Increased expression of sucrase and intestinal-type alkaline phosphatase in human gastric carcinomas with progression.
The activities of sucrase, total alkaline phosphatase (total ALP) and intestinal-type alkaline phosphatase (I-ALP) were assayed in gastric carcinomas and in their surrounding mucosae from 57 patients with advanced cancers, and the localization of sucrase in 203 carcinomas, including 86 early cancers, was examined immunohistochemically using polyclonal anti-sucrase antibody. All three enzymes were active in the 57 carcinomas as well as in their surrounding mucosae, but the levels were fairly low as compared to those in normal jejunum mucosa. A considerable part of the total ALP activity in tumor specimens was assumed to be due to I-ALP itself. Increased sucrase and I-ALP were found with greater depth of invasion by undifferentiated-type carcinomas. The pattern of immunohistochemical localization of sucrase in the 203 carcinomas also clearly indicated increased expression with greater depth of invasion even in differentiated-type carcinomas.
Nakamura
W
W
Laboratory of Pathology, Aichi Cancer Center Research Institute, Nagoya.
Inada
K
K
Hirano
K
K
Tsukamoto
T
T
Inoue
H
H
Kito
K
K
Yoshikawa
A
A
Nakamura
S
S
Tatematsu
M
M
D000230:Adenocarcinoma / Q000201:enzymology* / Q000473:pathology; D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D000469:Alkaline Phosphatase / Q000096:biosynthesis* / Q000378:metabolism; D018450:Disease Progression; D005260:Female; D006801:Humans; D007150:Immunohistochemistry; D007422:Intestines / Q000201:enzymology; D008297:Male; D008875:Middle Aged; D010641:Phenotype; D013274:Stomach Neoplasms / Q000201:enzymology* / Q000473:pathology; D013393:Sucrase / Q000096:biosynthesis* / Q000378:metabolism
D000469:Alkaline Phosphatase; D013393:Sucrase