.|
|The Physical Object|
|Pagination||ix, 275p. :|
|Number of Pages||275|
Mammalian transient receptor potential (TRP) channels mediate Ca2+ flux and voltage changes across membranes in response to environmental and cellular signals. At . Since the identification of the first mammalian TRP channels in the s, these entities have been addressed as potential targets for drugs, and Kaneko and Szallasi review the current status of TRP channels from a clinical perspective. Despite accumulating evidence to implicate a number of TRP channels in a wide range of diseases, only 4 of.
seven original articles summarizing the current state-of-the-art research on TRP channels, with a focus on TRP channel activation, their physiological and pathophysiological function, and their roles as pharmacological targets for future therapeutic options. Returning to the roots of the mammalian TRP channel discovery, TRPC1 may preferentially. TRPC channels. The classic TRP channel family comprises seven different genes with proteins showing the highest sequence similarity to the prototypic Drosophila TRP [8, 12, 19].The mammalian channel proteins are involved in receptor-regulated calcium entry .Receptor activation by hormones, neurotransmitter and in Drosophila light results in the phospholipase C-mediated .
TRP channels play a key role in sensory physiology and have been the focus of intensive investigation in recent years. The proposed book will be a comprehensive, detailed overview of the ways in which TRP channels are involved in a wide variety of sensory modalities. Authors will explore the involvement of TRP channels in photo transduction (sight), chemotransduction (taste and odor. Choosing among many possible topics in these broad areas was a daunting task Medical books Mammalian Trp Channels As Molecular Targets. Somerset New Jersey USA: John Wiley & Sons Inc pages. New in publishers shrinkwrap. Hard Cover - Pictorial Cover. New. 8vo - .
A select bibliography of chemistry, 1492-1902. Second supplement
eighteenth century village
Natural gas supplies and prospects in the community.
God and phenomenal consciousness
Sport for the unemployed
Pneumatic conveying of bulk materials
On regular variation and its application to the weak convergence of sample extremes
bibliography of newspapers and periodicals published in California in 1855
Prelude to history
Nonprofit sector in Pakistan
Victorian crisis of faith
It covers the structure, function and regulation of mammalian TRP channels and of mechanisms of signal transduction. The discussions highlight future studies towards a better understanding of the role of TRP channels in normal cellular physiology, the involvement of TRP channels in disease states, and their potential use as molecular targets.
It covers the structure, function and regulation of mammalian TRP channels and mechanisms of signal transduction. The discussions indicate research that would improve understanding of the role of TRP channels in normal cellular physiology, the involvement of TRP channels in disease states and their potential use as molecular targets for novel.
Get this from a library. Mammalian TRP channels as molecular targets. [Derek Chadwick; Jamie Goode;] -- Brings together contributions from key investigators in the area of TRP channels.
It covers the structure, function and regulation of mammalian TRP channels and of mechanisms of. Symposium on Mammalian TRP Channels as Molecular Targets ( Novartis Foundation).
Mammalian TRP channels as molecular targets. Chichester, UK ; Hoboken, NJ: John Wiley & Sons, (DLC) (OCoLC) Material Type: Conference publication, Document, Internet resource: Document Type: Internet Resource, Computer File.
This book offers a unique clinical approach by covering compounds that target TRP channels in pre-clinical and clinical phases, also offering a discussion of TRP channels as biomarkers. An entire section is devoted to the novel and innovative uses of these channels across a variety of diseases, offering strategies that can be used to overcome.
The large Trp gene family encodes transient receptor potential (TRP) proteins that form novel cation-selective ion channels. In mammals, 28 Trp channel genes have been identified. TRP proteins exhibit diverse permeation and gating properties and are involved in a plethora of physiologic functions with a strong impact on cellular sensing and signaling pathways.
The discovery of such agents and the identification of their molecular target resulted from the investigation of unexpected actions of known pharmacological agents. Ca 2+ influx through receptor‐operated channels in electrically non‐excitable cells such as leukocytes is also functionally important, but to date the channels involved have not.
Abnormal Ca2+ channel physiology, expression levels, and hypersensitivity to heat have been implicated in several pain states following treatment with chemotherapeutic agents. As members of the Ca2+ permeable transient receptor potential (TRP), five of the channels (TRPV and TRPM2) are activated by different heat temperatures, and two of the channels (TRPA1 and TRPM8) are activated by cold.
