• Biomedical Science Letters
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• v.23 no.3
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• pp.230-237
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• 2017

Changes in the activity of alkaline phosphatase (ALP) isoenzymes and isoforms in human serum have a major diagnostic value, therefore the regulation of ALP activities is a valuable target for therapeutic interventions. To assess the pharmacological activity of retinoids, i.e., all-trans retinoic acid and 13-cis retinoic acid, their tissue-specific inhibitory effect on human serum ALP activity was elucidated by chemical inhibition methods, heat-sensitive inactivation, and wheat-germ lectin precipitation test. Retinoids showed significant inhibition of the total ALP activity in human serum at a concentration of 5 mM. All-trans retinoic acid (5 mM) and 13-cis retinoic acid (5 mM) inhibited ALP activities by up to 12% and 15%, respectively, compared to that by guanidine hydrochloride (200 mM). L-phenylalanine (100 mM) and urea (30 mM) had no further inhibitory effect on ALP activities in human serum pretreated with retinoids (5 mM). Retinoids significantly inhibited ALP activities by up to 20% compared with that of tetramisole (30 mM). The ALP activities in retinoid-pretreated serum remained unchanged after the heat inactivation process. These results suggest that retinoids are inhibitors of the intestinal ALP isoenzyme. Remarkably, retinoids revealed potent inhibitory activities against ALP in wheat-germ lectin precipitant serum, indicating that they also function as inhibitors of the bone ALP isoform. The results show that retinoids inhibit the specific tissue-derived human serum ALP activities, moreover, the inhibitory effect of retinoids against bone ALP activity suggests their clinical utility as monitoring and prevention of metastasis of bone cancer.

• The Korean Journal of Zoology
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• v.25 no.1
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• pp.9-28
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• 1982

Cyclical changes in the fine structures of the surface epithelial, stroma and glandular cells of guinea pig endometrium during the estrous cycle were studied by transmission and scanning electron microscopy. Cytochemical studies were made in order to investigate the ultrastructural localization of the acid phosphatase, alkaline phosphatase and ATPase in these cells. The results obtained are as follows: 1. The endometrial surface epithelium was pseudostratified columnar during estrus and meterstrus, and simple columnar during proestrus and diestrus. The characteristic features observed in these cells include increased nucleocytoplasmic ratio at proestrus, elongated shapes of both the nucleus and the entire cell, increased volume of the cytoplasm and cytoplasmic bulding into the lumen during estrus, and smaller surface epithelial cells during metestrus. 2. In the cytoplasm of surface epithelial cells, the numbers of mitochondria and free ribosomes were increased, and rough endoplasmic reticulum and Golgi complex appeared during estrus, and the degenerated cells, lipid droplets, multilamellated bodies and lysosomes appeared during diestrus. 3. During estrus, scanning electron microscopic observations of endometrial surface showed a regular arrangement with polygonal outlines of epithelial cells, distinct intercellular border, and bulged surface into the lumen, whereas flat surface and indistinct cell border were characteristic during meterstrus and diestrus. 4. Microvilli which aligned on the surface were longer and most abundant during estrus while short and aparse during other phases. 5. Cytochemical studies indicated that during metestrus acid phosphatase activities were localized in the microvilli and vacuoles, and alkaline phosphatase activities were significant around luminal surface and lateral cell membrane in the surface epithelial cells. ATPase activities were present on the microvilli and cell membrane during proestrus and estrus.

