PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 411883

Segregation during cleavage of a factor determining endodermal alkaline phosphatase development in ascidian embryos.

J R Whittaker
View original source ↗Export metadata ↓

Abstract

Localized alkaline phosphatase activity (EC 3.1.3.1) develops progressively in endodermal tissues of the presumptive digestive system in Ciona intestinalis embryos. It was first detected histochemically at late gastrulation, and a puromycin sensitivity period coincident with this time suggests that new alkaline phosphatase is synthesized. Embryos in which cell division was blocked with cytochalasin B at early cleavage stages up to the 64-cell stage, eventually differentiated strong alkaline phosphatase activity in certain cells at each cleavage-arrested stage. The maximum cell numbers and their positions were identical to those of the previously known endodermal cell lineage. Actinomycin D did not prevent development of endodermal alkaline phosphatase when administered from fertilization onwards, nor did other inhibitors of RNA synthesis (chromomycin A3, cordycepin, and daunomycin). There is probably a preformed maternal mRNA for endodermal alkaline phosphatase present in the unfertilizec Ciona egg. Either this RNA itself, or some related translation factor, is localized in the egg cytoplasm and segregated during early cleavages into the endodermal cell lineage of the embryo.

Explore related subjects

AcetylcholinesteraseAlkaline PhosphataseAnimalsCiona intestinalisCytochalasin BDactinomycinEndodermFemaleFertilizationMitosisMonophenol MonooxygenaseOvumPhenylalaninePuromycinUrochordataJournal ArticleResearch Support, U.S. Gov't, P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J R Whittaker. 1977. Segregation during cleavage of a factor determining endodermal alkaline phosphatase development in ascidian embryos.. https://doi.org/10.1002/jez.1402020202

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

KEEP EXPLORING

Related citations

PubMed2007

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↗
PubMed2007

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↗
PubMed2007

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↗