Alkaline phosphatase levels in normal and diseased small bowel.

Ferguson, Anne; Watson, William C.; Maxwell, J. D.; Fell, G. S.

doi:10.1136/gut.9.1.96

Cited by 17 publications

(7 citation statements)

References 13 publications

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“…The reduced activities in coeliac disease of the four brush-border enzymes assayed in the present study are in good agreement with those of previous workers (Plotkin & Isselbacher, 1964;Sheehy & Anderson, 1965;Weser & Sleisenger, 1965;Ferguson, Watson, Maxwell & Fell, 1968;Cohen, McNamara, Blumenfeld & Arias, 1970;Campbell, Cowen, McGeary & Gaffney, 1972;Berg, Dahlquist, Lindberg & Norden, 1973;Cerf, Chariot, Fox & Debray, 1973). The return towards normal values noted in our treated patients was also found by these workers.…”

Section: Brush-border Changessupporting

confidence: 94%

Enzyme Activities and Properties of Lysosomes and Brush Borders in Jejunal Biopsies from Control Subjects and Patients with Coeliac Disease

1975

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1. Reduced activities of four enzymes from brush borders were found in intestianl biopsies from patients with untreated coeliac disease. The activities returned towards control values after treatment by gluten withdrawal. Parallel changes were noted for the cytosol enzyme lactate dehydrogenase. 2. Measurement of brush-border integrity by differential centrifugation of biopsy extracts indicated increased fragility of the brush borders in biopsies from untreated patients. Normal values were obtained for biopsies from treated patients. 3. Increased activites of six acid hydrolases (lysosomal enzymes) were found in biopsies from untreated coeliac patients. Normal values were obtained for biopsies from treated patients. 4. Assement of lysosomal integrity by assay of latent N-acetyl-beta-glucosaminidase and of sedimentable activity of four acid hydrolases demonstrated increased lysosomal fragility in untreated coeliac mucosa. These lysosomal changes return to within the normal range after treatment by gluten withdrawal. 5. The lysosomal changes are consistent with their having a pathogenic role in the enterocyte damage of coeliac disease. Possible mechanisms for the lysosomal changes are discussed.

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Section: Brush-border Changessupporting

confidence: 94%

Enzyme Activities and Properties of Lysosomes and Brush Borders in Jejunal Biopsies from Control Subjects and Patients with Coeliac Disease

1975

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“…Due to the necessity to treat patients lifelong, oral administration would be preferred for such a treatment. Phosphatases are abundantly present in the gut (Ferguson et al , ); therefore, it has been always claimed that orally administered PPi cannot reach the circulation and therefore is not effective in inhibiting ectopic calcification (Orriss et al , ). We have tested this assumption in healthy human individuals and in mouse models reflecting two human hereditary calcification disorders, PXE and GACI.…”

Section: Introductionmentioning

confidence: 99%

Oral administration of pyrophosphate inhibits connective tissue calcification

et al. 2017

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Various disorders including pseudoxanthoma elasticum (PXE) and generalized arterial calcification of infancy (GACI), which are caused by inactivating mutations in ABCC6 and ENPP1, respectively, present with extensive tissue calcification due to reduced plasma pyrophosphate (PPi). However, it has always been assumed that the bioavailability of orally administered PPi is negligible. Here, we demonstrate increased PPi concentration in the circulation of humans after oral PPi administration. Furthermore, in mouse models of PXE and GACI, oral PPi provided via drinking water attenuated their ectopic calcification phenotype. Noticeably, provision of drinking water with 0.3 mM PPi to mice heterozygous for inactivating mutations in Enpp1 during pregnancy robustly inhibited ectopic calcification in their Enpp1 −/− offspring. Our work shows that orally administered PPi is readily absorbed in humans and mice and inhibits connective tissue calcification in mouse models of PXE and GACI. PPi, which is recognized as safe by the FDA, therefore not only has great potential as an effective and extremely low‐cost treatment for these currently intractable genetic disorders, but also in other conditions involving connective tissue calcification.

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“…They therefore suggested that there must be a compensating increased production of alkaline phosphatase to allow this in the presence of the severe morphological abnormalities encountered. Ferguson, Watson, Maxwell, and Fell (1968) found the mean concentration of alkaline phosphatase per gram of mucosa considerably less than normal though the concentration in some patients with 'villous atrophy' did fall within the range of the normal control observations. Observations on the clinical significance of intestinal alkaline phosphatase in interpreting serum levels are few.…”

mentioning

confidence: 61%

Serum alkaline phosphatase in adult coeliac disease

Harris¹,

Warner²,

Cooke³

1969

Gut

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SUMMARYThe total alkaline phosphatase levels were determined in 118 patients with adult coeliac disease, 65 of whom had evidence of osteomalacia.The secretor and blood group status, intestinal isoenzyme, and liver alkaline phosphatase played no significant part in the levels of serum alkaline phosphatase found.There was a significant correlation between the levels of serum alkaline phosphatase and the presence of osteomalacia.

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Alkaline phosphatase levels in normal and diseased small bowel.

Cited by 17 publications

References 13 publications

Enzyme Activities and Properties of Lysosomes and Brush Borders in Jejunal Biopsies from Control Subjects and Patients with Coeliac Disease

Enzyme Activities and Properties of Lysosomes and Brush Borders in Jejunal Biopsies from Control Subjects and Patients with Coeliac Disease

Oral administration of pyrophosphate inhibits connective tissue calcification

Serum alkaline phosphatase in adult coeliac disease

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