• The Korean Journal of Community Living Science
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• v.16 no.4
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• pp.25-38
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• 2005

In order to investigate the effect of dietary zinc and phytic acid levels on enzyme activity and lipid metabolism in rats, male Sprague-Dawley rats, weighing approximately 60-74g, were fed different diets which contained 0, 0.35 or $1.05\%$ phytic acid each at 3 levels of zinc (0, 30 and 1500ppm zinc) for 28 days. Body weight gain, food consumption, and food efficiency ratio were lower in the rats fed a zinc deficient diet (0ppm zinc) than those consuming 30 or 1500ppm dietary zinc. The activities of GOT, GPT and alkaline phosphatase were lower in the rats consuming 30ppm zinc than those fed 0 or 1500ppm zinc diet. The activity of GOT was increased in rats consuming $0.35\%$ phytic acid, whereas that of alkaline phosphatase was decreased in the rats fed phytic acid-containing diet. The concentration of phospholipid in serum was higher in rats fed $0.35\%$ dietary phytic acid, whereas that of liver phospholipid was higher in zinc deficient groups, and increased by addition of dietary phytic acid. The concentration of triglyceride in serum from rats fed 30ppm zinc was lower than those fed 0 or 1500ppm zinc On the other hand, liver triglyceride was higher in both the rats fed 30ppm zinc and $0.35\%$ phytic acid. The concentration of serum total cholesterol was lower in the rats fed 30ppm zinc diet, and it was increased by addition of dietary phytic acid. But liver total cholesterol was higher in 30ppm zinc group. HDL-cholesterol in serum was the highest in both rats consuming 30ppm zinc and $0.35\%$ dietary phytic acid, and the ratio of HDL-cholesterol to total cholesterol was higher in rats consuming 30ppm zinc diet. In conclusion, we suggest that coronary heart disease or liver disease can be prevented with phytic acid in rats which are fed the high zinc diet.

• Clinical and Experimental Reproductive Medicine
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• v.8 no.2
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• pp.1-11
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• 1981

The quantitative analyses of the phosphatase activity in the endometrium of the rat ovariectomized on Day 2 of pregnancy was carried out in comparison with the intact one, in order to investigate the hormonal dependency of the uterus prior to the implantation, and to study the phosphatase activity in the endometrial tissues in vitro incubated in different acidity of the medium. The results obtained were as follows: 1. The activity of the total phosphatase was the highest at Day 3 of pregnancy of the intact animals irrespective of acidity of the medium. However, the ovariectomized rat showed its peak somewhat delayed. The time of the highest activity of the enzymes was matched with the time of high secretion of the ovarian hormones. 2. The activity of acid phosphatase in the endometrium was twice or four times as much high as that of neutral or alkaline phosphatase, respectively. 3. The activity of alkaline phosphatase was rather steady in Day 3 through Day 5 of the pregnancy of the rat intact or ovariectomized but with low level compared to those of other phosphatase. 4. The present re~lt indicated more important role by $Mg^{2+}$-dependent phosphatase than by $K^+$-dependent one for the preparation for decidualization.

• BMB Reports
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• v.29 no.5
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• pp.417-422
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• 1996

In clonal sublines with different metastatic ability derived from Dunning rat prostate tumor, phosphoamino acid levels of cellular proteins were determined. Cell lines with high metastatic ability exhibited 5-fold higher phosphotyrosine level than did cell lines with low metastatic ability, while the contents of phosphoserine and phosphothreonine were similar among cell lines examined, All cell lines showed similar activities of protein tyrosine kinases as well as overall protein kinases. Phosphotyrosine protein phosphatase (PTPP) activities of the cells with high metastatic ability were very low, compared to those of the cells with low metastatic ability, suggesting that the different phosphotyrosine levels among the cell lines were due to the difference in PTPP activities rather than protein tyrosine kinase activities. Cellular activities of prostatic acid phosphatase (PAcP), which has been reported to possess phosphotyrosine protein phosphatase activity, were shown to be inversely related to the phosphotyrosine levels and metastatic abilities of the prostate tumor cells, These results suggest that cellular PAcP activity, regulating phosphotyrosine levels of cellular proteins, is closely connected with the metastatic process in prostate tumor cells and can be utilized as a good biochemical marker for the diagnosis of metastasis of prostate tumor.

