Vitamin D receptor is not required for the rapid actions of 1,25-dihydroxyvitamin D3 to increase intracellular calcium and activate protein kinase C in mouse osteoblasts

The rapid, non‐genomic actions of 1,25‐dihydroxyvitamin D3 [1,25(OH)2D3] have been well described, however, the role of the nuclear vitamin D receptor (VDR) in this pathway remains unclear. To address this question, we used VDR(+/+) and VDR(−/−) osteoblasts isolated from wild‐type and VDR null mice...

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Vydané v:	Journal of cellular biochemistry Ročník 88; číslo 4; s. 794 - 801
Hlavní autori:	Wali, Ramesh K., Kong, Juan, Sitrin, Michael D., Bissonnette, Marc, Li, Yan Chun
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	New York Wiley Subscription Services, Inc., A Wiley Company 01.03.2003
Predmet:	Animals Calcitriol - pharmacology Calcitriol - physiology calcium Calcium - analysis Calcium - metabolism Cells, Cultured Dose-Response Relationship, Drug Enzyme Activation - drug effects Enzyme Inhibitors - pharmacology Indoles - pharmacology Isoenzymes - biosynthesis Maleimides - pharmacology Mice Mice, Knockout non-genomic actions Osteoblasts - drug effects Osteoblasts - physiology Phosphorylation - drug effects protein kinase C Protein Kinase C - analysis Protein Kinase C - antagonists & inhibitors Protein Kinase C - biosynthesis Protein Kinase C - metabolism Receptors, Calcitriol - genetics Receptors, Calcitriol - physiology RNA - analysis RNA - isolation & purification VDR vitamin D
ISSN:	0730-2312, 1097-4644
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Abstract	The rapid, non‐genomic actions of 1,25‐dihydroxyvitamin D3 [1,25(OH)2D3] have been well described, however, the role of the nuclear vitamin D receptor (VDR) in this pathway remains unclear. To address this question, we used VDR(+/+) and VDR(−/−) osteoblasts isolated from wild‐type and VDR null mice to study the increase in intracellular calcium ([Ca2+]i) and activation of protein kinase C (PKC) induced by 1,25(OH)2D3. Within 1 min of 1,25(OH)2D3 (100 nM) treatment, an increase of 58 and 53 nM in [Ca2+]i (n = 3) was detected in VDR(+/+) and VDR(−/−) cells, respectively. By 5 min, 1,25(OH)2D3 caused a 2.1‐ and 1.9‐fold increase (n = 6) in the phosphorylation of PKC substrate peptide acetylated‐MBP4–14 in VDR(+/+) and VDR(−/−) osteoblasts. The 1,25(OH)2D3‐induced phosphorylation was abolished by GF109203X, a general PKC inhibitor, in both cell types, confirming that the secosteroid induced PKC activity. Moreover, 1,25(OH)2D3 treatment resulted in the same degree of translocation of PKC‐α and PKC‐δ, but not of PKC‐ζ, from cytosol to plasma membrane in both VDR(+/+) and VDR(−/−) cells. These experiments demonstrate that the 1,25(OH)2D3‐induced rapid increases in [Ca2+]i and PKC activity are neither mediated by, nor dependent upon, a functional nuclear VDR in mouse osteoblasts. Thus, VDR is not essential for these rapid actions of 1,25(OH)2D3 in osteoblasts. © 2003 Wiley‐Liss, Inc.
