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Aldolase isozymes in human tissue and serum. With special reference to cancer diagnosis

✍ Scribed by Kiyoshi Tsunematsu; Tadao Shiraishi

Publisher
John Wiley and Sons
Year
1969
Tongue
English
Weight
448 KB
Volume
24
Category
Article
ISSN
0008-543X

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✦ Synopsis

Aldolase isozyme activity was estimated on the basis of rate of degradation of 2 substrates, fructose-1, 6-diphosphate (FDP) and fructose-1-phosphate (FIP).

Degradation ratios of these 2 substrates (FDP/FlP) in the liver and skeletal muscle were 1 and 54 respectively. In other tissues, it was found to be between these 2 values. However, FDP/FlP ratio of cancerous tissues was approximately that in skeletal muscle, irrespective of tissue origin. FDP/FlP ratio in healthy human serum was less than 5 i n all cases, while that of cancer patient serum was mostly elevated to over 5. In other diseases, only muscular dystrophy showed serum FDP/FlP ratio of more than 5. This was also true of the effusions due to various diseases; FDP/FlP ratio was over 5 in all cancerous effusions and less than 1.5 in noncancerous. These results, therefore, indicate that the determination of aldolase isozyme ratio FDP/FIP in serum and effusions can be of value for the diagnosis of cancer.

LTHOUGH ESTIMATION OF ALDOLASE ACTIVITY

A is presently based on the rate of fructose-1, 6-diphosphate (FDP) degradation, this enzyme is also known to split fructose-l-phosphate (FlP).1.zr3 Of interest is the marked difference in the rate of degradation of these 2 substrates in enzyme preparations obtained from the liver and muscle. If the activity ratio is expressed as FDP/FlP, it has been shown to be about one in the liver and about 50 in the muscle. 19 Recently, Schapirag reported that FDP/FlP ratio of the liver was approximately one both in humans and albino rats, while that of hepatoma increased to a mean value of 5.48 in humans and 24 to 50 in rats.

The aim of the present study was to investigate the aldolase activity in various human cancer tissues, including hepatoma, by measuring the rate of degradation of 2 sub-From the

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