• The Korean Journal of Zoology
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• v.18 no.4
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• pp.173-180
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• 1975

Activities of serum alkaline phosphatase(SALP) and serum acid phosphatase (SACP) have been assayed in adult male Sprague-Dawley rats acclimated to $30^\\circ C$ and $33^\\circ C$for 240 hours and 64 hours, respectively. The alteration in the activities of SALP and SACP in rats acclimated to $33^\\circ C$ was generally greater than those acclimated to $30^\\circ C$. The SACP and SALP activities of the rats acclimated to $30^\\circ C$ showed generally a persistently high levels in comparison to the control. It may be inferred that the SALP and SACP positibly be involved directly or indirectly in thermoregulation during acclimation to $30^\\circ C$.

• Current Research on Agriculture and Life Sciences
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• v.3
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• pp.85-91
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• 1985

The change of acid-phosphatase in Fuji apples Was investigated in terms of storage temperature and pressure. The firmness, sugar contents, acidity and activity of acid-phosphatase with electrophoretic pattern were studied during storage. The firmness, sugar contents and acidity were decreased during storage. Ratio of decrease was greater at normal temperature than low temperature and normal atmosphere than sub-atmosphere. Acid phosphatase activity of apples was mainly existed cell wall fraction and increased with climacteric rise and decreased later. The activity was higher at normal temperature than low temperature and at atmosphere than sub-atmosphere. The optimal temperature and pH were $45^{\circ}C$ and pH 5.6, respectively. In stability of heat and pH, enzyme solution was stabilized to $30^{\circ}C$ and pH 5-8. Electrophoretic pattern of enzyme solution extracted from sub-atmospheric pressure with low temperature and normal atmospheric pressure with normal temperature yielded two activity bands during storage.

• Applied Biological Chemistry
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• v.20 no.1
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• pp.136-141
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• 1977

DEAE-Cellulose, Sephadex column chromatography and polyacrylamide gel electrophoresis were used to purify acid phosphatase, aryl sulfatases, ${\beta}-glucuronidase$ and cathepsin D in n-butyl alcohol extracts of porcine leukocyte Iysosomes. The degree of purification was quite high for all enzymes studied and some could be identified by histochemical reactions.

• Proceedings of the Korean Society of Life Science Conference
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• 2007.10a
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• pp.100.1-100.1
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• 2007

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• BMB Reports
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• v.34 no.6
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• pp.517-525
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• 2001

Six renaturable protein kinases that utilize the myelin basic protein (MBP) as a substrate were activated during prolonged exposure of cardiac myocytes to okadaic acid (OA). We characterized the substrate preference and activation of these kinases, with particular emphasis on 3 novel kinases-MBPK-55, MBPK-62 and MBPK-87. The transcription factors c-Jun, Elk, ATF2, and c-Fos that are used to assess mitogen-activated protein kinase activation were all poor substrates for these three kinases. MAPKAPK2 was also not phosphorylated. In contrast, Histone IIIS was phosphorylated by MBPK-55 and MBPK-62. These protein kinases were activated in cultured cardiac fibroblasts, H9c2 cardiac myoblasts, and Cos cells. High concentrations (0.5 to $1\;{\mu}M$) of OA were essential for the activation of the protein kinases in all of the cell types examined, whereas calyculin A [an inhibitor of protein phosphatase 1 (PP1) and PP2A], cyclosporin A (a PP2B inhibitor), and an inactive OA analog all failed to activate these kinases. The high dose of okadaic acid that is required for kinase activation was also required for phosphatase inhibition, as assessed by immunoblotting whole cell lysates with anti-phosphothreonine antibodies. A variety of chemical inhibitors, including PD98059 (MEK-specific), genistein (tyrosine kinase-specific) and Bisindolylmaleimide I (protein kinase C-specific), failed to inhibit the OA activation of these kinases. Thus, MBPK-55 and MBPK-62 are also Histone IIIS kinases that are widely expressed and specifically activated upon exposure to high OA concentrations.