AbstractList	The rapid, non‐genomic actions of 1,25‐dihydroxyvitamin D3 [1,25(OH)2D3] have been well described, however, the role of the nuclear vitamin D receptor (VDR) in this pathway remains unclear. To address this question, we used VDR(+/+) and VDR(−/−) osteoblasts isolated from wild‐type and VDR null mice to study the increase in intracellular calcium ([Ca2+]i) and activation of protein kinase C (PKC) induced by 1,25(OH)2D3. Within 1 min of 1,25(OH)2D3 (100 nM) treatment, an increase of 58 and 53 nM in [Ca2+]i (n = 3) was detected in VDR(+/+) and VDR(−/−) cells, respectively. By 5 min, 1,25(OH)2D3 caused a 2.1‐ and 1.9‐fold increase (n = 6) in the phosphorylation of PKC substrate peptide acetylated‐MBP4–14 in VDR(+/+) and VDR(−/−) osteoblasts. The 1,25(OH)2D3‐induced phosphorylation was abolished by GF109203X, a general PKC inhibitor, in both cell types, confirming that the secosteroid induced PKC activity. Moreover, 1,25(OH)2D3 treatment resulted in the same degree of translocation of PKC‐α and PKC‐δ, but not of PKC‐ζ, from cytosol to plasma membrane in both VDR(+/+) and VDR(−/−) cells. These experiments demonstrate that the 1,25(OH)2D3‐induced rapid increases in [Ca2+]i and PKC activity are neither mediated by, nor dependent upon, a functional nuclear VDR in mouse osteoblasts. Thus, VDR is not essential for these rapid actions of 1,25(OH)2D3 in osteoblasts. © 2003 Wiley‐Liss, Inc. The rapid, non-genomic actions of 1,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)] have been well described, however, the role of the nuclear vitamin D receptor (VDR) in this pathway remains unclear. To address this question, we used VDR(+/+) and VDR(-/-) osteoblasts isolated from wild-type and VDR null mice to study the increase in intracellular calcium ([Ca(2+)](i)) and activation of protein kinase C (PKC) induced by 1,25(OH)(2)D(3). Within 1 min of 1,25(OH)(2)D(3) (100 nM) treatment, an increase of 58 and 53 nM in [Ca(2+)](i) (n = 3) was detected in VDR(+/+) and VDR(-/-) cells, respectively. By 5 min, 1,25(OH)(2)D(3) caused a 2.1- and 1.9-fold increase (n = 6) in the phosphorylation of PKC substrate peptide acetylated-MBP(4-14) in VDR(+/+) and VDR(-/-) osteoblasts. The 1,25(OH)(2)D(3)-induced phosphorylation was abolished by GF109203X, a general PKC inhibitor, in both cell types, confirming that the secosteroid induced PKC activity. Moreover, 1,25(OH)(2)D(3) treatment resulted in the same degree of translocation of PKC-alpha and PKC-delta, but not of PKC-zeta, from cytosol to plasma membrane in both VDR(+/+) and VDR(-/-) cells. These experiments demonstrate that the 1,25(OH)(2)D(3)-induced rapid increases in [Ca(2+)](i) and PKC activity are neither mediated by, nor dependent upon, a functional nuclear VDR in mouse osteoblasts. Thus, VDR is not essential for these rapid actions of 1,25(OH)(2)D(3) in osteoblasts.The rapid, non-genomic actions of 1,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)] have been well described, however, the role of the nuclear vitamin D receptor (VDR) in this pathway remains unclear. To address this question, we used VDR(+/+) and VDR(-/-) osteoblasts isolated from wild-type and VDR null mice to study the increase in intracellular calcium ([Ca(2+)](i)) and activation of protein kinase C (PKC) induced by 1,25(OH)(2)D(3). Within 1 min of 1,25(OH)(2)D(3) (100 nM) treatment, an increase of 58 and 53 nM in [Ca(2+)](i) (n = 3) was detected in VDR(+/+) and VDR(-/-) cells, respectively. By 5 min, 1,25(OH)(2)D(3) caused a 2.1- and 1.9-fold increase (n = 6) in the phosphorylation of PKC substrate peptide acetylated-MBP(4-14) in VDR(+/+) and VDR(-/-) osteoblasts. The 1,25(OH)(2)D(3)-induced phosphorylation was abolished by GF109203X, a general PKC inhibitor, in both cell types, confirming that the secosteroid induced PKC activity. Moreover, 1,25(OH)(2)D(3) treatment resulted in the same degree of translocation of PKC-alpha and PKC-delta, but not of PKC-zeta, from cytosol to plasma membrane in both VDR(+/+) and VDR(-/-) cells. These experiments demonstrate that the 1,25(OH)(2)D(3)-induced rapid increases in [Ca(2+)](i) and PKC activity are