Effect of Follicle-Stimulating Hormone and Estrogen on the Expression of Betaglycan Messenger Ribonucleic Acid Levels in Cultured Rat Granulosa Cells

Abstract Betaglycan (TGFβ type III receptor) was recently identified as a coreceptor to enhance the binding of inhibin A to activin type II receptor. This inhibin/betaglycan/activin type II receptor complex prevents activins from binding to their own receptors. The present study was undertaken to identify the expression and the regulation of the betaglycan gene in cultured rat granulosa cells. Northern blot analysis indicated betaglycan mRNA transcript of approximately 6.4 kbp. The treatment of the cells with FSH increased the betaglycan mRNA level, and a concurrent treatment with estradiol brought a significant increase in betaglycan mRNA. The protein kinase A activator, 8-bromoadenosine-cAMP, also increased the expression of its mRNA. Furthermore, betaglycan mRNA was induced additively by estradiol, which was blocked by estrogen receptor antagonists [ICI 182780, (R, R)-cis-diethyltetrahydro-2,8-chrysenediol]. In the luciferase assay, FSH altered the promoter activity of betaglycan. Moreover, when FSH plus estradiol was added to the granulosa cells, a significant increase in the half-life of betaglycan mRNA transcript was seen. In summary, FSH and estradiol increased betaglycan mRNA expression, most possibly through the protein kinase A pathway and the estrogen receptor-β. The increase of betaglycan mRNA was due to an increase in transcription and altered mRNA stability. In ovarian regulatory function, the expression of betaglycan may involve the functional antagonism of inhibin A in activin signal transduction.

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A-Kinase anchoring protein-13 (AKAP13) may be required for protein kinase A (PKA)-mediated aromatase Expression in granulosa cells

Fertility and Sterility ◽

10.1016/j.fertnstert.2017.07.328 ◽

2017 ◽

Vol 108 (3) ◽

pp. e107

Author(s):

K. C. Cayton Vaught ◽

P. Driggers ◽

J. Segars

Keyword(s):

Protein Kinase ◽

Protein Kinase A ◽

Granulosa Cells ◽

Aromatase Expression ◽

Anchoring Protein ◽

Kinase A

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Spatial targeting of type II protein kinase A to filopodia mediates the regulation of growth cone guidance by cAMP

The Journal of Cell Biology ◽

10.1083/jcb.200607128 ◽

2007 ◽

Vol 176 (1) ◽

pp. 101-111 ◽

Cited By ~ 28

Author(s):

Jianzhong Han ◽

Liang Han ◽

Priyanka Tiwari ◽

Zhexing Wen ◽

James Q. Zheng

Keyword(s):

Protein Kinase ◽

Protein Kinase A ◽

Growth Cone ◽

Regulatory Protein ◽

Cyclic Adenosine Monophosphate ◽

Spatial Localization ◽

Adenosine Monophosphate ◽

Type Ii ◽

Regulation Of Growth ◽

Kinase A

The second messenger cyclic adenosine monophosphate (cAMP) plays a pivotal role in axonal growth and guidance, but its downstream mechanisms remain elusive. In this study, we report that type II protein kinase A (PKA) is highly enriched in growth cone filopodia, and this spatial localization enables the coupling of cAMP signaling to its specific effectors to regulate guidance responses. Disrupting the localization of PKA to filopodia impairs cAMP-mediated growth cone attraction and prevents the switching of repulsive responses to attraction by elevated cAMP. Our data further show that PKA targets protein phosphatase-1 (PP1) through the phosphorylation of a regulatory protein inhibitor-1 (I-1) to promote growth cone attraction. Finally, we find that I-1 and PP1 mediate growth cone repulsion induced by myelin-associated glycoprotein. These findings demonstrate that the spatial localization of type II PKA to growth cone filopodia plays an important role in the regulation of growth cone motility and guidance by cAMP.

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H89, an inhibitor of protein kinase A (PKA), stimulates Na+ transport by translocating an epithelial Na+ channel (ENaC) in fetal rat alveolar type II epithelium

Biochemical Pharmacology ◽

10.1016/s0006-2952(03)00456-8 ◽

2003 ◽

Vol 66 (6) ◽

pp. 1083-1089 ◽

Cited By ~ 22

Author(s):

Yoshinori Marunaka ◽

Naomi Niisato

Keyword(s):

Protein Kinase ◽

Protein Kinase A ◽

Na Channel ◽

Alveolar Type ◽

Type Ii ◽

Na Transport ◽

Fetal Rat ◽

Epithelial Na Channel ◽

Kinase A

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Differential Localization of Protein Kinase A Type II Isozymes in the Golgi–Centrosomal Area

Experimental Cell Research ◽

10.1006/excr.1999.4447 ◽

1999 ◽

Vol 249 (1) ◽

pp. 131-146 ◽

Cited By ~ 33

Author(s):

Guy Keryer ◽

Bjørn S. Skålhegg ◽

Brynjar F. Landmark ◽

Vidar Hansson ◽

Tore Jahnsen ◽

...

