Effects of parathyroid hormone on plasma and urinary adenosine 3′,5′-monophosphate in man

Kaminsky, Neil I.; Broadus, Arthur E.; Hardman, Joel G.; Jones, Douglas J.; Ball, John H.; Sutherland, Earl W.; Liddle, Grant W.

doi:10.1172/jci106458

Cited by 258 publications

(108 citation statements)

References 21 publications

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“…Purification appeared to be unnecessary for assay of cyclic AMP and cyclic GMP in urine*. The infusion of calcium gluconate in a patient increased urinary excretion of cyclic GMP (Table 2) as reported previously (17).…”

Section: Assay Conditionssupporting

confidence: 56%

A Simple, Sensitive Protein-binding Assay for Guanosine 3′:5′-Monophosphate

Murad

Manganiello

Vaughan

1971

Proc. Natl. Acad. Sci. U.S.A.

151

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A protein-binding assay for guanosine 3':5'-monophosphate, which employs an enzyme preparation from lobster tail muscle, is described. The binding constant for cyclic GMP was 2-10 nM for four different enzyme preparations. The method can be set up in several days and permits the detection of as little as 0.5-1 pmol of cyclic GMP. In some instances, it is possible to assay the nucleotide in urine or deproteinized extracts of tissue without purification. For other samples, a simple method for separating and purifying cyclic AMP and cyclic GMP is described.Although guanosine 3': 5'-monophosphate (cyclic GMP) has been found in urine and many tissues (1-5), its physiological role remains to be established. Investigation in this area has been hampered by the relatively difficult and/or insensitive methods currently available for its assay, and the necessity of complicated purification procedures before assay (2, 3, 6). Assays for cyclic AMP, using preparations of cyclic AMPbinding protein from skeletal muscle (7) or adrenal (8), have recently been described. The cyclic AMP-binding protein is apparently a component of preparations that contain cyclic AMP-stimulated protein kinase activity. We have developed a similar binding assay for cyclic GMP using a protein fraction from lobster muscle that contains cyclic GMP-stimulated protein kinase activity (9). The method described permits the detection of as little as 1 pmol of cyclic GMP. Deproteinized extracts from some sources can be assayed directly, but samples from tissues in which cyclic GMP concentrations are relatively low require prior purification. A simple method for separation and purification of cyclic GMP and cyclic AMP is also described. MATERIALS AND METHODS Preparation of enzymeThe protein preparation used for binding of cyclic GMP was prepared from lobster tail muscle, through the dialyzed (NH4)r-S04 step, by essentially the same procedures as described by Kuo and Greengard (9) for the preparation of a cyclic GMPdependent protein kinase. Protein-kinase activity (9, 10) at this stage of purification was stimulated about 2.5-fold with 1 ;zM cyclic GMP and 2-fold with 1 ,uM cyclic AMP. The protein-kinase activity of the homogenate, and of the pH 4.9 supernatant fraction, was essentially unaltered by cyclic GMP or cyclic AMP. Attempts to further purify the dialyzed (NH4)2S04 fraction by chromatography on DEAE-cellulose, carboxymethyl-cellulose, phosphocellulose, or gel filtration with Sephadex G-100 resulted in large losses in both protein-kinase and cyclic GMP-binding activities. The dialyzed (NH4)2S04 fractions have been stored at -70OC for several months without significant loss of binding activity. With each thawing and refreezing of a preparation, however, about 5-10% of the binding activity is lost. For use in the assay, the dialyzed preparation (11-15 mg protein/ml) was divided into 1-to 2-ml portions, which were stored at -700C. Preparation of tissue samplesMale Wistar rats were anesthetized with ether and pieces of liver, lung, and cerebellum ...

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Section: Assay Conditionssupporting

confidence: 56%

A Simple, Sensitive Protein-binding Assay for Guanosine 3′:5′-Monophosphate

Murad

Manganiello

Vaughan

1971

Proc. Natl. Acad. Sci. U.S.A.