neither mediated by, nor dependent upon, a functional nuclear VDR in mouse osteoblasts. Thus, VDR is not essential for these rapid actions of 1,25(OH)(2)D(3) in osteoblasts. The rapid, non-genomic actions of 1,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)] have been well described, however, the role of the nuclear vitamin D receptor (VDR) in this pathway remains unclear. To address this question, we used VDR(+/+) and VDR(-/-) osteoblasts isolated from wild-type and VDR null mice to study the increase in intracellular calcium ([Ca(2+)](i)) and activation of protein kinase C (PKC) induced by 1,25(OH)(2)D(3). Within 1 min of 1,25(OH)(2)D(3) (100 nM) treatment, an increase of 58 and 53 nM in [Ca(2+)](i) (n = 3) was detected in VDR(+/+) and VDR(-/-) cells, respectively. By 5 min, 1,25(OH)(2)D(3) caused a 2.1- and 1.9-fold increase (n = 6) in the phosphorylation of PKC substrate peptide acetylated-MBP(4-14) in VDR(+/+) and VDR(-/-) osteoblasts. The 1,25(OH)(2)D(3)-induced phosphorylation was abolished by GF109203X, a general PKC inhibitor, in both cell types, confirming that the secosteroid induced PKC activity. Moreover, 1,25(OH)(2)D(3) treatment resulted in the same degree of translocation of PKC-alpha and PKC-delta, but not of PKC-zeta, from cytosol to plasma membrane in both VDR(+/+) and VDR(-/-) cells. These experiments demonstrate that the 1,25(OH)(2)D(3)-induced rapid increases in [Ca(2+)](i) and PKC activity are neither mediated by, nor dependent upon, a functional nuclear VDR in mouse osteoblasts. Thus, VDR is not essential for these rapid actions of 1,25(OH)(2)D(3) in osteoblasts.
Author	Bissonnette, Marc Wali, Ramesh K. Sitrin, Michael D. Li, Yan Chun Kong, Juan
Author_xml	– sequence: 1 givenname: Ramesh K. surname: Wali fullname: Wali, Ramesh K. organization: Evanston Northwestern Healthcare, Evanston, Illinois 60201 – sequence: 2 givenname: Juan surname: Kong fullname: Kong, Juan organization: Department of Medicine, University of Chicago, Chicago, Illinois 60637 – sequence: 3 givenname: Michael D. surname: Sitrin fullname: Sitrin, Michael D. organization: Department of Medicine, University of Chicago, Chicago, Illinois 60637 – sequence: 4 givenname: Marc surname: Bissonnette fullname: Bissonnette, Marc organization: Department of Medicine, University of Chicago, Chicago, Illinois 60637 – sequence: 5 givenname: Yan Chun surname: Li fullname: Li, Yan Chun email: cyan@medicine.bsd.uchicago.edu organization: Department of Medicine, University of Chicago, Chicago, Illinois 60637
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References_xml	– reference: Erben RG, Soegiarto DW, Weber K, Zeitz U, Lieberherr M, Gniadecki R, Moller G, Adamski J, Balling R. 2002. Deletion of deoxyribonucleic acid binding domain of the vitamin D receptor abrogates genomic and nongenomic functions of vitamin D. Mol Endocrinol 16: 1524-1537. – reference: Zanello LP, Norman AW. 1997. Stimulation by 1alpha,25(OH)2-vitamin D3 of whole cell chloride currents in osteoblastic ROS 17/2.8 cells. A structure-function study. J Biol Chem 272: 22617-22622. – reference: Baran DT, Quail JM, Ray R, Leszyk J, Honeyman T. 2000. Annexin II is the membrane receptor that mediates the rapid actions of 1alpha,25-dihydroxyvitamin D(3). J Cell Biochem 78: 34-46. – reference: Baum CL, Wali RK, Sitrin MD, Bolt MJ, Brasitus TA. 1990. 1,2-Dimethylhydrazine-induced alterations in protein kinase C activity in the rat preneoplastic colon. Cancer Res 50: 3915-3920. – reference: Caffrey JM, Farach-Carson MC. 1989. 