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H L Henry

Publications and source records attributed to H L Henry.

At least 55 records · Page 3Linked to original sources
PubMed1983

Cyclic AMP dependent protein kinase and its endogenous inhibitor protein: tissue distribution and effect of vitamin D status in the chick.

1. Vitamin D deficiency in the chick leads to decreased (to 55% of normal) cyclic AMP-dependent protein kinase activity in the kidney but does not alter calcium-dependent phospholipid-sensitive protein kinase activity. 2. Decreased cyclic AMP-dependent protein kinase activity in response to vitamin D deficiency was not observed in other tissues including pancreas, brain, liver, intestinal mucosa, or heart. 3. Vitamin D deficiency leads to elevated levels of the endogenous inhibitor protein of cyclic AMP-dependent protein kinase in kidney, but not heart, muscle, pancreas, or brain.

Animals↗
PubMed1983

Homologous desensitization of cultured chick kidney cells to parathyroid hormone.

The development of refractoriness of the cAMP response to PTH in primary cultures of chick kidney cells and recovery from the refractory state was investigated. When cells were preincubated with bovine PTH1-34, complete refractoriness to a subsequent challenge with the hormone developed within 2 h and at hormone concentrations as low as 5 ng/ml. The ability of PTH to stimulate activation of cAMP-dependent protein kinase was also abolished by preincubation with the hormone. When cells were desensitized and then incubated in hormone-free medium, recovery of the cAMP response began within an hour and was maximal, but not complete (80%) after 16 h. Cycloheximide did not affect either desensitization or the rate or extent of recovery from the refractory state. Low concentrations of forskolin (2.5 X 10(-7) M) greatly enhanced cAMP production stimulated by PTH and higher concentrations (10(-6) - 10(-4) M) stimulated rates of cAMP production 50 times those obtained with PTH alone. Preincubation with forskolin did not bring about desensitization to PTH nor did preincubation with PTH affect the subsequent response to forskolin. The half-life of biologically active bovine PTH1-34 in chick kidney cell culture was approximately 12 h and the rate of its removal was not significantly altered during a 20-h incubation period. The results suggest that desensitization of chick kidney cells to PTH is not suggest that desensitization of chick kidney cells to PTH is not brought about by cAMP generation itself, is not primarily dependent on protein synthesis, and does not involve a change in the rate of removal of biologically active hormone from the medium. In addition, recovery of the cAMP response to PTH also does not require new protein synthesis. These results are compatible with a mechanism of desensitization which occurs at the level of the receptor or hormone-receptor coupling to adenyl cyclase.

Animals↗
PubMed1981

Effect of vitamin D status on cyclic AMP-dependent protein kinase activity and its heat-stable inhibitor in chick kidney.

Cyclic AMP-dependent protein kinase activity in supernatants of homogenates of kidneys from vitamin D-deficient chicks is decreased to 70% of the level measured in kidneys from normal chicks. Activity was restored to normal by oral administration of vitamin D or 1,25-dihydroxyvitamin D3 for 1 or 2 weeks. Both isozymes of cAMP-dependent protein kinase were reduced to the same extent by vitamin D deficiency. The decreased enzyme activity could not be accounted for by a shift to the particulate fraction nor by an increased requirement for cyclic AMP. A heat stable, trichloroacetic acid-precipitable, trypsin-labile inhibitor of protein kinase activity was identified and quantitated in kidneys from vitamin D-deficient chicks (16 to 26 units/mg of protein) and from those given vitamin D (2 to 6 units/mg of protein). The measured difference in inhibitor levels could not be attributed to differential stability in kidney homogenates from vitamin D-deficient or -repleted chicks. The observed increase in inhibitor level with vitamin D deficiency is not sufficient to account for the decrease in cyclic AMP-dependent protein kinase activity, suggesting that the total amount of this enzyme activity is reduced in vitamin D deficiency.

Aging↗
PubMed1981

25(OH)D3 metabolism in kidney cell cultures: lack of a direct effect of estradiol.