151

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“…PTH is one of the most potent acute phosphaturic factors inducing urinary phosphate excretion within 15 to 45 minutes after application (15,18). We and others have shown that PTH causes phosphate excretion at least in part by inducing the internalization of the NaPi-IIa phosphate cotransporter from the brush border membrane of proximal tubules in rats and mice (2,3,7,12,30,48).…”

Section: -mentioning

confidence: 99%

“…However, the relative contribution of these transporters to overall renal phosphate handling and the integration of several signals on the level of the proximal under these circumstances remains an open question. PTH application elicits a rapid phosphaturic response both in humans and rodents (15,18). In contrast to rodents, several lines of evidence suggest that NaPiIIa may not be the major type II phosphate transporters in human kidney.…”

Section: Napi-iic Expression Was Not Altered By Pth In Agreement Withmentioning

confidence: 99%

“…The expression of Pit-2 and the relevance of an PFA-sensitive phosphate transport activity in the brush border membrane has not been studied in human kidney and remains unknown to date. If NaPi-IIa does not play a major role in human kidney and if NaPi-IIc does internalize or inactivate only with a delayed time course (as indicated by studies in rodents (37)), then other phosphate transporters must mediate the acute phosphaturic effect of PTH in humans (18). Whether Pit-2 could be a candidate for this transport activity, remains to be investigated in humans and human cell lines.…”

Section: Napi-iic Expression Was Not Altered By Pth In Agreement Withmentioning

confidence: 99%

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Acute parathyroid hormone differentially regulates renal brush border membrane phosphate cotransporters

Picard

Capuano

Stange

et al. 2010

Pflugers Arch - Eur J Physiol

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“…Fluctuations in the high basal ratios of milligrams phosphate/milligrams creatinine excretion [9] obscured a phosphaturic response to PTH, if indeed, this did occur (Table III). Thus, the increased excretion of 3',5'-AMP after PTH infusion can be interpreted as a demonstration of PTH responsiveness of the kidney in diis disease [5,9,23,30,41,44].…”

Section: 'Y-amp Excretionmentioning

confidence: 99%

Vitamin D-Dependent Rickets: Actions of Parathyroid Hormone and 25-Hydroxycholecalciferol

Rosen

Finberg

1972

Pediatr Res

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ExtractDuring active rickets, the increase in 3',5'-adenosine monophosphate (3',5'-AMP) excretion after infusion of parathyroid hormone (PTH) can be claimed as a demonstration of PTH responsiveness, at least as far as the kidney is concerned (Table II). In patients with vitamin D-dependent rickets, following 25-HGC therapy, the basal excretion ratios of nanomoles 3',5'-AMP/milligrams creatinine fall within the normal range, and, although the basal ratios of milligrams phosphate/milligrams creatinine excretion decrease to normal (Tables III, IV, and V), a phosphaturic response to PTH is still not evident. The high basal ratios of nanomoles 3',5'-AMP/ milligrams creatinine and milligrams phosphate/milligrams creatinine suggest underlying hyperparathyroidism during a phase of this syndrome marked by hypocalcemia and hyperaminoaciduria. During 2-day PTH challenges, while rickets was active, the peak increases in serum calcium above base line were 1.92, 1.80, and 1.86 mg/100 ml. After treatment with 25-hydroxycholecalciferol (25-HCG), no further significant increases in serum calcium above base line could be elicited (Tables VI, VII, VIII). It would seem, therefore, that, while these patients were untreated, small but sufficient amounts of 25-HCC or another metabolite of vitamin D were available to permit the calcium-mobilizing action of PTH on bone. The observed hypocalcemia in vitamin D-dependent rickets, then, is most likely secondary to a defect in gastrointestinal absorption. Mineral balance studies during active rickets revealed an absorptive defect for calcium, phosphorus, and magnesium-a defect completely reversible after 25-HCC treatment. Speculation

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Effects of parathyroid hormone on plasma and urinary adenosine 3′,5′-monophosphate in man

Cited by 258 publications

References 21 publications

A Simple, Sensitive Protein-binding Assay for Guanosine 3′:5′-Monophosphate

A Simple, Sensitive Protein-binding Assay for Guanosine 3′:5′-Monophosphate

Acute parathyroid hormone differentially regulates renal brush border membrane phosphate cotransporters

Vitamin D-Dependent Rickets: Actions of Parathyroid Hormone and 25-Hydroxycholecalciferol

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