PubMed Health⌕ Search

Biomedical subjects

J T Potts

Publications and source records attributed to J T Potts.

At least 253 records · Page 14Linked to original sources
PubMed1973

Secretion of calcitonin in hypocalcemic states in man.

The control of calcitonin secretion in humans has been studied extensively only in patients with medullary thyroid carcinoma since the peripheral concentration of the hormone in normal subjects is too low for accurate measurement by existing assay procedures. However, we have recently found that the concentrations of calcitonin in the peripheral plasma of hypocalcemic subjects during provocative tests of hormone secretion were high enough to be measured by radioimmunoassay. Accordingly, the effect of calcium and pentagastrin infusions on plasma calcitonin was studied in nine patients with pseudohypoparathyroidism, seven patients with idiopathic hypoparathyroidism, and six patients with hypocalcemia not due to parathyroid disease. The infusion of calcium in these hypocalcemic subjects resulted in increases in plasma calcitonin to levels that could be readily detected by our radioimmunoassay. Pentagastrin infusion also caused an increase of plasma calcitonin in some subjects, but calcium was approximately 10 times more effective than gastrin in its stimulatory effect on hormone secretion. These results demonstrate that in humans as well as other mammals the secretion of calcitonin by parafollicular cells that are not involved by medullary thyroid carcinoma is directly related to plasma calcium and that gastrin can also stimulate hormone secretion. The results are consistent with the thesis that the secretion of calcitonin by normal human subjects does occur but at peripheral concentrations of the hormone below the detection limits of most existing immunoassays; hypocalcemia leads to increased stores of hormone that can be related by the appropriate stimuli.

Calcitonin↗
PubMed1972

Proparathyroid hormone: biosynthesis by human parathyroid adenomas.

Biosynthesis of a precursor (proparathyroid hormone) to human parathyroid hormone was demonstrated during incubation of tissue from parathyroid adenomas. The proparathyroid hormone is labeled more rapidly than parathyroid hormone during incubation with amino acids labeled with carbon-14 and is progressively converted to the hormone. Apparent differences in the relative rate of conversion of precursor to hormone found in different tumors suggest that proparathyroid hormone may accumulate in some of the tumors and be secreted into the circulation.

Adenoma↗
PubMed1972

Proparathyroid hormone: identification of a biosynthetic precursor to parathyroid hormone.

Biosynthesis of a precursor to bovine parathyroid hormone has been demonstrated in slices of parathyroid tissue incubated in vitro. The proparathyroid hormone is 15-20 amino acids larger than the bovine hormone, and has a molecular weight of about 11,500 as determined by polyacrylamide gel electrophoresis. Upon incubation of parathyroid slices with [(14)C]aminoacids, radioactivity is detected initially in the precursor. If incorporation of [(14)C]aminoacids is inhibited after a short incubation either by replacement of radioactive amino acids with unlabeled amino acids or by addition of puromycin, the amount of radioactivity in the precursor decreases, while the radioactivity in the hormone continues to increase. The precursor is bound by an antibody that is specific for parathyroid hormone, and its binding can be inhibited by addition of the hormone. Analysis of tryptic digests indicates that the precursor and the hormone have common tryptic peptides, and that there are at least two additional peptides in the precursor.

Amino Acids↗