[An immunohistochemical study on three aldolase isozymes in human lung cancer].
We investigated three aldolase isozymes (aldolase A, B, and C) in human lung cancer by using an indirect peroxidase labeled antibody method. We used 27 tissue samples obtained at surgical operations which were fixed in periodate-lysine-4% paraformaldehyde (PLP) solution, and embedded in optimum cutting temperature (OCT) compound. They were 11 adenocarcinomas, 9 squamous cell carcinomas, 3 large cell carcinomas, 3 small cell carcinomas, and 1 adenosquamous carcinoma. Aldolase A and C expressed intensely positive stainings in the cytoplasm of cancer cells compared with normal lung tissues, and its positivities were 81% respectively. However, Aldolase B showed almost negative staining, and its positivities were only 41%. These rates had no relation to the histological types or pathological stages of lung cancers, and suggested that human lung cancer contained increased levels of aldolase A, and C.
Ojika
T
T
Department of Thoracic Surgery, Nagoya University School of Medicine, Japan.
Imaizumi
M
M
Watanabe
H
H
Abe
T
T
Kato
K
K
D000230:Adenocarcinoma / Q000201:enzymology; D018288:Carcinoma, Small Cell / Q000201:enzymology; D002294:Carcinoma, Squamous Cell / Q000201:enzymology; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D007527:Isoenzymes / Q000378:metabolism*; D008175:Lung Neoplasms / Q000201:enzymology*
D007527:Isoenzymes; D005634:Fructose-Bisphosphate Aldolase