PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Light Signal Transduction”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 703 records · Page 39Linked to original sources

Temperature synchronization of the Drosophila circadian clock.

BACKGROUND: Circadian clocks are synchronized by both light:dark cycles and by temperature fluctuations. Although it has long been known that temperature cycles can robustly entrain Drosophila locomotor rhythms, nothing is known about the molecular mechanisms involved. RESULTS: We show here that temperature cycles induce synchronized behavioral rhythms and oscillations of the clock proteins PERIOD and TIMELESS in constant light, a situation that normally leads to molecular and behavioral arrhythmicity. We show that expression of the Drosophila clock gene period can be entrained by temperature cycles in cultured body parts and isolated brains. Further, we show that the phospholipase C encoded by the norpA gene contributes to thermal entrainment, suggesting that a receptor-coupled transduction cascade signals temperature changes to the circadian clock. We initiated the further genetic dissection of temperature-entrainment and isolated the novel Drosophila mutation nocte, which is defective in molecular and behavioral entrainment by temperature cycles but synchronizes normally to light:dark cycles. CONCLUSIONS: We conclude that temperature synchronization of the circadian clock is a tissue-autonomous process that is able to override the arrhythmia-inducing effects of constant light. Our data suggest that it involves a cell-autonomous signal-transduction cascade from a thermal receptor to the circadian clock. This process includes the function of phospholipase C and the product specified by the novel mutation nocte.

Animals↗

Light-driven translocation of signaling proteins in vertebrate photoreceptors.

The dynamic localization of proteins within cells is often determined by environmental stimuli. In retinal photoreceptors, light exposure results in the massive translocation of three key signal transduction proteins, transducin, arrestin and recoverin, into and out of the outer segment compartment where phototransduction takes place. This phenomenon has rapidly taken the center stage of photoreceptor cell biology, thanks to the introduction of new quantitative and transgenic approaches. Here, we discuss evidence that intracellular protein translocation contributes to adaptation of photoreceptors to diurnal changes in ambient light intensity and summarize the current debate on whether it is driven by diffusion or molecular motors.

Animals↗

Characterization of retinoic acid neuromodulation in the carp retina.

Visual sensation in vertebrates starts with the isomerization of 11-cis retinaldehyde into all-trans retinaldehyde. Aldehyde dehydrogenases, present in the pigment epithelium and some retinal cells, convert all-trans retinaldehyde into all-trans retinoic acid (at-RA). Evidence in the retina and the hippocampus has accumulated, showing that at-RA, besides being a morphogenetic factor, also acts as a neuromodulator. In mature retina, at-RA affects visual processing by acting on gap junctional conductances and the synaptic transfer between photoreceptors and horizontal cells. We present evidence supporting a neuromodulatory role of at-RA in the carp retina. High performance liquid chromatography (HPLC) measurements and an RA bioassay indicate a light dependency of at-RA formation, which can explain the observed effects of at-RA on spinule formation at horizontal cell dendrites in this retina. Furthermore, inhibiting endogenous metabolism and catabolism of at-RA affects formation and persistence of spinules in a way, supporting a direct involvement of at-RA in this light-dependent mechanism of synaptic plasticity. The action of at-RA, however, seems independent of the dopaminergic system, known for its light-signaling role in the retina, because at-RA effects on spinule formation persisted in retina depleted of dopaminergic neurons or in the presence of haloperidol. Together, these data indicate that at-RA acts effectively as a direct neuromodulator in carp retina, transmitting information about ambient light conditions to the neuronal retina.

Animals↗

Length-dependent modulation of myosin phosphorylation and contractile force in coronary arterial smooth muscle.

