Acta Neuropathologica

, Volume 75, Issue 6, pp 547–553 | Cite as

Localisation of calcium-activated adenosine-triphosphatase (Ca2+-ATPase) in intracerebral arterioles in acute hypertension

Regular Papers


The plasma membrane calcium-activated adenosine triphosphatase (Ca2+-ATPase) is known to regulate intracellular calcium levels. This enzyme was localised in intracerebral cortical vessels of normotensive and acutely hypertensive rats. Of interest was whether the arterioles that develop increased permeability to horseradish peroxidase (HRP) in acute hypertension demonstrate any alteration in localisation of Ca2+-ATPase as compared to normotensive controls. Rats were injected with HRP intravenously and acute hypertension was induced by a 2-min infusion of angiotensin amide. Following perfusion of fixative, brains were sliced and reacted for demonstration of HRP reaction product and Ca2+-ATPase. Normotensive rats showed discontinuous distribution of Ca2+-ATPase on the outer plasma membranes of endothelial, smooth muscle and adventitial cells of arterioles. The localisation of Ca2+-ATPase in pinocytotic vesicles present in endothelial and smooth muscle cells was quite striking. Focal cortical areas of hypertensive rats showed increased arteriolar permeability to HRP. Permeable arterioles showed marked reduction of Ca2+-ATPase on the outer plasma membranes of endothelium and smooth muscle cells as compared to nonpermeable arterioles of the same animals and arterioles of normotensive controls. The latter finding suggests that calcium may be involved in increased cerebrovascular permeability mechanisms in acute hypertension.

Key words

Cerebrovascular Ca2+-ATPase Hypertension Endothelium 


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  1. 1.
    Ando T, Fujimoto K, Mayahara H, Miyajima H, Ogawa K (1981) A new one-step method for the histochemistry and cytochemistry of Ca2+-ATPase activity. Acta Histochem Cytochem 14:705–726Google Scholar
  2. 2.
    Bambauer H, Ueno S, Umar H, Ueck M (1985) Histochemical and cytochemical demonstration of Ca++-ATPase activity in the stellate cells of the adenohypophysis of the guinea pig. Histochemistry 83:195–200Google Scholar
  3. 3.
    Cossu M, Lantini M, Puxwssu P, Riva A (1984) Cytochemical localization of ouabain-sensitive K+-dependentp-nitrophenyl phosphatase and Ca++-stimulated adenosine triphosphatase activities in human parotid and submandibular glands. Histochemistry 81:221–226Google Scholar
  4. 4.
    Ghijsen WJEM, Dejong MD, VanOs CH (1980) Dissociation between Ca2+-ATPase and alkaline phosphatase activities in plasma membranes of rat duodenum. Biochim Biophys Acta 599:538–551Google Scholar
  5. 5.
    Losse H, Zidek W, Zumkley H, Wessels F, Vetter H (1981) Intracellular Na as a genetic marker of essential hypertension. Clin Exp Hypertens [A] 3:627–640Google Scholar
  6. 6.
    Marchesi V, Barrnett R (1963) The demonstration of enzymatic activity in pinocytic vesicles of blood capillaries with the electron microscope. J Cell Biol 17:547–556Google Scholar
  7. 7.
    Nag S (1984) Cerebral endothelial surface charge in hypertension. Acta Neuropathol (Berl) 63:276–281Google Scholar
  8. 8.
    Nag S (1985) Ultrastructural localisation of monosaccharide residues on cerebral endothelium. Lab Invest 5:553–558Google Scholar
  9. 9.
    Nag S (1986) Cerebral endothelial plasma membrane alterations in acute hypertension. Acta Neuropathol (Berl) 70:38–43Google Scholar
  10. 10.
    Nag S (1987) Ultrastructural localisation of calcium-activated adenosine triphosphatase (Ca2+-ATPase) in cerebral endothelium. Lab Invest 57:52–56Google Scholar
  11. 11.
    Nag S, Harik SI (1987) Cerebrovascular permeability to horseradish peroxidase in hypertensive rats: effects of unilateral locus ceruleus lesion. Acta Neuropathol (Berl) 73:247–253Google Scholar
  12. 12.
    Nag S, Robertson D, Dinsdale H (1979) Quantitative estimate of pinocytosis in acute experimental hypertension. Acta Neuropathol (Berl) 46:107–116Google Scholar
  13. 13.
    Nellans HN, Popovitch JE (1981) Calmodulin-regulated, ATP-driven calcium transport by basolateral membranes of rat small intestine. J Biol Chem 256:9932–9936Google Scholar
  14. 14.
    Terepka AR, Coleman JR, Armbrecht HJ, Gunter TE (1976) Transcellular transport of calcium. J Biol Chem 30:117–140Google Scholar
  15. 15.
    Vezzoli G, Elli A, Tripodi G, Bianchi G, Carafoli E (1985) Calcium ATPase in erythrocytes of spontaneously hypertensive rats of the Milan strain. J Hypertension 3:645–648Google Scholar

Copyright information

© Springer-Verlag 1988

Authors and Affiliations

  • S. Nag
    • 1
  1. 1.Department of PathologyQueen's University and Kingston General HospitalKingstonCanada

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