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Histochemical study of the enzymatic activity of human neoplasms. III. Structural‐functional relationships in a hepatoma
Author(s) -
Braunstein Herbert
Publication year - 1966
Publication title -
cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.052
H-Index - 304
eISSN - 1097-0142
pISSN - 0008-543X
DOI - 10.1002/1097-0142(196607)19:7<939::aid-cncr2820190707>3.0.co;2-z
Subject(s) - enzyme , staining , alkaline phosphatase , excretory system , atpase , glycogen , biochemistry , chemistry , pathology , biology , endocrinology , medicine
A human hepatoma obtained at surgery was studied histochemically and compared with adjacent normal liver. While glycogen content was diminished in the hepatoma, glucose‐6‐phosphatase staining was approximately the same as normal. Enzymatic activity of those enzymes concerned with cellular energy production and associated with mitochondria was similar to normal. Alkaline phosphomonoesterases were absent in the hepatoma while increased canalicular polyphosphatase (“ATPase”) was associated with bizarre canalicular structure. Lysosomes and the enzymes associated with them were more prominent than normal in hepatoma. There was evidence of increased staining intensity for an enzyme associated with DNA synthesis in the hepatoma. Many of these findings appear to be consistent features of human and well‐differentiated experimental hepatomas. The author suggests that virtually all of the abnormalities reflect either the failure of the neoplasm to obtain access to normal vascular supply and excretory ducts or its rate and manner of growth.