Sensory Transduction

2019 ◽  
Author(s):  
Gordon L. Fain
Keyword(s):  
Ion Channels ◽  
Receptor Cell ◽  
Electrical Response ◽  
Second Messengers ◽  
Sensory Transduction ◽  
Sensory Receptor ◽  
Signal Pathways ◽  
Sense Organs ◽  
Sensory Physiology ◽  
Effector Molecules

Sensory Transduction provides a thorough and easily accessible introduction to the mechanisms that each of the different kinds of sensory receptor cell uses to convert a sensory stimulus into an electrical response. Beginning with an introduction to methods of experimentation, sensory specializations, ion channels, and G-protein cascades, it provides up-to-date reviews of all of the major senses, including touch, hearing, olfaction, taste, photoreception, and the “extra” senses of thermoreception, electroreception, and magnetoreception. By bringing mechanisms of all of the senses together into a coherent treatment, it facilitates comparison of ion channels, metabotropic effector molecules, second messengers, and other components of signal pathways that are common themes in the physiology of the different sense organs. With its many clear illustrations and easily assimilated exposition, it provides an ideal introduction to current research for the professional in neuroscience, as well as a text for an advanced undergraduate or graduate-level course on sensory physiology.

scholarly journals Regulation of mitochondrial pyruvate carboxylation in isolated hepatocytes by acute insulin treatment

1983 ◽  
Vol 214 (2) ◽  
pp. 451-458 ◽  
Author(s):  
A B Chisholm ◽  
E H Allan ◽  
M A Titheradge
Keyword(s):  
Insulin Treatment ◽  
Second Messengers ◽  
Isolated Hepatocytes ◽  
Carboxylase Activity ◽  
Effector Molecules ◽  
Pyruvate Carboxylation ◽  
Isolated Mitochondria ◽  
Glucose Synthesis ◽  
Important Site ◽  
Stimulation Of

The effect of acute insulin treatment of hepatocytes on pyruvate carboxylation in both isolated mitochondria and cells rendered permeable by filipin was examined. Challenging the cells with insulin alone had no effect on either the basal rate of pyruvate carboxylation or gluconeogenesis, although it did suppress the responses to both glucagon and catecholamines. Insulin treatment was unable to antagonize the enhanced rate of pyruvate carboxylation caused by stimulation of the cells with either angiotensin or vasopressin. Neither insulin nor the gluconeogenic hormones altered the total extractable pyruvate carboxylase activity in the isolated mitochondria, suggesting that the effect of hormones at the level of the isolated intact organelle was mediated via alterations in the intramitochondrial concentrations of effector molecules, notably ATP and the [ATP]/[ADP] ratio and substrate availability. The alterations in pyruvate carboxylation correlate well with glucose synthesis in terms of sensitivity to effector molecules, putative second messengers and time of onset of the response, indicating that alterations in the flux through this enzyme are compatible with it being an important site in the control of gluconeogenesis from C3 precursors.

Calcium Signals in Nerve Cells

Physiology ◽  
1991 ◽  
Vol 6 (1) ◽  
pp. 6-10 ◽  
Author(s):  
PG Kostyuk ◽  
AV Tepikin
Keyword(s):  
Endoplasmic Reticulum ◽  
Ion Channels ◽  
Nerve Cell ◽  
Second Messengers ◽  
Cell Activity ◽  
Nerve Cells ◽  
Calcium Signals ◽  
Intracellular Ca ◽  
Ca Ions

Increases in intracellular Ca ions follow each cycle of nerve cell activity. Sources of Ca are voltage- and receptor-operated membrane ion channels and endoplasmic reticulum (ER). Ca release from ER can be triggered by different second messengers, and uptake into the ER can terminate the Ca signal.

