Literature DB >> 1330315

Ecto-ATPase/phosphatase activity in the olfactory sensilla of the spiny lobster, Panulirus argus: localization and characterization.

R A Gleeson1, H G Trapido-Rosenthal, L M McDowell, H C Aldrich, W E Carr.   

Abstract

Electrophysiological studies have shown that the olfactory organ (antennule) of the spiny lobster, Panulirus argus, has chemoreceptors that are selectively excited by adenine nucleotides in seawater. Biochemical studies have revealed that these same nucleotides can be rapidly dephosphorylated by ectoenzymes associated with the olfactory sensilla (aesthetascs). In this study the distribution of ecto-ATPase/phosphatase activity within aesthetascs was determined cytochemically and the nature of the adenine-nucleotide dephosphorylating activity was dissected biochemically. Cytochemically, the distribution of ATP-dephosphorylating activity was similar to that shown previously for AMP and beta-glycerol phosphate; i.e., cerium phosphate reaction product was specifically localized to the transitional zone where the sensory dendrites develop cilia and branch to form the outer dendritic segments. Unlike the dephosphorylation of AMP and beta-glycerol phosphate, Mg2+ or Ca2+ was required for ecto-ATPase/phosphatase activity. Biochemical measures of both AMP- and ATP-dephosphorylating activity within aesthetascs corroborated the cytochemical evidence that these activities are localized to the transitional zone. A major portion of the AMP dephosphorylation (about 67%) derives from nonspecific alkaline phosphatase activity that is insensitive to levamisole and L-bromotetramisole. In contrast, nonspecific phosphatase activity accounted for a much smaller part of the ATP dephosphorylation (about 15%). Ectoenzymatic activity in the transitional zone may be an important means of removing excitatory/inhibitory nucleotides from this region.

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Year:  1992        PMID: 1330315     DOI: 10.1007/bf00353899

Source DB:  PubMed          Journal:  Cell Tissue Res        ISSN: 0302-766X            Impact factor:   5.249


  14 in total

1.  Kinetics and inhibition of rat and avian alkaline phosphatases.

Authors:  H van Belle
Journal:  Gen Pharmacol       Date:  1976

2.  Ultrastructural localization of Na+/K(+)-ATPase in rodent olfactory epithelium.

Authors:  R C Kern; T P Kerr; T V Getchell
Journal:  Brain Res       Date:  1991-04-12       Impact factor: 3.252

3.  The inhibition of alkaline phosphatase by L-p-bromotetramisole.

Authors:  M Borgers; F Thoné
Journal:  Histochemistry       Date:  1975-08-28

4.  Divalent cation-activated ecto-nucleoside triphosphatase activity of nervous system cells in tissue culture.

Authors:  V Stefanovic; M Lédig; P Mandel
Journal:  J Neurochem       Date:  1976-09       Impact factor: 5.372

5.  Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans.

Authors:  H Van Belle
Journal:  Clin Chem       Date:  1976-07       Impact factor: 8.327

6.  Kinetics and inhibition of alkaline phosphatases from canine tissues.

Authors:  H Van Belle
Journal:  Biochim Biophys Acta       Date:  1972-11-10

7.  Preparation and properties of 5'-nucleotidase from smooth muscle of small intestine.

Authors:  R M Burger; J M Lowenstein
Journal:  J Biol Chem       Date:  1970-12-10       Impact factor: 5.157

8.  Ectonucleotidase activities associated with cholinergic synaptosomes isolated from Torpedo electric organ.

Authors:  E J Grondal; H Zimmermann
Journal:  J Neurochem       Date:  1986-09       Impact factor: 5.372

9.  ATP-sensitive chemoreceptors: antagonism by other nucleotides and the potential implications of ectonucleotidase activity.

Authors:  R A Gleeson; W E Carr; H G Trapido-Rosenthal
Journal:  Brain Res       Date:  1989-09-11       Impact factor: 3.252

10.  Enzymic characteristics of ecto-adenosine triphosphatase in rat epididymal intact spermatozoa.

Authors:  G C Majumder
Journal:  Biochem J       Date:  1981-04-01       Impact factor: 3.857

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