Is there a chloride ATPase in the gills of the shore crab Carcinus maenas?

Siebers, D.; Petrausch, G.; Böttcher, K.

doi:10.1007/bf00300958

Cited by 5 publications

(2 citation statements)

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“…As outlined by Siebers et al (1990), mitochondrial ATPase has previously been considered as plasma membranous CI--ATPase located in the gills of fishes and crustaceans (see also Kirschner, 1979). In addition to the work pubhshed in 1990, the present paper describes the mitochondrial ATPase as being strictly bound to cellular particulates represented by the combined mitochondrial fractions uncontaminated with plasma membranes (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Since in crab gills the majority of mitochondria is embedded in the dense network of basolateral plasma membrane invaginations, the sites of ATP synthesis in mitochondria and ATP utlhzation by Na-K-ATPase present in plasma membranes are located in close vicinity. The relation between ATP synthesis and consumption was shown by Siebers et al (1990) using crude gill homogenates. They found out that in posterior gills of shore crabs Carcinus maenas, the activities of both enzymes were increased greatly in osmoregulating specimens maintained in brackish water of 10 %~ S.…”

Section: Discussionmentioning

confidence: 99%

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Mitochondrial ATPase in the gills of the shore crabCarcinus maenas

Siebers

Hentschel

Böttcher

et al. 1992

Helgolander Meeresunters

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Posterior gills (No. 7 and 8) of shore crabs Carcinus maenas were homogenized and fractionated by means of differential and density gradient centrffugation. Employment of marker enzymes Na-K-ATPase and carbonic anhydrase for plasma membranes and cytochrome oxidase for mitochondria showed that these structural elements were separated. Ultramicroscopic investigations of combined fractions confirmed the presence of the respective mitochondrial and vesicular plasma membrane structures. An ATPase which did not depend on the presence of sodium (20 raM) ions in the incubation medium but on the presence of potassium (20 mM) ions only was found in the mitochondrial fractions. The mitochondrial ATPase was tightly bound to cellular particulates and activated approximately threefold by bicarbonate (20 mM) ion~. The activity of this ATPase was nearly completely inhibited by oligomycin (1 ~g m1-1) and greatly inhibited by low levels (5 mM) of thiocyanate and calcium ions, the Ki for Ca 2+ being ca 4 raM. The results obtained confirm literature data on high mitochondrial densities in crab gills and allow the assumption of significant rates of energy metabolism in these organs. Considering its properties the mitochondrial ATPase is clearly distinct from crab gilI Na-K-ATPase and can be measured specifically in samples containing Na-KATPase. Mitochondrial ATPase is therefore considered a suitable and reliable marker enzyme for mitochondria.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Mitochondrial ATPase in the gills of the shore crabCarcinus maenas

Siebers

Hentschel

Böttcher

et al. 1992

Helgolander Meeresunters

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Mechanisms of Excretion and Ion Transport in Invertebrates

O’Donnell

1997

Comprehensive Physiology

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The sections in this article are: Ion Transport and Osmoregulation in Invertebrates: Functional Morphology and Cellular Mechanisms Water Expulsion Vesicles and Contractile Vacuoles in Protozoans, Sponges, and Cnidarians Nephridia and Coelomoducts: Embryology and Terminology Nephridia Coelomoduct‐Derived Renal Organs Gut‐Derived Renal Organs Other Ion‐Transporting Structures Excretion in Invertebrates Nitrogenous Wastes Alkaloids Organic Anions Organic Cations Magnesium and Sulfate Storage and Deposit Excretion Catabolism of Insect Neurohormones by Malpighian Tubules Roles of Arthropod Excretory Systems and Molluscan Mantle in Acid‐Base Regulation Active Transport of Sugars Transport of Cardiac Glycosides Passive Permeability to Metabolites and Toxins Future Research

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