A new method for the cytochemical demonstration of phosphatase activities in yeasts based on the use of cerous ions

Veenhuis, Marten; Dijken, Johannes P. van; Harder, W.

doi:10.1111/j.1574-6968.1980.tb05654.x

Cited by 67 publications

(18 citation statements)

References 20 publications

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“…The presence of a peroxisomal P~-pool was confirmed cytochemically in all yeast strains studied using Ce 3 +-ions as an orthophosphate-trapping agent (Veenhuis et al 1980). After incubation of formaldehyde-fixed spheroplasts with CeC13 in the presence of ATP at pH 8.5, reaction deposits were distributed throughout the peroxisomal matrix (Fig.…”

Section: Resultsmentioning

confidence: 62%

“…In the latter case only the vacuoles were stained (Fig. 5 B), most probably due to alkaline phosphatase activity (Veenhuis et al 1980).…”

Section: Resultsmentioning

confidence: 88%

“…All samples were washed in 0.1 M cacodylate buffer pH 6.0 before postfixation in OsO4/KzCr207 mixtures as described previously (Veenhuis et al 1980). 4 0 PPM Fig.…”

Section: Cytochemistrymentioning

confidence: 99%

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A 31P NMR study of the internal pH of yeast peroxisomes

et al. 1987

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Section: Resultsmentioning

confidence: 62%

“…In the latter case only the vacuoles were stained (Fig. 5 B), most probably due to alkaline phosphatase activity (Veenhuis et al 1980).…”

Section: Resultsmentioning

confidence: 88%

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A 31P NMR study of the internal pH of yeast peroxisomes

et al. 1987

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“…It is considered to be a reliable, useful method, although it does not distinguish Ca 2+ -transporting ATPases from ecto-ATPases. We used cerium as the capture agent (instead of lead) for the ultrastructural demonstration of phosphate ions released, because it does not cause non-specific precipitation (Veenhuis et al, 1980). This method proved to be sensitive when used in combination with X-ray analysis, which permits the identification and precise localization of small amounts of reaction products.…”

Section: Discussionmentioning

confidence: 99%

Detection and Localization of a Ca2+-ATPase Activity in Toxoplasma gondii.

Bouchot

Jaillet

Bonhomme

et al. 2001

Cell Struct. Funct.

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ABSTRACT. Toxoplasma gondii, the agent causing toxoplasmosis, is an obligate intracellular protozoan parasite.A calcium signal appears to be essential for intracellular transduction during the active process of host cell invasion. We have looked for a Ca 2+ -transport ATPase in tachyzoites and found Ca 2+ -ATPase activity (11-22 nmol Pi liberated/mg protein/min) in the tachyzoite membrane fraction. This ATP-dependent activity was stimulated by Ca 2+ and Mg 2+ ions and by calmodulin, and was inhibited by pump inhibitors (sodium orthovanadate or thapsigargin). We used cytochemistry and X-ray microanalysis of cerium phosphate precipitates and immunolabelling to find the Ca 2+ , Mg 2+ -ATPase. It was located mainly in the membrane complex, the conoid, nucleus, secretory organelles (rhoptries, dense granules) and in vesicles with a high calcium concentration. Thus, Toxoplasma gondii possesses Ca 2+ -pump ATPase (Ca 2+ , Mg 2+ -ATPase) as do eukaryotic cells.

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“…Whenever observed, the lead phosphate precipitate was spotty over the ER and Golgi apparatus, and, in addition, a fine nonspecific lead deposit was observed over the nucleus and cytoplasm of the various testicular cells. The utilization of cerium chloride as a capture agent instead of lead nitrste, originally recommended by Veenhuis et al [42], and utilized by some investigators thereafter [14,20,22,33], considerably improved the localization of G6Pase activity within testicular cells. Indeed, the consistency of the results obtained in several successive experiments, the uniformity of the distribution of the fine cerium precipitate over ER cisternae and some Golgi elements as well as the absence of non-specific dusty cerium deposits over the nucleus and cytoplasm of the testicular cell argued in favor of using cerium ions as capture agents.…”

Section: Value ~F the Cerium Technique For The Ultrastructural Localmentioning

confidence: 99%

Glucose‐6‐phosphatase activity of endoplasmic reticulum and Golgi apparatus in spermatocytes and spermatids of the rat: an electron microscopic cytochemical study

Thorne-Tjomsland

Clermont

Tang³

1991

Biology of the Cell

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Summary -The glucose-6-phosphatase (G6Pase) activity of cytoplasmic components of spermatocytes and spermatids of the rat was examined by electron microscope cytochemistry using cerium chloride as a capture agent. G6Pase activity, a recognized ERresident enzyme, was present in all ER cisternae of spermatocytes. In spermatids, while some ER cisternae were G6Pase-rcactive, others were negative or only slightly reactive, indicating an unequal distribution of the enzymatic activity throughout the network of ER cisternae in these cells. In spermatocytes, the c/s-and trans-elements of the stacks of Golgi saccules were slightly but significantly reactive for G6Pase. In the Golgi apparatus of spermatids, the c/s-element, 4 or 5 underlying saccules, as well as one or two thick trans Golgi elements were G6Pase reactive. The G6Pase activity of the various Golgi elements, fike that of the ER cisternae was not affected by the pH of the medium and was completely inhibited by Na-vanadate, a known G6Pase inhibitor. Sertoli and Leydig cells, submitted to the same cytochemical conditions, showed complete G6Pase reactivity of their ER; however in Sertoli cells, all Golgi components were consistently negative while in Leydig cells the c/s-and trans-elements of the Golgi stacks were slightly reactive, as in spermatocytes. Thus, the G6Pase reactivity of Golgi elements, appeared variable from one cell type to another. The compact juxtanuclear Golgi apparatuses of spermatocyte, and spermatids were both associated with numerous G6Pase reactive ER cisternae; some were present at their Curface, others crossed their cortices between Golgi stacks and formed elaborate networks in their cores. Other ER cisternae, in tur:,, were closely apposed to or intertwined with trans-elements of the Golgi stacks, a relationship raising the possibility of molecular ex~,,langes at this pole of the stacks in germinal cells.lllueose-6-phosphatme I endopluml¢ retleulum I Golgi apparatus I spermulocytes I spermatids

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A new method for the cytochemical demonstration of phosphatase activities in yeasts based on the use of cerous ions

Cited by 67 publications

References 20 publications

A 31P NMR study of the internal pH of yeast peroxisomes

A 31P NMR study of the internal pH of yeast peroxisomes

Detection and Localization of a Ca2+-ATPase Activity in Toxoplasma gondii.

Glucose‐6‐phosphatase activity of endoplasmic reticulum and Golgi apparatus in spermatocytes and spermatids of the rat: an electron microscopic cytochemical study

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