Signal-Transduction Pathways that Regulate Smooth Muscle Function II. Receptor-ion channel coupling mechanisms in gastrointestinal smooth muscle

2005 ◽  
Vol 288 (4) ◽  
pp. G598-G602 ◽  
Author(s):  
Hamid I. Akbarali
Keyword(s):  
Signal Transduction ◽  
Smooth Muscle ◽  
Ion Channels ◽  
Intracellular Signaling ◽  
Molecular Mechanisms ◽  
Second Messengers ◽  
Gastrointestinal Smooth Muscle ◽  
Smooth Muscle Function ◽  
Muscle Excitability ◽  
Coupling Mechanisms

Regulation of membrane ion channels by second messengers is an important mechanism by which gastrointestinal smooth muscle excitability is controlled. Receptor-mediated phosphorylation of Ca2+ channels has been known for some time; however, recent findings indicate that these channels may also modulate intracellular signaling. The plasmalemma ion channels may also function as a point of convergence between different receptor types. In this review, the molecular mechanisms that link channel function and signal transduction are discussed. Emerging evidence also indicates altered second-messenger modulation of the Ca2+ channel in the pathophysiology of smooth muscle dysmotility.

Ion channel regulation by G proteins

1995 ◽  
Vol 75 (4) ◽  
pp. 865-885 ◽  
Author(s):  
K. Wickman ◽  
D. E. Clapham
Keyword(s):  
Ion Channels ◽  
Ion Channel ◽  
G Protein ◽  
G Proteins ◽  
Second Messengers ◽  
Channel Activity ◽  
Ion Channel Regulation ◽  
Protein Subunits ◽  
Channel Regulation ◽  
Intracellular Cascades

Ion channels are poised uniquely to initiate, mediate, or regulate such distinct cellular activities as action potential propagation, secretion, and gene transcription. In retrospect, it is not surprising that studies of ion channels have revealed considerable diversities in their primary structures, regulation, and expression. From a functional standpoint, the various mechanisms coopted by cells to regulate channel activity are particularly fascinating. Extracellular ligands, membrane potential, phosphorylation, ions themselves, and diffusible second messengers are all well-established regulators of ion channel activity. Heterotrimeric GTP-binding proteins (G proteins) mediate many of these types of ion channel regulation by stimulating or inhibiting phosphorylation pathways, initiating intracellular cascades leading to elevation of cytosolic Ca2+ or adenosine 3',5'-cyclic monophosphate levels, or by generating various lipid-derived compounds. In some cases, it seems that activated G protein subunits can interact directly with ion channels to elicit regulation. Although there is currently little direct biochemical evidence to support such a mechanism, it is the working hypothesis for the most-studied G protein-regulated ion channels.

scholarly journals The odontoblast as a sensory receptor cell? The expression of TRPV1 (VR-1) channels

2005 ◽  
Vol 68 (4) ◽  
pp. 251-257 ◽  
Author(s):  
Reijiro Okumura ◽  
Kaori Shima ◽  
Takashi Muramatsu ◽  
Kan-ichi Nakagawa ◽  
Masaki Shimono ◽  
...  
Keyword(s):  
Receptor Cell ◽  
Sensory Receptor

Observations on the sensory Physiology and Behaviour of larvae of the cattle tick, Boophilus Microplus (Can.) (Ixodidae).

1953 ◽  
Vol 1 (3) ◽  
pp. 345 ◽  
Author(s):  
PR Wilkinson
Keyword(s):  
Early Morning ◽  
Boophilus Microplus ◽  
Sensory Function ◽  
Cattle Tick ◽  
Sense Organs ◽  
Direct Sunlight ◽  
Sensory Physiology ◽  
Late Afternoon ◽  
Cattle Ticks ◽  
Skin Secretions

In larval cattle ticks the main sense organs which have been recognized are the eyes, Haller's organs, and the palpal organs; the four pairs of sensilla sagittiformia may also have a sensory function. Larvae were allowed to ascend supports simulating grass stalks and were tested for response to vibration, air currents, interrupted illumination, warm and moist objects, and odours from skin secretions of man and cattle. The strongest questing response was to the odours. Larvae which had been exposed to low humidities collected around and imbibed from drops of water. The main stimulus governing ascent of the grass blades appeared to be positive phototaxis to moderate light intensities. Larvae sheltered from direct sunlight. Larvae in the field were found to be more exposed in the early morning, often being at the tops of grass stalks. Measurements of light, air temperature, and humidity indicated that light intensity might govern this movement. This suggests that larval sampling in the pasture should take place in the first half of the morning. In a single series of observations, larvae which had hatched at the base of straws were observed to ascend them in the late afternoon. In a few experiments isolated larvae ascended artificial supports above the reach of a bovine host but groups were always found at heights within reach.