(1) Background: Human transient receptor potential (TRP) channels constitute a large family of ion-conducting membrane proteins that allow the sensation of environmental cues.
As the dysfunction of TRP channels contributes to the pathogenesis of many widespread diseases, including cardiac disorders, these proteins also represent important pharmacological targets. In: Chadwick DJ, Goode J (eds) Mammalian TRP channels as molecular targets: Novartis Foundation Symposium, vol Wiley, Chichester, UK, pp 44–62 Google Scholar Zhu MH, Chae M, Kim HJ et al () Desensitization of canonical transient receptor potential channel 5 by protein kinase C.
Am J Physiol C–C Google Scholar. In this fast moving field the main goal of this volume is to provide up-to-date information on the molecular and functional properties and pharmacology of mammalian TRP channels.
Leading experts in the field will describe properties of a single TRP protein/channel or portray more general principles of TRP function and important pathological. Eukaryote voltage-gated Ca 2+ channels of the Ca V 2 channel family are hetero-oligomers formed by the pore-forming Ca V α1 protein assembled with auxiliary Ca V α2δ and Ca V β subunits.
Ca V β subunits are formed by a Src homology 3 (SH3) domain and a guanylate kinase (GK) domain connected through a HOOK domain. The GK domain binds a conserved cytoplasmic region of the pore-forming. The mammalian members of TRP superfamily are (except for two members) Ca2+-permeable non-selective cation channels which are constitutively active or gated by a multitude of physicochemical stimuli such as receptor stimulation, phospholipids, oxidants, pheromones, cell volume change/shear stress, exogenous compounds affecting sensations, and.
Mammalian TRP Channels as Molecular Targets – Novartis Foundation Symposium No. Wiley: Europe, pp. 1– Putney JW (). Physiological mechanisms of TRPC activation. Pflügers Arch 29– Qian F, Noben-Trauth K (). Cellular and molecular function of mucolipins (TRPML) and polycystin 2 (TRPP2).
Transient receptor potential (TRP) channels are a group of membrane proteins involved in the transduction of a plethora of chemical and physical stimuli. These channels modulate ion entry, mediating a variety of neural signaling processes implicated in the sensation of temperature, pressure, and pH, as well as smell, taste, vision, and pain perception.
Many diseases involve TRP channel. Transient Receptor Potential (TRP) proteins constitute a family of cation channels with very diverse permeation and gating properties. Likewise they have a very diverse role in mammalian physiology ranging from sensory nerve endings, the cardiac muscle to immune cells.
Increasing evidence has implic. Mammalian transient receptor potential (TRP) cation channels. Volume I / In this fast moving field the main goal of this volume is to provide up-to-date information on the molecular and functional properties and pharmacology of mammalian TRP channels.
TRP Channels as Therapeutic Targets: From Basic Science to Clinical Use is authored by experts across academia and industry, providing readers with a complete picture of the therapeutic potential and challenges associated with using TRP channels as drug targets.
This book offers a unique clinical approach by covering compounds that target TRP channels in pre-clinical and clinical phases, also. Mammalian TRP channels as molecular targets / [edited by Derek J.
Chadwick and Jamie A. Goode]. Almost 25 years ago, the first mammalian transient receptor potential (TRP) channel, now named TRPC1, was cloned and published (reviewed in ).Although the exact function of TRPC1 is still elusive , TRP channels now represent an extended family of 28 members, fulfilling multiple roles in the living organism .Their identified functions include control of body temperature, transmitter.
In this fast moving field the main goal of this volume is to provide up-to-date information on the molecular and functional properties and pharmacology of mammalian TRP channels. Leading experts in the field will describe properties of a single TRP protein/channel or portray more general principles.Title:TRP Channels as Therapeutic Targets in Kidney Disease and Hypertension VOLUME: 13 ISSUE: 3 Author(s):Paolo Mene, Giorgio Punzo and Nicola Pirozzi Affiliation:Dipartimento di Medicina Clinica e Molecolare, Cattedra di Nefrologia, Azienda Ospedaliera Sant'Andrea, Via di GrottarossaRome, Italy.
Keywords:TRP channels, store-operated Ca2+ channels, receptor-operated Ca2.In this fast moving field the main goal of this volume is to provide up-to-date information on the molecular and functional properties and pharmacology of mammalian TRP channels.
Leading experts in the field describe properties of a single TRP protein/channel or portray more general principles of.