Histochemical study on the ouabain-sensitive potassium-dependent p-nitrophenyl phosphatase activity along the nephron in several mammals.

Kubo, Takashi; Mayahara, Hiroshi; Kawai, Chuichi; Ogawa, Kazuo

doi:10.1267/ahc.15.717

Cited by 4 publications

(1 citation statement)

References 33 publications

(69 reference statements)

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“…The structural internephron and species heterogeneity is paralleled by a corresponding heterogeneity of several enzymes that are related to specific cell organelles. Thus the Na +,K +-ATPase activity, associated with the lateral cell membranes (31,110,204,278,341), shows a pattern of decrease along the segment similar to the decrease observed in the lateral cell membrane area (207,249,323,359,360). The enzyme is localized exclusively in the lateral membranes, where it is co-localized with ankyrin (224), and it is absent in the basal cell membranes, abutting on the basement membrane (204,224).…”

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confidence: 74%

Morphology of the Loop of Henle, Distal Tubule, and Collecting Duct

Kaissling

Kriz

1992

Comprehensive Physiology

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The sections in this article are: Loops of Henle Intermediate Tubule Thick Ascending Limb Macula Densa Distal Segments Definition and Nomenclature General Cytological Organization of the Distal Segments Distal Convoluted Tubule Connecting Tubule Cortical Collecting Duct Medullary Collecting Ducts Microanatomical Organization and Histotopographical Aspects Outer Medullary Collecting Duct Inner Medullary Collecting Duct Cytochemical Aspects Structure—Function Correlations Intercalated Cells Cell Structure Intercalated Cells in the Cortex Cytochemical Aspects Distribution of Intercalated Cells in the Kidney Zones Structure—Function Correlations

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confidence: 74%

Morphology of the Loop of Henle, Distal Tubule, and Collecting Duct

Kaissling

Kriz

1992

Comprehensive Physiology

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Quantitative immunogold localization of Na, K-ATPase along rat nephron

et al. 1992

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Ultrastructural localization of Na, K-ATPase alpha-subunit along rat nephron segments was investigated quantitatively by immunogold electron microscopy on LR-White ultrathin sections using affinity-purified antibody against alpha-subunit of the enzyme. Ultrathin sections were incubated with the antibody at a saturation level and the number of gold particles bound per micron of the plasma membrane (particle density) of the tubular epithelial cells from the proximal tubule to the collecting duct was determined. In all the tubular epithelial cells, gold particles were located exclusively on the basolateral surface, and no significant binding of gold particles to the apical surface was observed. Distribution of gold particles on the basolateral membranes was quite heterogeneous; lateral membranes and infolded basal membranes were highly labeled, whereas the basal membranes which are in direct contact with the basal lamina were scarcely labeled. The average particle density on the basal surface was highest in the distal straight tubule cells (11.4 units), very high in the distal convoluted tubule cells (9.8 units), intermediate in the proximal tubule cells (3.3 units), in the connecting tubule cells (4.3 units), and in the principal cells of the collecting duct (5.6-3.8 units), low in the thin limb of Henle's loop (1.0 unit), and at the control level in the intercalated cells in the connecting and collecting duct. The relative number of gold particles/mm nephron segment and the relative number of gold particles in the various nephron segments were calculated using quantitative morphological data. The estimated distribution profile of the former was in good agreement with the Na, K-ATPase activity profile in rat nephron, which was determined biochemically with a microenzymatic method.

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