PubMed Health⌕ Search

PubMed · 7226202

Pineal complex of the clawed toad, Xenopus laevis Daud.: structure and function.

Abstract

The morphological and physiological properties of the pineal complex of Xenopus laevis were investigated in larval, juvenile and adult animals. In a representative majority of adult X. laevis, the frontal organ does not display signs of degeneration. Fully differentiated frontal organs contain photoreceptors typical of the pineal complex of lower vertebrates. By means of the acetylcholinesterase (AChE)-reaction approximately 30 neurons of two different types were demonstrated in the frontal organ. The frontal-organ nerve is composed of approximately 10 myelinated and 40 unmyelinated nerve fibers. The neuropil areas of the frontal organ are generally similar to the corresponding structures of the intracranial epiphysis. The neuronal apparatus of the epiphysis cerebri of X. laevis consists of (i) photoreceptor cells, (ii) approximately 100 AChE-positive neurons, (iii) complex neuropil areas, and (iv) a pineal tract formed by approximately 10 myelinated and approximately 100 unmyelinated nerve fibers. Some of them exhibit granular inclusions indicating that pinealopetal elements may enter the pineal complex of X. laevis via this pathway. The topography of the pineal tract of X. laevis differs considerably from that in ranid species. The most conspicuous element of the plexiform zones is the ribbon synapse. The basal processes of the photoreceptor cells may be presynaptic elements of simple, tangential, dyad or triad synaptic contacts. Conventional synapses were observed only occasionally. Electrophysiological recordings revealed that the pineal complex of Xenopus laevis is directly sensitive to light. In response to light stimuli, two types of responses, achromatic and chromatic, were recorded from the nerve of the frontal organ. In contrast, the epiphysis exhibited only achromatic units. The opposed color mechanism of the chromatic response showed a maximum sensitivity at approximately 360 nm for the inhibitory and at 520 nm for the excitatory event. The action spectrum of the achromatic response of the epiphysis and the frontal organ peaked between 500 and 520 nm and showed no Purkinje-shift during dark adaptation. The functional significance of these phenomena is discussed.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

H W Korf, R Liesner, H Meissl, A Kirk. 1981. Pineal complex of the clawed toad, Xenopus laevis Daud.: structure and function.. https://doi.org/10.1007/bf00234548

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Honeybee Apis mellifera acetylcholinesterase--a biomarker to detect deltamethrin exposure.

The purpose of this study is to investigate the possibility to use acetylcholinesterase (AChE) as a biomarker of exposure to deltamethrin insecticide in the honeybee, Apis mellifera and to test its reliability in the presence of other contaminants, as carbamate insecticide. Joined actions of deltamethrin (pyrethroid) and pirimicarb (carbamate), alone or in association, are investigated on AChE activity in surviving and dead honeybees, with a special focus on the relative proportions of its membrane and soluble forms. At the 0.5X dose (12.5 ng of deltamethrin and/or 2.5 microg of pirimicarb per bee), the residual tissue AChE activity in dead bees was 78% with deltamethrin, 43% with pirimicarb and 33% with dual treatment. In surviving bees, tissue AChE activity represented 250%, and 270% of control AChE activity with deltamethrin and dual treatment, respectively. The analysis of membrane and soluble AChE forms revealed an increase in the soluble form in dead bees after deltamethrin and dual treatment. However, in vitro investigations showed no direct interaction of deltamethrin on soluble and membrane AChE activity. The results suggest that the action of deltamethrin on AChE activity, in honeybee intact organisms, could be due to indirect mechanisms. The duality of AChE response to deltamethrin exposure, exhibited by the possibility of increase (surviving bees) or decrease (dead bees) of its activity has been pointed out for the first time. The important increase in AChE activity in response to deltamethrin, not altered by pirimicarb treatment, suggests that AChE activity could represent a robust biomarker specific to deltamethrin exposure in living bees.

Acetylcholinesterase↗

An unusual cause of atrial fibrillation: exposure to insecticides.

BACKGROUND: Although there are many well-known cardiac results of insecticide poisoning, atrial fibrillation (AF) has not been reported as the result of insecticide intoxication. CASE: Twenty-six-year-old male, complaining of nausea and vomiting, presented to the emergency department with a history of methomyl dust exposure. All physical examination findings were normal except irregular heart rate on cardiac auscultation. The electrocardiogram of the patient showed AF with normal ventricular response. Patient's acetylcholinesterase (ACE) level was 3,319 IU/L in presentation and pralidoxim use was seen unnecessary for the treatment. The patient's rhythm spontaneously returned to sinus rhythm 24 hr after the presentation and no cardiopulmonary pathology was found during the follow-up. The patient was discharged without symptoms. CONCLUSION: AF is a rare complication of insecticide intoxication. In this case, treatment of symptoms was adequate until a normal sinus rhythm returned.

Acetylcholinesterase↗

Screening of acetylcholinesterase inhibitors in natural extracts by CE with electrophoretically mediated microanalysis technique.

An electrophoretically mediated microanalysis (EMMA) method for screening acetylcholinesterase (AChE) inhibitors in natural extracts is described. In this method, solutions of AChE and the mixture of the substrate and the natural extract were successively injected into the capillary, and mixed electrophoretically by applying a voltage for a short time. Afterwards the voltage was reapplied to separate the product from the unreacted substrate and the natural extract. The measured peak area of the product at UV 230 nm represents the enzyme activity. Since the extract is mixed with the substrate, there is no need to separate the components before testing the inhibition. The inhibitory activity of the natural extract as a whole can be easily found if the peak area of the product is reduced. This makes the present method suitable for screening inhibitors in complex mixtures, such as natural extracts. Compared to the commonly used spectrometric method for screening of AChE inhibitors, the major advantage of the present method is the elimination of Ellman reagent, which is essential for the spectrometric method. This not only simplifies the experimental procedure but also minimizes false-positive results. Moreover, it is an obvious advantage of combining the separation power with the on-column enzyme assay for further investigating which compound(s) is/are responsible for the inhibition. The method was validated using a commercially available AChE inhibitor tacrine and a small chemical library containing four AChE inhibitors and 32 natural extracts. Inhibitors in natural extracts were identified with the present method.

Acetylcholinesterase↗