Keyword(s):

Protein Kinase ◽

Protein Kinase A ◽

Type Ii ◽

Differential Localization ◽

Kinase A

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Regulation of expression of type II sodium-phosphate cotransporters by protein kinases A and C

AJP Renal Physiology ◽

10.1152/ajprenal.1998.275.2.f270 ◽

1998 ◽

Vol 275 (2) ◽

pp. F270-F277 ◽

Cited By ~ 14

Author(s):

Eleanor D. Lederer ◽

Sameet S. Sohi ◽

Jeanine M. Mathiesen ◽

Jon B. Klein

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Protein Kinase A ◽

Sodium Phosphate ◽

Broad Band ◽

Confocal Imaging ◽

Type Ii ◽

Ok Cells ◽

Kinase C ◽

Kinase A

The purpose of the present study was to determine the effect of protein kinase A and protein kinase C activation on the membrane expression of NaPi-4, the type II sodium-phosphate cotransporter in OK cells. NaPi-4 expression was measured using polyclonal antisera produced in rabbits against a peptide identical to the carboxy-terminal 12-amino acid sequence of NaPi-4. The antisera identified an apically localized protein by confocal imaging of intact OK cells and a broad band of 110–140 kDa by immunoblot analysis of OK cell membranes. Treatment of OK cells with parathyroid hormone (PTH) decreased the intensity of the 110- to 140-kDa band, which was detectable by 2 h, maximal by 4 h at 62%, and sustained for 24 h. 8-Bromo-cAMP (8-BrcAMP) inhibited NaPi-4 expression for up to 24 h by over 90%. However, phorbol 12-myristate 13-acetate inhibited NaPi-4 expression by less than 10%. PTH-(3–34), a fragment which stimulates only protein kinase C, inhibited phosphate transport but also had no effect on NaPi-4 expression. We conclude that protein kinase A but not protein kinase C inhibits sodium-phosphate uptake in OK cells by downregulation of NaPi-4 expression.

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Interleukin-1 alpha stimulates dopamine release by activating type II protein kinase A in PC-12 cells

AJP Endocrinology and Metabolism ◽

10.1152/ajpendo.1995.269.6.e1083 ◽

1995 ◽

Vol 269 (6) ◽

pp. E1083-E1088

Author(s):

A. Joseph ◽

A. Kumar ◽

N. A. O'Connell ◽

R. K. Agarwal ◽

A. R. Gwosdow

Keyword(s):

Protein Kinase ◽

Protein Kinase A ◽

Dopamine Release ◽

Interleukin 1 ◽

Intracellular Camp ◽

Type I ◽

Camp Accumulation ◽

Type Ii ◽

Pc 12 Cells ◽

Kinase A

A recent study from this laboratory [A. R. Gwosdow, N. A. O'Connell, and A. B. Abou-Samra. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E461-E466, 1992] showed that the inflammatory mediator interleukin-1 alpha (IL-1 alpha) stimulates catecholamine release from primary cultures of rat adrenal cells. The present studies were conducted to determine whether 1) IL-1 alpha stimulates catecholamine/dopamine release from the adrenal medullary cell line PC-12 and 2) the adenosine 3',5'-cyclic monophosphate (cAMP)-protein kinase A (PKA) pathway is involved in IL-1 alpha-induced dopamine release from PC-12 cells. The results indicate that IL-1 alpha significantly (P < 0.05) elevated dopamine release after a 24-h incubation period. IL-1 alpha did not stimulate cAMP accumulation at any time period between 5 min and 2 h. In contrast, forskolin-treated cells elevated (P < 0.05) intracellular cAMP levels and increased dopamine release. Because IL-1 alpha did not affect cAMP accumulation, the effect of IL-1 alpha on PKA activity was investigated. IL-1 alpha increased (P < 0.05) PKA activity at 15 and 30 min and returned to control levels by 1 h. Forskolin also increased (P < 0.05) PKA activity. The type of PKA activated (P < 0.05) by IL-1 alpha was type II PKA. In contrast, forskolin activated (P < 0.05) type I and type II PKA. Inhibition of PKA with the PKA inhibitor H-8 blocked PKA activity and dopamine secretion by both IL-1 alpha and forskolin in PC-12 cells. These observations demonstrate that 1) IL-1 alpha stimulated dopamine release from PC-12 cells by activating PKA, 2) the mechanism of IL-1 alpha activation of PKA does not involve detectable increases in intracellular cAMP accumulation, and 3) IL-1 alpha activates type II PKA, which is used by IL-1 alpha to stimulate dopamine secretion from PC-12 cells.

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