Phosphorylation of the 20,000 dalton myosin light chain (LC) is a central regulatory mechanism of smooth muscle contraction. Our previous findings on airway smooth muscle have led us to hypothesize that length-dependent and length-independent modulation of myosin phosphorylation coexist in smooth muscle. In this study, we tested the general applicability of this hypothesis by investigating the length dependences of myosin phosphorylation and contractile force in bovine coronary arterial smooth muscle. Comparison of the time courses of myosin phosphorylation at optimal (Lo) and preshortened lengths indicated that the initial peak myosin phosphorylation induced by K(+)-depolarization, histamine, and endothelin were all length dependent. Additional experiments focusing on the length dependence of steady-state myosin phosphorylation revealed that the length dependence of K(+)-depolarization-induced steady-state myosin phosphorylation (0.13 mol P(i)/mol LC/Lo) was significant, but smaller than that found in airway smooth muscle. In contrast, the length dependence of endothelin-induced steady-state myosin phosphorylation (0.03 mol P(i)/mol LC/Lo) was insignificant. The different length dependences of depolarization- and endothelin-induced myosin phosphorylation were found to correlate with different length-force relations. The length-force relationships in K+-depolarized and endothelin-activated tissues remained different even when the force was normalized by the maximum value at Lo. Variable length-force relations have been reported but the biochemical basis is not understood. Results from this study suggest that length-dependent modulation of myosin phosphorylation may be an important determinant of length-force relationship in smooth muscle.

Animals↗

On bipolar cells: following in the footsteps of phototransduction.

The electrical signals resulting from phototransduction are decomposed by bipolar cells and then encoded into spike trains by ganglion cells. The signal decomposition by bipolar cells includes formation of ON and OFF pathways and separation of tonic and phasic signals. The decomposition is accomplished by post-synaptic receptors in the ON and OFF bipolar cells. This chapter focuses on these phenomena in ON bipolar cells and the role of metabotropic glutamate receptors in these processes.

Animals↗

The amplitudes of unit events in Limulus photoreceptors are modulated from an input that resembles the overall response.

Light adaptation is a gain-control process that endows photoreceptors with large dynamic range. In invertebrates, this process appears to be mediated by a negative feedback that sets the amplitude of the isolated photon responses (bumps) by modulating an enzyme's rate of catalysis. This paper reports measurements of the feedback dynamics of Limulus from the responses to small modulations in light intensity. The responses show a noise that apparently arises from the random arrival of photons. We use a dynamic noise-analysis technique to extract the cell's frequency-response transfer function for bump amplitude. Its ratio to the transfer function for the summed response of the cell has a simple form at low frequencies. This indicates that the origin of the feedback responsible for the adaptation is at a stage temporally close to the final conductance response. Moreover, the form of the transfer function suggests feedback by a chemical agent which is removed by a single enzymatic-like stage at low light intensity and by several such stages in parallel but with a spread of time constants at high intensity.

Adaptation, Ocular↗

[What do we know about the molecular mechanism of visual excitation?].

The mechanism of transduction of the light stimulus into an electrical response signal is described for visual cells of vertebrates and invertebrates. Absorption of a photon by a rhodopsin molecule in the photosensory membrane of the visual cell leads to a delayed, relatively large single-photon-evoked response, the elementary excitatory response. The rhodopsin molecule starts an enzyme cascade via a G-protein. This leads to a considerably amplified decrease (vertebrates), or increase (invertebrates) of a large number of intracellular messenger molecules. Binding of these messenger molecules causes the opening of the sodium-preferring ion channels in the plasma membrane. Our present knowledge of the molecular mechanisms involved is described.

Animals↗

Adenosine diphosphate moiety does not participate in structural changes for the signaling state in the sensor of blue-light using FAD domain of AppA.

A sensor of blue light using FAD (BLUF) protein is a flavin adenine dinucleotide (FAD) based new class blue-light sensory flavoprotein. The BLUF domain of AppA was reconstituted in vitro from apoprotein and flavin adenine dinucleotide, flavin adenine mononucleotide or riboflavin. The light-induced FTIR spectra of the domain reconstituted from various flavins and the 13C-labeled apoprotein showed that identical light-induced structural changes occur in both the flavin chromophore and protein for the signaling state in all of the reconstituted holoproteins. The results showed that an adenosine 5'-dinucleotide moiety is not required for signaling-state formation in a BLUF domain.

