Dissociation of cAMP accumulation and phosphate uptake in opossum kidney (OK) cells with parathyroid hormone (PTH) and parathyroid hormone related protein (PTHrP)

Muff, Roman; Caulfield, Michael P.; Fischer, Jan A.

doi:10.1016/0196-9781(90)90014-v

Cited by 14 publications

(6 citation statements)

References 16 publications

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“…A dual mechanism for the regulation of P uptake and the existence of two receptors for PTH in oppossum kidney cells has been postulated (Cole, Eber, Poelling, Thorne & Forte, 1987). Some recent results are consistent with the hypothesis that high and low affinity receptors and/or second messengers besides cAMP are necessary for PTH/PTHrP-regulated P kidney transport (Muff, Caulfield & Fischer, 1990). …”

Section: Discussionsupporting

confidence: 68%

Parathyroid hormone‐related peptide increases urinary phosphate excretion in fetal lambs

Davicco¹,

Coxam²,

Lefaivre³

et al. 1992

Experimental Physiology

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Section: Discussionsupporting

confidence: 68%

Parathyroid hormone‐related peptide increases urinary phosphate excretion in fetal lambs

Davicco¹,

Coxam²,

Lefaivre³

et al. 1992

Experimental Physiology

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“…It is therefore possible that the already inhibited phosphate transport is not further affected by these changes in CAMP. Other studies have also shown a dissociation between PTHstimulated cAMP accumulation and the inhibition of phosphate transport in OK cells (Cole et al, 1987;Muff et al, 1990). Intermediaries other than cAMP may be involved in the control of phosphate transport.…”

Section: Discussionmentioning

confidence: 95%

Identification of estrogen receptor mRNA and the estrogen modulation of parathyroid hormone‐stimulated cyclic AMP accumulation in opossum kidney cells

Stock

Coderre

Burke

et al. 1992

Journal Cellular Physiology

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The opossum kidney (OK) cell was used as a model to test the hypothesis that estrogen directly affects proximal renal tubular epithelial cells. To demonstrate the expression of estrogen receptor in OK cells, we developed an approach using reverse transcription and the polymerase chain reaction. Analysis of the DNA amplified with nested primers revealed the predicted size fragment and restriction enzyme digestion products. To demonstrate the functional effects of estrogen, OK cells at confluence were preincubated in serum-free medium for 7-10 days with or without 17 beta-estradiol. Bovine PTH(1-34) (bPTH(1-34)) then stimulated a dose-dependent intracellular accumulation of cAMP that was maximal after 1 min and then gradually declined. Cyclic AMP in the medium slowly increased over 60 min. Preincubation with 17 beta-estradiol did not affect cell proliferation as measured by total protein content but caused an inhibition of bPTH(1-34)-stimulated intracellular cAMP accumulation that was maximal at 10(-11) M 17 beta-estradiol (71 +/- 3% control, p less than .001). bPTH(1-34) also increased cAMP release into the medium, an effect maximal using 10(-10) M 17 beta-estradiol (118 +/- 3% control, p less than .001). Preincubation with the inactive isomer 17 alpha-estradiol caused no changes in cAMP accumulation or release. Coincubation with the antiestrogen tamoxifen blocked the effects of 17 beta-estradiol. Sodium-dependent phosphate transport was: (1) inhibited by 2-h incubations with 10(-8) or 10(-10) M bPTH(1-34) and not affected by preincubation with 17 beta-estradiol, and (2) not inhibited by a 20-min incubation with 10(-8) M bPTH(1-34) unless cells were preincubated with 10(-8) M 17 beta-estradiol, suggesting that any possible effects of estrogen on phosphate transport are not directly mediated by changes in cAMP. These studies demonstrate the presence of estrogen receptor mRNA in OK cells as well as direct and specific effects of physiologic concentrations of estrogen on cAMP accumulation in these cells. This system may be a good model for further study of estrogen and PTH effects on the kidney.

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“…Stimulation of cAMP production was done essentially according to Muff et al . ( 21 ) . Briefly, confluent cells were washed once with 500 μl of culture medium containing 1% BSA.…”

Section: Methodsmentioning

confidence: 99%

Scutellaria barbata D. Don induces c-fos gene expression in human uterine leiomyomal cells by activating beta2-adrenergic receptors

Lee

Cho

Kim

et al. 2004

Int J Gynecol Cancer

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Scutellaria barbata D. Don (Lamiaceae; SB) inhibited the growth of uterine leiomyomal (LM) cells with unknown actions. The expression patterns of beta-adrenergic receptors (beta-ARs) in human uterine LM cells and functional coupling to gene expression have also been investigated. Northern blot analysis showed that beta-AR subtypes are expressed at different levels in the uterine LM cells and myometrial smooth muscle cells (SMCs). beta1-AR expression was to be found approximately at the same level in the two cell types. beta2-ARs were expressed at higher levels in uterine LM cells than that in myometrial SMCs. beta3-AR expression was not found in both the cells. c-fos gene expression was induced by SB in uterine LM cells via increases in adenosine-3',5', cyclic monophosphate (cAMP), which in turn activated the cAMP/protein kinase A (PKA) pathway. The PKA inhibitor, H89, inhibited c-fos gene expression induced by SB. It seems that the mechanism of proto-oncogenes c-fos different leiomyoma from other myometrial cancer. Further studies are necessary to elucidate whether c-fos induction by SB in uterine LM cells influences a regression of leiomyoma or induces other differentiation.

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Dissociation of cAMP accumulation and phosphate uptake in opossum kidney (OK) cells with parathyroid hormone (PTH) and parathyroid hormone related protein (PTHrP)

Cited by 14 publications

References 16 publications

Parathyroid hormone‐related peptide increases urinary phosphate excretion in fetal lambs

Parathyroid hormone‐related peptide increases urinary phosphate excretion in fetal lambs

Identification of estrogen receptor mRNA and the estrogen modulation of parathyroid hormone‐stimulated cyclic AMP accumulation in opossum kidney cells

Scutellaria barbata D. Don induces c-fos gene expression in human uterine leiomyomal cells by activating beta2-adrenergic receptors

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