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start-page: 1269 year: 1991 end-page: 1275 article-title: 1a,25‐Dihydroxyvitamin D3 rapidly increases cytosolic calcium in clonal rat osteosarcoma cells lacking the vitamin D receptor publication-title: J Bone Miner Res – volume: 85 start-page: 1296 year: 1990 end-page: 1303 article-title: 1,25(OH) vitamin D3 stimulates membrane phosphoinositide turnover, activates protein kinase C, and increases cytosolic calcium in rat colonic epithelium publication-title: J Clin Invest – volume: 66 start-page: 457 year: 1997 end-page: 470 article-title: Hybrid structural analogues of 1,25‐(OH) D regulate chondrocyte proliferation and proteoglycan production as well as protein kinase C through a nongenomic pathway publication-title: J Cell Biochem – volume: 16 start-page: 1524 year: 2002 end-page: 1537 article-title: Deletion of deoxyribonucleic acid binding domain of the vitamin D receptor abrogates genomic and nongenomic functions of vitamin D publication-title: Mol Endocrinol – volume: 13 start-page: 1360 year: 1998 end-page: 1369 article-title: Receptors for 1alpha,25(OH) D : Past, present, and future [editorial; comment] publication-title: J Bone Miner Res – start-page: 233 year: 1997 end-page: 256 – volume: 260 start-page: 3440 year: 1985 end-page: 3450 article-title: A new generation of Ca indicators with greatly improved fluorescence properties publication-title: J Biol Chem – volume: 137 start-page: 3649 year: 1996 end-page: 3658 article-title: Association of 1 alpha,25‐dihydroxyvitamin D3‐occupied vitamin D receptors with cellular membrane acceptance sites publication-title: Endocrinology – volume: 222 start-page: 61 year: 1996 end-page: 69 article-title: 1,25‐Dihydroxyvitamin D3 primes acute promyelocytic cells for TPA‐induced monocytic differentiation through both PKC and tyrosine phosphorylation cascades publication-title: Exp Cell Res – volume: 269 start-page: 23750 year: 1994 end-page: 23756 article-title: Identification of a specific binding protein for 1a,25‐dihydroxyvitamin D3 in basal‐lateral membranes of chick intestinal epithelium and relationship to transcaltachia publication-title: J Biol Chem – volume: 66 start-page: 147 year: 2001 end-page: 158 article-title: Different shapes of the steroid hormone 1alpha,25(OH)(2)‐vitamin D(3) act as agonists for two different receptors in the vitamin D endocrine system to mediate genomic and rapid responses publication-title: Steroids – volume: 56 start-page: 510 year: 1994 end-page: 517 article-title: Binding characteristics of a membrane receptor that recognizes 1 alpha,25‐dihydroxyvitamin D3 and its epimer, 1 beta,25‐dihydroxyvitamin D3 publication-title: J Cell Biochem – volume: 267 start-page: G465 year: 1994 end-page: G475 article-title: 1,25(OH) vitamin D3 activates PKC‐alpha in Caco‐2 cells: A mechanism to limit secosteroid‐induced rise in [Ca ]i publication-title: Am J Physiol – volume: 86 start-page: 128 year: 2002 end-page: 135 article-title: 1,25(OH) ‐vitamin D3 induces translocation of the vitamin D receptor (VDR) to the plasma membrane in skeletal muscle cells publication-title: J Cell Biochem – volume: 227 start-page: 680 year: 1970 end-page: 685 article-title: Cleavage of structural proteins during the assembly of the head of bacteriophage T4 publication-title: Nature
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Snippet	The rapid, non‐genomic actions of 1,25‐dihydroxyvitamin D3 [1,25(OH)2D3] have been well described, however, the role of the nuclear vitamin D receptor (VDR) in... The rapid, non-genomic actions of 1,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)] have been well described, however, the role of the nuclear vitamin D receptor...
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SubjectTerms	Animals Calcitriol - pharmacology Calcitriol - physiology calcium Calcium - analysis Calcium - metabolism Cells, Cultured Dose-Response Relationship, Drug Enzyme Activation - drug effects Enzyme Inhibitors - pharmacology Indoles - pharmacology Isoenzymes - biosynthesis Maleimides - pharmacology Mice Mice, Knockout non-genomic actions Osteoblasts - drug effects Osteoblasts - physiology Phosphorylation - drug effects protein kinase C Protein Kinase C - analysis Protein Kinase C - antagonists & inhibitors Protein Kinase C - biosynthesis Protein Kinase C - metabolism Receptors, Calcitriol - genetics Receptors, Calcitriol - physiology RNA - analysis RNA - isolation & purification VDR vitamin D
Title	Vitamin D receptor is not required for the rapid actions of 1,25-dihydroxyvitamin D3 to increase intracellular calcium and activate protein kinase C in mouse osteoblasts
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