Amylase in lung carcinomas. An ultrastructural and immunohistochemical study of two adenocarcinomas, and a review of the literature.
The ultrastructure of two lung adenocarcinomas with immunohistochemical and biochemical expression of amylase is reported. Isoenzyme determination performed on tumour tissue showed a salivary-type amylase. None of the carcinomas was associated with hyperamylasaemia. Ultrastructurally, the adenocarcinomas contained a varying number of heterogeneous granules resembling lysosomes. None of the tumours contained mature zymogen granules. The findings are discussed in relation to previous cases of amylase-containing lung carcinomas subjected to electron microscopy. The vast majority of these carcinomas were associated with a significant elevation of serum amylase. Various theories which might explain the absence of hyperamylasaemia in the presented cases are proposed. The biological and diagnostic significance of amylase production is discussed.
Grove
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Institute of Pathology, Aalborg Hospital, Denmark.
D000230:Adenocarcinoma / Q000201:enzymology* / Q000473:pathology / Q000601:surgery / Q000648:ultrastructure; D000368:Aged; D000681:Amylases / Q000032:analysis*; D000951:Antigens, Neoplasm / Q000032:analysis; D003896:Desmosomes / Q000473:pathology / Q000648:ultrastructure; D005260:Female; D006801:Humans; D007124:Immunoenzyme Techniques; D008175:Lung Neoplasms / Q000201:enzymology* / Q000473:pathology / Q000601:surgery / Q000648:ultrastructure; D008297:Male; D008854:Microscopy, Electron; D008875:Middle Aged
D000951:Antigens, Neoplasm; D000681:Amylases