scholarly journals The Ca2+-activated Cl− channel ANO1/TMEM16A regulates primary ciliogenesis

2014 ◽  
Vol 25 (11) ◽  
pp. 1793-1807 ◽  
Author(s):  
Chelsey Chandler Ruppersburg ◽  
H. Criss Hartzell
Keyword(s):  
Ion Channels ◽  
Primary Cilium ◽  
Primary Cilia ◽  
Chloride Transport ◽  
Small Gtpases ◽  
Sensory Transduction ◽  
Anoctamin 1 ◽  
Hairpin Rna ◽  
Cellular Morphogenesis ◽  
Mother Centriole

Many cells possess a single, nonmotile, primary cilium highly enriched in receptors and sensory transduction machinery that plays crucial roles in cellular morphogenesis. Although sensory transduction requires ion channels, relatively little is known about ion channels in the primary cilium (with the exception of TRPP2). Here we show that the Ca2+-activated Cl− channel anoctamin-1 (ANO1/TMEM16A) is located in the primary cilium and that blocking its channel function pharmacologically or knocking it down with short hairpin RNA interferes with ciliogenesis. Before ciliogenesis, the channel becomes organized into a torus-shaped structure (“the nimbus”) enriched in proteins required for ciliogenesis, including the small GTPases Cdc42 and Arl13b and the exocyst complex component Sec6. The nimbus excludes F-actin and coincides with a ring of acetylated microtubules. The nimbus appears to form before, or independent of, apical docking of the mother centriole. Our data support a model in which the nimbus provides a scaffold for staging of ciliary components for assembly very early in ciliogenesis and chloride transport by ANO1/TMEM16A is required for the genesis or maintenance of primary cilia.

scholarly journals Cyclic nucleotide-gated ion channels in sensory transduction

FEBS Letters ◽  
2006 ◽  
Vol 580 (12) ◽  
pp. 2853-2859 ◽  
Author(s):  
Simone Pifferi ◽  
Anna Boccaccio ◽  
Anna Menini
Keyword(s):  
Ion Channels ◽  
Cyclic Nucleotide ◽  
Sensory Transduction ◽  
Gated Ion Channels

scholarly journals Antagonistic regulation of trafficking to Caenorhabditis elegans sensory cilia by a Retinal Degeneration 3 homolog and retromer

2017 ◽  
Vol 115 (3) ◽  
pp. E438-E447 ◽  
Author(s):  
Luis A. Martínez-Velázquez ◽  
Niels Ringstad
Keyword(s):  
Caenorhabditis Elegans ◽  
Retinal Degeneration ◽  
Sensory Neurons ◽  
Secretory Pathway ◽  
Early Stage ◽  
Sensory Modality ◽  
Retinal Dystrophy ◽  
Sensory Transduction ◽  
Sensory Receptor

Sensory neurons often possess cilia with elaborate membrane structures that are adapted to the sensory modality of the host cell. Mechanisms that target sensory transduction proteins to these specialized membrane domains remain poorly understood. Here, we show that a homolog of the human retinal dystrophy gene Retinal Degeneration 3 (RD3) is a Golgi-associated protein required for efficient trafficking of a sensory receptor, the receptor-type guanylate cyclase GCY-9, to cilia in chemosensory neurons of the nematode Caenorhabditis elegans. The trafficking defect caused by mutation of the nematode RD3 homolog is suppressed in vivo by mutation of key components of the retromer complex, which mediates recycling of cargo from endosomes to the Golgi. Our data show that there exists a critical balance in sensory neurons between the rates of anterograde and retrograde trafficking of cargo destined for the sensory cilium and this balance requires molecular specialization at an early stage of the secretory pathway.

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