Effect of calcium on rat intestinal alkaline phosphatase activity and molecular aggregation

Abstract Macromolecular alkaline phosphatase (EC 3.1.3.1) was found in the serum of a patient suffering from myasthenia gravis (adult type II) complicated with thymoma, and was shown by immunoelectrophoresis to be bound to immunoglobulins A and G (IgG). Placental alkaline phosphatase, complexed with either the patient's serum or IgG purified from the patient's serum, remained at the origin on electrophoresis, with significant loss of activity. Intestinal alkaline phosphatase, complexed with either the patient's serum or the patient's IgG, migrated to a position similar to that of the macromolecular alkaline phosphatase in the patient's serum on electrophoresis. About 50% of the placental alkaline phosphatase activity was inhibited with 0.1-0.2 g of the patient's IgG per liter, but 6.93 g of the IgG per liter was required for about 20% inhibition of the intestinal alkaline phosphatase activity. The complex of intestinal alkaline phosphatase with the patient's IgG was fairly heat stable. From these results, we concluded that the macromolecular alkaline phosphatase in the patient's serum consisted of intestinal alkaline phosphatase and IgG that was specific for placental alkaline phosphatase.

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In vitro stimulation of apparent intestinal alkaline phosphatase activity by thyrocalcitonin

Clinica Chimica Acta ◽

10.1016/0009-8981(74)90426-4 ◽

1974 ◽

Vol 57 (2) ◽

pp. 171-173 ◽

Cited By ~ 5

Author(s):

C. Lechi ◽

G. De Bastiani ◽

M. Zatti

Keyword(s):

Alkaline Phosphatase ◽

Phosphatase Activity ◽

Alkaline Phosphatase Activity ◽

Intestinal Alkaline Phosphatase ◽

Stimulation Of

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Tissue alkaline phosphatase activity and expression in an experimental infant swine model of cardiopulmonary bypass with deep hypothermic circulatory arrest

10.21203/rs.3.rs-21432/v1 ◽

2020 ◽

Author(s):

Ludmila Khailova ◽

Justin Robison ◽

James Jaggers ◽

Richard Ing ◽

Scott Lawson ◽

...

Keyword(s):

Alkaline Phosphatase ◽

Cardiac Surgery ◽

Cardiopulmonary Bypass ◽

Phosphatase Activity ◽

Alkaline Phosphatase Activity ◽

Circulatory Arrest ◽

Deep Hypothermic Circulatory Arrest ◽

Hypothermic Circulatory Arrest ◽

Swine Model ◽

Intestinal Alkaline Phosphatase

Abstract Background: Infant cardiac surgery with cardiopulmonary bypass results in decreased circulating alkaline phosphatase that is associated with poor post-operative outcomes. Bovine intestinal alkaline phosphatase infusion represents a novel therapy for post-cardiac surgery organ injury. However, the effects of cardiopulmonary bypass and bovine-intestinal alkaline phosphatase infusion on tissue-level alkaline phosphatase activity/expression are unknown.Methods: Infant pigs (n=20) underwent cardiopulmonary bypass with deep hypothermic circulatory arrest followed by four hours of intensive care. Seven control animals underwent mechanical ventilation only. Cardiopulmonary bypass/deep hypothermic circulatory arrest animals were given escalating doses of bovine intestinal alkaline phosphatase infusion (0-25U/kg/hr; n=5/dose). Kidney, liver, ileum, jejunum, colon, heart and lung were collected for measurement of tissue alkaline phosphatase activity and mRNA.Results: Tissue alkaline phosphatase activity varied significantly across organs with the highest levels found in the kidney and small intestine. Cardiopulmonary bypass with deep hypothermic circulatory arrest resulted in decreased kidney alkaline phosphatase activity and increased lung alkaline phosphatase activity, with no significant changes in the other organs. Alkaline phosphatase mRNA expression was increased in both the lung and the ileum. The highest dose of bovine intestinal alkaline phosphatase resulted in increased kidney and liver tissue alkaline phosphatase activity.Conclusions: Changes in alkaline phosphatase activity after cardiopulmonary bypass with deep hypothermic circulatory arrest and bovine intestinal alkaline phosphatase delivery are tissue specific. Kidneys, lung, and ileal alkaline phosphatase appear most affected by cardiopulmonary bypass with deep hypothermic circulatory arrest and further research is warranted to determine the mechanism and biologic importance of these changes.