There are several reports of increased production of 1 alpha,25-dihydroxyvitamin D3 [1,25(OH)2D3] by the kidney of birds in response to estrogen treatment. To determine whether estradiol influences the renal cell directly, primary cultures of chick kidney cells were exposed to the steroid under a variety of conditions. In the absence of 1,25(OH)2D3, treatment of cultures for 20-24 h with 10(-5) and 10(-6) M estradiol led to inhibition of 25-hydroxyvitamin D3 [25(OH)D3]-1-hydroxylase activity. When the 1-hydroxylase was suppressed and 25(OH)2D3-24-hydroxylase was induced by treatment with 1,25(OH)2D3, estradiol in concentrations of 10(-9) and 10(-5) M either had no effect or slightly inhibited 1,25(OH)2D3 production. Similarly, 24R,25-dihydroxyvitamin D3[24,25(OH)2D3] production was not affected consistently by estradiol. These results were unaltered when either testosterone (10(-6) M) or insulin (5 micrograms/ml) was present in the medium. Shorter treatments (0.5, 2, 4, and 8 h) with estradiol resulted in a transient decrease in both 1,25(OH)2D3 and 24,25(OH)2D3 production, but at no time was stimulation observed. These results suggest that the effects of estrogens on 25(OH)D3 metabolism observed in vivo are exerted elsewhere than directly at the renal cell.

Animals↗
PubMed1981

Insulin permits parathyroid hormone stimulation of 1,25-dihydroxyvitamin D3 production in cultured kidney cells.

Primary cultures of chick kidney cells in serum free medium respond to PTH with increased production of 1,25(OH)2D3 only when exposed to insulin. The response of 1,25(OH)2D3 is maximal at 5 ng bPTH (1-34) per ml and decreases at higher hormone concentrations. Increased 1,25(OH)2D3 synthesis is not evident after 30 minutes exposure to bPTH and is maximal at 4-6 hours of treatment. Insulin does not increase the cyclic AMP response to PTH suggesting that whatever permissive role it is playing occurs beyond the generation of cyclic AMP.

Animals↗
PubMed1980

Effects of vitamin D metabolites on bovine parathyroid hormone release in vitro.

We evaluated the effects of 1 alpha,25-dihydroxycholecalciferol (1,25(OH)2D3), 24R,25-dihydroxycholecalciferol (24,25(OH)2D3), and 25-hydroxycholecalciferol (25(OH)D3) on the release of parathyroid hormone (PTH). Bovine parathyroid tissues were incubated in vitro for 4 h in low-calcium (1.0 mM) medium. 1,25(OH)2D3 ((10(-9)-10(-12)M), 24,25(OH)2D3 (10(-6)-10(-8)M), and 25(OH)D3 (5 X 10(-7)-5 X 10(-9)M) inhibited PTH release. Inhibition by all metabolites was concentration and time dependent. On a molar basis, 1,25(OH)2D3 was the most potent metabolite, being at least 100 times more potent than 24,25(OH)2D3 and 25(OH)D3; 24,25(OH)2D3 was about 5 times more potent than 25(OH)D3 at concentrations producing 65% inhibition. Inhibition by high concentrations of metabolites was evident by 1 h of incubation; inhibition was progressive throughout incubation, and maximal suppression to 30-40% of control occurred during the fourth and final hour of incubation. 1,25(OH)2D3 (10(-11) M), a low concentration that did not inhibit secretion, transiently stimulated release. In conclusion, under conditions of low-calcium-stimulated PTH release, 1,25(OH)2D3, 24,25(OH)2D3, and 25(OH)D3 inhibited PTH release, 1,25(OH)2D3 was the most potent inhibitor.

Animals↗
PubMed1980

Recent advances in the understanding of the metabolism and functions of vitamin D.

Many advances have been made in the past several years in our understanding of the metabolism and mechanism of action of vitamin D. Recognition of the clinical implications of this knowledge continues to grow. Despite these gains, however, many questions remain unanswered. These include the role of 24,25(OH)2D3 in physiologic processes, the nature of the contribution of vitamin D metabolism to bone growth and development, the responses of other possible target tissues such as the pancreas and parathyroid gland, and the further elucidation of interactions between vitamin D metabolites and parathyroid hormone in the maintenance of calcium and phosphorus homeostasis. The next decade of research is bound to bring insight into these and other questions.

Bone and Bones↗
PubMed1978

Vitamin D: two dihydroxylated metabolites are required for normal chicken egg hatchability.

When hens are raised to sexual maturity from hatching with 1,25-dihydroxyvitamin D3 [1,25(OH)2D3] as their sole source of cholecalciferol (vitamin D3), fertile eggs appear to develop normally but fail to hatch. When hens receive a combination of 1,25(OH)2D3 and 24R,25-dihydroxyvitamin D3 [24,25(OH)2D3], hatchability equivalent to that with hens given vitamin D3 is obtained. These results suggest a biological role for 24,25(OH)2D3 not previously recognized.

Animals↗