Fine structural localization of alkaline phosphatase in the granular pneumonocytes of hamster lung.
The fine structural localization of nonspecific alkaline phosphatase was studied in the granular pneumonocytes (type II alveolar epithelial cells) of hamster lung by incubating sections of glutaraldehyde-fixed tissues in a medium containing lead ions and sodium beta-glycerophosphate or alpha-naphthyl acid phosphate. The specificity of the reaction was tested by exposing the sections to inhibitors of alkaline phosphatase. The results showed that alkaline phosphatase activity was present in the inclusion bodies of granular pneumonocytes. The enzyme reaction was strong in the membrane lining the inclusion bodies and a weaker reaction was generally detectable in the inclusion contents. Although only a proportion of the inclusion bodies showed enzyme activity, there was no obvious correlation between the reactivity of the inclusions and their intracellular position or size. The other organelles were unreactive. The finding of alkaline phosphatase activity within the inclusion bodies of granular pneumonocytes is an enigma as these organelles are generally considered to be lyosomes.
D000469:Alkaline Phosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D006224:Cricetinae; D004847:Epithelial Cells; D004848:Epithelium / Q000201:enzymology; D006651:Histocytochemistry; D066298:In Vitro Techniques; D002479:Inclusion Bodies / Q000201:enzymology; D008247:Lysosomes / Q000201:enzymology; D011650:Pulmonary Alveoli / Q000201:enzymology* / Q000648:ultrastructure
D000469:Alkaline Phosphatase