Adenosine Diphosphate↗

Myosin light chain kinase A is activated by cGMP-dependent and cGMP-independent pathways.

Stimulation of Dictyostelium cells with the chemoattractant cAMP results in transient phosphorylation of the myosin regulatory light chain (RLC). We show that myosin light chain kinase A (MLCK-A) is responsible for RLC phosphorylation during chemotaxis, and that MLCK-A itself is transiently phosphorylated on threonine-166, dramatically increasing its catalytic activity. MLCK-A activation during chemotaxis is highly responsive to cellular cGMP levels and the cGMP-binding protein GbpC. MLCK-A- cells have a partial cytokinesis defect, and do not phosphorylate RLC in response to concanavalin A (conA), but cells lacking cGMP or GbpC divide normally and phosphorylate in response to conA. Thus MLCK-A is activated by a cGMP/GbpC-independent mechanism activated during cytokinesis or by conA, and a cGMP/GbpC-dependent pathway during chemotaxis.

Animals↗

The autonomous pathway: epigenetic and post-transcriptional gene regulation in the control of Arabidopsis flowering time.

Mechanisms that mediate the control of flowering time have been accessed through a molecular genetic approach in Arabidopsis. Flowering is regulated by different pathways and, in the past year, all of the known components of the so-called autonomous pathway have been identified. The autonomous pathway comprises a combination of factors involved in RNA processing and epigenetic regulation that downregulate the floral repressor, FLOWERING LOCUS C (FLC). However, components of the autonomous pathway are more widely conserved in plant species other than Arabidopsis than is FLC. Therefore, the broadest lessons we learn from dissecting the function of the autonomous pathway may be in revealing how precision in regulated gene expression is delivered.

AGAMOUS Protein, Arabidopsis↗

Light-induced GTPase activity and GTP[gamma S] binding in squid retinal photoreceptors.

Illumination greatly increases the GTPase activity in homogenates of squid (Loligo) whole retinas or rhabdomeric membranes. Adenylylimidodiphosphate inhibits the light-insensitive (but not the light-sensitive) GTPase activity in these homogenates. Illumination also greatly increases the binding of GTP[gamma S] to the rhabdomeric membranes. This binding at saturating illuminations indicates that there are approximately 10-100 times more rhodopsin molecules than G-protein molecules in squid photoreceptors. Each light-activated rhodopsin molecule activates about 10 G-protein molecules which might provide amplification for the first stage of the phototransduction cascade.

Adenylyl Imidodiphosphate↗

Multilevel regulation of the circadian clock.

Living organisms adapt to light-dark rhythmicity using a complex programme based on internal clocks. These circadian clocks, which are regulated by the environment, direct various physiological functions. As the molecular mechanisms that govern clock function are unravelled, we are starting to appreciate simple patterns as well as exquisite layers of regulation.

Animals↗

Inflammation and the IKK beta/I kappa B/NF-kappa B axis in obesity- and diet-induced insulin resistance.

Antidiabetic effects associated with salicylates have been known for years, although the underlying mechanisms were not understood. We have been reinvestigating these effects in the light of recent discoveries in the areas of signal transduction and insulin resistance. Our findings showed that signaling pathways leading to I kappa B kinase beta (IKK beta) and NF-kappa B are activated in insulin-responsive tissues of obese and high-fat-fed animals. Since activation correlates with the development of insulin resistance, we asked whether signaling through this might be involved in the pathogenesis of insulin resistance. Heterozygous gene deletion (Ikk beta+/-) or salicylates, working as IKK beta inhibitors, improved insulin sensitivity in insulin-resistant rodent models. Furthermore, high doses of salicylates (aspirin or salicylate) improved insulin sensitivity in patients with type II diabetes. Our studies implicate an inflammatory process in the pathogenesis of insulin resistance in obesity and type II diabetes mellitus and identify the IKK beta/NF-kappa B pathway as a molecular mediator of insulin resistance and pharmacological target for insulin sensitization.

Animals↗