Parathyroid cell polarity as revealed by cytochemical localization of ATPases, alkaline phosphatase and 5'-nucleotidase.
Activities of Ca2(+)-dependent ATPase, Mg2(+)-dependent ATPase, Na(+)-K(+)-dependent ATP-ase, alkaline phosphatase, and 5'-nucleotidase were demonstrated after incubation of 40-microns vibratome sections of bovine parathyroids and subsequent visualization by electron microscopy. Prior to sectioning, parathyroid tissue was fixed with 1% glutaraldehyde for localization of alkaline phosphatase, and with 2% formaldehyde and 1% glutaraldehyde for demonstration activities of ATPases and 5'-nucleotidase. The activities of the five enzymes were found at the apicolateral domain of the plasma membrane in parathyroid cells, i.e. at the site parathyroid cells face neighbouring parenchymal cells. Ca2(+)-ATPase activity was also seen on mitochondria, Golgi complex and RER. The presence of these plasma membrane associated enzymes at the apicolateral domain only indicate polarity in parathyroid cells. It further suggests that many processes including transmembrane transport take place at the apicolateral domain, the site of parathyroid cells opposing blood capillaries.
Wild
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Veterinär-Anatomisches Institut, Universität Zürich.
Schraner
E M
EM
D015720:5'-Nucleotidase / Q000032:analysis*; D000251:Adenosine Triphosphatases / Q000032:analysis*; D000469:Alkaline Phosphatase / Q000032:analysis*; D000818:Animals; D002417:Cattle; D007150:Immunohistochemistry; D008854:Microscopy, Electron; D010280:Parathyroid Glands / Q000201:enzymology* / Q000648:ultrastructure
D000469:Alkaline Phosphatase; D015720:5'-Nucleotidase; D000251:Adenosine Triphosphatases