Differential localization of alkaline phosphatase in barrier tissues of the frog and rat nervous systems: a cytochemical and biochemical study
- PMID: 3500190
- DOI: 10.1002/cne.902640302
Differential localization of alkaline phosphatase in barrier tissues of the frog and rat nervous systems: a cytochemical and biochemical study
Erratum in
- J Comp Neurol 1988 Mar 8;269(2):313
Abstract
We investigated the localization of alkaline phosphatase (AP) in the peripheral and central nervous systems of the frog (Rana pipiens) and rat. In the frog sciatic nerve, AP reaction product was seen as a precipitate within caveolae and vesicular profiles of perineurial cells, and frequently filled the extracellular space. In the rat peripheral nerve, AP reaction product appeared as small tufts on the cell surfaces and within vesicular profiles of endoneurial blood vessels. AP reaction product was not detected in the rat perineurium or in endoneurial blood vessels of the frog. In the frog central nervous system, AP reaction product was detected in the arachnoid membrane adjacent to the subarachnoid space, but not in the cerebral or pial vessels, whereas in the rat it was detected in the outer arachnoid membrane and in the cerebral and pial blood vessels. Biochemical analysis indicated a sevenfold higher AP activity in the frog perineurium over the endoneurium, whereas in the rat, threefold more activity was measured in the endoneurium over the perineurium. Levamisole, an AP inhibitor, decreased the enzyme activity by 95% in rat tissues, and by 70% in frog tissues and in plasma from both animals. Similar decrements were observed cytochemically. This study suggests that: (1) the distribution of AP varies between species, but that it is always present in at least one component of the blood-brain and blood-nerve barriers, (2) because barrier tissues of the nervous system have enzymatic activity, they may biochemically modify the adjacent environment, (3) vesicular profiles and caveolae in the blood vessels and perineurium may function as microenvironments for enzymatic activity, and (4) in the rat and frog, different isozymes of AP may be present.
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