1,25-Dihydroxyvitamin D increases calmodulin binding to specific proteins in the chick duodenal brush border membrane.

Bikle, Daniel D.; Munson, Scott

doi:10.1172/jci112241

Cited by 39 publications

(12 citation statements)

References 36 publications

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“…The high degree of localization suggests the existence of high capacity Ca-binding components. Other studies (Bikle and Munson 1985;Bikle et al 1984;Kaune et al 1994) have suggested a possible role for this complex in the 1,25(OH) 2 D 3 -stimulated Ca uptake across the brush border membrane. Much of the brush border calmodulin is known to be associated with a 110-kDa (variously reported as 102-110 kDa) calmodulin-binding protein, the brush border myosin I, which exhibits ATPase activity and mechanoenzyme properties (Mooseker et al 1991).…”

Section: Discussionmentioning

confidence: 91%

Ion microscopic imaging of calcium during 1,25-dihydroxyvitamin D-mediated intestinal absorption

Fullmer

Chandra

Smith

et al. 1996

Histochem Cell Biol

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A combination of ion microscopic and conventional radionuclide techniques was employed to investigate the temporal-spatial dynamics of 1,25-dihydroxyvitamin D3 [1,25(OH)2D3]-stimulated intestinal calcium (Ca) absorption. At varying times following the administration of a single intravenous dose of 1,25(OH)2D3 to vitamin D-deficient chicks, transepithelial transport and tissue retention of Ca were quantitated in vivo, using the ligated duodenal loop technique and 47Ca as the tracer. The localization of Ca in the intestinal tissue during absorption was monitored by ion microscopy, using the stable Ca isotope, 44Ca, as the absorbed species. There was little transepithelial absorption of Ca in the vitamin D-deficient animals despite a substantial tissue accumulation of luminally derived Ca, the latter localizing predominantly in the brush border region of the enterocyte, as shown by the 44Ca-ion microscopic images. The early (30 min-1 h) response to 1,25(OH)2D3 was an increased tissue uptake of luminal 47Ca, which also primarily associated with the brush border region, again as shown by ion microscopy. At 2-4 h after the 1,25(OH)2D3 dose, there was a progressive redistribution of Ca from the brush border region throughout the cytoplasm and into the lamina propria. At 8-16 h, 47Ca absorption was maximal and 44Ca was sparsely distributed in the intestinal tissue. 47Ca absorption gradually declined and reached pre-dose levels by 72 h. At this time, tissue 44Ca was again largely limited to the brush border region. These results provide support for the multiple actions of 1,25(OH)2D3 on the intestinal Ca absorption process. The ion microscopic images provided unique information on the specific time-dependent changes in the tissue localization of Ca during the process of its intestinal absorption as affected by 1,25(OH)2D3.

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Section: Discussionmentioning

confidence: 91%

Ion microscopic imaging of calcium during 1,25-dihydroxyvitamin D-mediated intestinal absorption

Fullmer

Chandra

Smith

et al. 1996

Histochem Cell Biol

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“…4 and Ref. 2) may result from the more highly purified nature of luminal and basolateral membrane preparations. Moreover, the presence of renal CaMBP-D110 in luminal membranes suggests that this CaMBP-D may be similar to 110-kDa chick intestinal BBM 1 (5,6,21). However, whether there is any association of luminal membrane CaMBP-D74 with CaMBP-D110 and its functions remains a question for future studies.…”

Section: Discussionmentioning

confidence: 98%

“…2). Two CaMBPs related to functions of vitamin D (4,5,12,22,46) were previously localized to specific cellular membrane poles, i.e., the 136-kDa plasma membrane Ca 2ϩ -ATPase in renal basolateral membranes (8,19,35) and the 110-Da brush-border myosin 1 (BBM 1) protein in luminal membranes of chick intestinal cells (5, 6, 21). Thus it was important to determine whether the CaMBP-Ds could be detected in purified renal basolateral and luminal membrane preparations.…”

Section: Discussionmentioning

confidence: 99%

1,25-Dihydroxyvitamin D-stimulated calmodulin binding proteins: a sustained effect on distal tubules

Siaw

Walters

2002

American Journal of Physiology-Renal Physiology

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(CaMBP-Ds) in the rat kidney and the specificity of their induction were characterized to better understand renal responses to protracted 1,25(OH) 2D3 treatment in vivo. None of the other hormones tested (parathyroid hormone, calcitonin, estradiol-17␤, testosterone, progesterone, hydrocortisone, or dexamethasone) stimulated the CaMBP-Ds, whereas maximal 1,25(OH) 2D3 stimulation occurred after a 5-to 7-day treatment with 100 ng/day 1,25(OH) 2D3. With the exception of the more ubiquitously distributed CaMBP-D150, the CaMBP-Ds were localized in distal, but not proximal, tubule preparations. 1,25(OH) 2D3 MATERIALS AND METHODS Animals.Male weanling rats (21 days old, Sprague-Dawley strain, Charles River, Madison, WI) were housed in incandescent light and fed a vitamin D-deficient (ϪD) diet containing 2.0% calcium, 1.25% phosphorous, and 20% lactose (TD 87095, Teklad, Madison, WI). This dietary regimen results in ϪD with normocalcemia after 6-8 wk, which is sustained for at least 4-5 mo (26,27). In these studies, rats were maintained on the ϪD diet for 7 wk-5 mo before hor-

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“…1,25-(OH)2D3 did not increase TSH secretion induced by K+ depolarisation. induc¬ tion of transcellular calcium transport (Bikle & Munson 1985). This could indicate that l,25(OH)2D3 enhances the mecha¬ nism responsible for the TRH-induced TSH re¬ lease.…”

Section: Discussionmentioning

confidence: 99%

Effect of 1,25-dihydroxyvitamin D3 on TSH secretion from rat pituitary cells in culture

Törnquist

Lamberg‐Allardt

1987

Acta Endocrinologica

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The effect of 1,25-dihydroxyvitamin D3 ( 1,25(OH)2D3) on TSH secretion from rat pituitary cells was studied. When incubating cells with 1,25(OH)2D3 even at 100 \m=x\ the physiological concentrations (10\m=-\8), no effect on basal TSH secretion was observed. The TRH-induced TSH secretion increased after a 24-h incubation with 10\m=-\8mol/l 1,25(OH)2D3 (2.9 \m=+-\0.2 ng/well vs 4.3 \m=+-\0.5 ng/well, mean \m=+-\ sd; P < 0.05).When serum was omitted from the incubation medium, the potentiating effect of 1,25(OH)2D3 on the TRH-induced TSH release was blunted. No effect on cellular protein content was observed after incubating the cells with 10\m=-\8mol/l 1,25(OH)2D3. The results indicate that at unphysiological concentrations, 1,25(OH)2D3 affects the TRH-induced TSH secretion from pituitary cells.The physiological significance remains unclear.

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1,25-Dihydroxyvitamin D increases calmodulin binding to specific proteins in the chick duodenal brush border membrane.

Abstract: In previous studies we demonstrated that the biologically active

Cited by 39 publications

References 36 publications

Ion microscopic imaging of calcium during 1,25-dihydroxyvitamin D-mediated intestinal absorption

Ion microscopic imaging of calcium during 1,25-dihydroxyvitamin D-mediated intestinal absorption

1,25-Dihydroxyvitamin D-stimulated calmodulin binding proteins: a sustained effect on distal tubules

Effect of 1,25-dihydroxyvitamin D3 on TSH secretion from rat pituitary cells in culture

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