Activation of Both Protein Kinase A (PKA) Type I and PKA Type II Isozymes Is Required for Retinoid-Induced Maturation of Acute Promyelocytic Leukemia Cells

2013 ◽  
Vol 83 (5) ◽  
pp. 1057-1065 ◽  
Author(s):  
Eric Nguyen ◽  
Gro Gausdal ◽  
Jacqueline Varennes ◽  
Frédéric Pendino ◽  
Michel Lanotte ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Acute Promyelocytic Leukemia ◽  
Promyelocytic Leukemia ◽  
Leukemia Cells ◽  
Type I ◽  
Type Ii ◽  
Kinase A

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

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.

scholarly journals Identification of a Novel Protein Kinase A Anchoring Protein That Binds Both Type I and Type II Regulatory Subunits

1997 ◽  
Vol 272 (12) ◽  
pp. 8057-8064 ◽  
Author(s):  
Lily Jun-shen Huang ◽  
Kyle Durick ◽  
Joshua A. Weiner ◽  
Jerold Chun ◽  
Susan S. Taylor
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Type I ◽  
Type Ii ◽  
Regulatory Subunits ◽  
Anchoring Protein ◽  
Kinase A ◽  
Novel Protein

scholarly journals Protein Kinase A Type I and Type II Define Distinct Intracellular Signaling Compartments

2008 ◽  
Vol 103 (8) ◽  
pp. 836-844 ◽  
Author(s):  
Giulietta Di Benedetto ◽  
Anna Zoccarato ◽  
Valentina Lissandron ◽  
Anna Terrin ◽  
Xiang Li ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Intracellular Signaling ◽  
Type I ◽  
Type Ii ◽  
Kinase A

Type II protein kinase A regulates CFTR in airway, pancreatic, and intestinal cells

1998 ◽  
Vol 274 (3) ◽  
pp. C819-C826 ◽  
Author(s):  
Wendy K. Steagall ◽  
Thomas J. Kelley ◽  
Rebecca J. Marsick ◽  
Mitchell L. Drumm
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Type I ◽  
Transmembrane Conductance Regulator ◽  
Type Ii ◽  
Transmembrane Conductance ◽  
Apparent Paradox ◽  
Calcium Dependent ◽  
Cellular Compartments ◽  
Kinase A

The type of protein kinase A (PKA) responsible for cystic fibrosis transmembrane conductance regulator (CFTR) activation was determined with adenosine 3′,5′-cyclic monophosphate analogs capable of selectively activating type I or type II PKA. The type II-selective pair stimulated chloride efflux in airway, pancreatic, and colonic epithelial cells; the type I-selective pair only stimulated a calcium-dependent efflux in airway cells. The type II-selective analogs activated larger increases in CFTR-mediated current than did the type I-selective analogs. Measurement of soluble PKA activity demonstrated similar levels stimulated by type I- and type II-selective analogs, creating an apparent paradox regarding PKA activity and current generated. Also, addition of forskolin after the type I-selective analogs resulted in an increase in current; little increase was seen after the type II-selective analogs. Measurement of insoluble PKA activity stimulated by the analogs resolved this paradox. Type II-selective analogs stimulated three times as much insoluble PKA activity as the type I-selective pair, indicating that differential activation of PKA in cellular compartments is important in CFTR regulation.

106 EXPRESSION PATTERNS OF PROTEIN KINASE A SUBUNITS DURING MEIOTIC MATURATION OF PORCINE OOCYTES

2008 ◽  
Vol 20 (1) ◽  
pp. 133
Author(s):  
J. S. Kim ◽  
Y. S. Cho ◽  
B. S. Song ◽  
X. L. Jin ◽  
K. K. Lee ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Expression Patterns ◽  
Mitogen Activated Protein Kinase ◽  
Meiotic Maturation ◽  
Type I ◽  
Type Ii ◽  
Regulatory Subunits ◽  
Mitogen Activated Protein ◽  
Kinase A

Many extracellular ligands activate adenylyl cyclase and then alter the intracellular concentrations of the second messenger, cAMP. High intracellular concentrations of cAMP activate cAMP-dependent protein kinase A (PKA), which regulates the meiotic arrest of oocytes at the germinal vesicle (GV) stage. In this study, we investigated the expression patterns of PKA subunits in porcine oocytes during meiotic maturation. Porcine oocytes were matured in the NCSU-23 medium supplemented with 10% (v/v) porcine follicular fluid, 10 ng mL–1 of EGF, 25 µm β-mercaptoethanol, 0.57 mm cysteine, 10 IU mL–1 of pregant mare serum gonadotropin, 10 IU mL–1 of hCG, 1 mm dbcAMP for 22 h and further cultured without dbcAMP and hormone for 22 h. All experiments were repeated more than 3 times. All data were analyzed by using Duncan's test of ANOVA by Statistical Analysis System (SAS Institute Inc., Cary, NC, USA). We found that the expression of type I and type II regulatory subunits (RI and RII) of PKA were higher in the GV stage than those of metaphase II stage porcine oocytes. In addition, their expressions were dynamically changed from the metaphase I to metaphase II stage. The expression levels of PKA regulatory subunits type I and type II were evaluated byWestern blot analysis by using specific antibodies such as anti-PKAc, anti-PKARIα, anti-PKARIIα, and anti-PKARIIβ in porcine GV and metaphase II oocytes (n = 25). To confirm the relationship between PKA and cell cycle regulators such as MPF or MAPK during meiosis, the expression of maturation-promoting factor or mitogen-activated protein kinase were examined by Western blot with anti-cdc2 or anti-ERK1/2. The expressions of the RI and RII subunits of PKA were decreased, whereas the expression of maturation-promoting factor (cdc2) or mitogen-activated protein kinase (ERK1/2) were increased in metaphase II stage oocytes. In conclusion, our findings indicate that the dynamic change of PKA subunits plays an important role not only in cAMP/PKA signaling pathway but also in the regulation of meiotic progression beyond the metaphase II stage in porcine oocytes.

scholarly journals Protein kinase A type I activates a CRE-element more efficiently than protein kinase A type II regardless of C subunit isoform

2011 ◽  
Vol 12 (1) ◽  
pp. 7 ◽  
Author(s):  
Øystein Stakkestad ◽  
Anja CV Larsen ◽  
Anne-Katrine Kvissel ◽  
Sissel Eikvar ◽  
Sigurd Ørstavik ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Type I ◽  
Type Ii ◽  
C Subunit ◽  
Kinase A

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

2007 ◽  
Vol 176 (1) ◽  
pp. 101-111 ◽  
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.

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

1999 ◽  
Vol 249 (1) ◽  
pp. 131-146 ◽  
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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