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Non-thermal effects of 0.1 THz radiation on intestinal alkaline phosphatase activity and conformation

Chinese Physics B ◽

10.1088/1674-1056/ab50fd ◽

2019 ◽

Vol 28 (12) ◽

pp. 128702

Author(s):

Xin-Xin Zhang ◽

Ming-Xia He ◽

Yu Chen ◽

Cheng Li ◽

Jin-Wu Zhao ◽

...

Keyword(s):

Alkaline Phosphatase ◽

Phosphatase Activity ◽

Alkaline Phosphatase Activity ◽

Thermal Effects ◽

Thz Radiation ◽

Intestinal Alkaline Phosphatase

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Possible role of intestinal alkaline phosphatase activity in thiamine transport

Cellular and Molecular Life Sciences ◽

10.1007/bf01921875 ◽

1978 ◽

Vol 34 (1) ◽

pp. 18-20 ◽

Cited By ~ 13

Author(s):

T. Matsuda ◽

A. Baba ◽

H. Iwata

Keyword(s):

Alkaline Phosphatase ◽

Phosphatase Activity ◽

Alkaline Phosphatase Activity ◽

Intestinal Alkaline Phosphatase ◽

Thiamine Transport

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Effect of fat feeding on intestinal alkaline phosphatase activity in tissue and serum

AJP Gastrointestinal and Liver Physiology ◽

10.1152/ajpgi.1981.241.6.g461 ◽

1981 ◽

Vol 241 (6) ◽

pp. G461-G468 ◽

Cited By ~ 7

Author(s):

G. P. Young ◽

S. Friedman ◽

S. T. Yedlin ◽

D. H. Allers

Keyword(s):

Alkaline Phosphatase ◽

Enzyme Activity ◽

Small Bowel ◽

Phosphatase Activity ◽

Alkaline Phosphatase Activity ◽

Intestinal Alkaline Phosphatase ◽

Serum Enzyme ◽

Small Bowel Mucosa ◽

Fat Feeding ◽

Bowel Mucosa

Serum intestinal alkaline phosphatase activity is increased by fat feeding, but the mechanism of this increase is not fully understood. Fasting rats were fed a single feed of either corn oil (12 kcal) or an isocaloric elemental feed (Vivonex 100 HN). Changes in enzyme activity in the small bowel mucosa and serum were followed for 20 h. Only the fat-fed rats had increased serum enzyme activity, being maximal at 7 h and three times the fasting level. This resulted from an increase in the amount of enzyme protein in the serum and not from an increase in its catalytic efficiency. The serum biological half-life of 125I-labeled intestinal alkaline phosphatase was the same in fasted (2.51 min) and fat-fed rats (2.55 min). Both types of feed caused a quantitatively similar increase in brush-border-bound alkaline phosphatase activity. However, levels of soluble intracellular alkaline phosphatase in intestinal mucosa were affected differently: the elemental diet caused a substantial rise, whereas no significant change was seen after fat feeding. The isoelectric pattern of phosphatase activity in serum after fat feeding was identical to that of soluble intracellular and not membranous alkaline phosphatase. Therefore, serum intestinal alkaline phosphatase activity rises in response to a single fat feed as a result of increased delivery of the enzyme to the blood and not as a result of an increase in its normally short biological half-life. This rise cannot be directly linked to an increase in the amount of brush-border-bound enzyme, and it appears that the serum enzyme is derived directly from a pool of soluble intracellular enzyme in the small bowel mucosa.

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