scholarly journals Differential Regulation of the Apical Plasma Membrane Ca2+-ATPase by Protein Kinase A in Parotid Acinar Cells

2007 ◽  
Vol 282 (52) ◽  
pp. 37678-37693 ◽  
Author(s):  
Erin Baggaley ◽  
Stuart McLarnon ◽  
Irma Demeter ◽  
Gabor Varga ◽  
Jason I. E. Bruce
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Acinar Cells ◽  
Differential Regulation ◽  
Apical Plasma Membrane ◽  
Parotid Acinar Cells ◽  
Kinase A

scholarly journals Oncostatin M-stimulated Apical Plasma Membrane Biogenesis Requires p27Kip1-Regulated Cell Cycle Dynamics

2004 ◽  
Vol 15 (9) ◽  
pp. 4105-4114 ◽  
Author(s):  
Sven C.D. van IJzendoorn ◽  
Delphine Théard ◽  
Johanna M. van der Wouden ◽  
Willy Visser ◽  
Kacper A. Wojtal ◽  
...  
Keyword(s):  
Phase Transition ◽  
Plasma Membrane ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
S Phase ◽  
Oncostatin M ◽  
Apical Plasma Membrane ◽  
Membrane Biogenesis ◽  
Phase Progression ◽  
Kinase A

Oncostatin M regulates membrane traffic and stimulates apicalization of the cell surface in hepatoma cells in a protein kinase A-dependent manner. Here, we show that oncostatin M enhances the expression of the cyclin-dependent kinase (cdk)2 inhibitor p27Kip1, which inhibits G1-S phase progression. Forced G1-S-phase transition effectively renders presynchronized cells insensitive to the apicalization-stimulating effect of oncostatin M. G1-S-phase transition prevents oncostatin M-mediated recruitment of protein kinase A to the centrosomal region and precludes the oncostatin M-mediated activation of a protein kinase A-dependent transport route to the apical surface, which exits the subapical compartment (SAC). This transport route has previously been shown to be crucial for apical plasma membrane biogenesis. Together, our data indicate that oncostatin M-stimulated apicalization of the cell surface is critically dependent on the ability of oncostatin M to control p27Kip1/cdk2-mediated G1-S-phase progression and suggest that the regulation of apical plasma membrane-directed traffic from SAC is coupled to centrosome-associated signaling pathways.

cAMP increases liver Na+-taurocholate cotransport by translocating transporter to plasma membranes

1997 ◽  
Vol 273 (4) ◽  
pp. G842-G848 ◽  
Author(s):  
Sunil Mukhopadhayay ◽  
M. Ananthanarayanan ◽  
Bruno Stieger ◽  
Peter J. Meier ◽  
Frederick J. Suchy ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Fusion Protein ◽  
Protein Kinase A ◽  
Plasma Membranes ◽  
Membrane Vesicles ◽  
Rat Hepatocytes ◽  
Plasma Membrane Vesicles ◽  
Short Term ◽  
Kinase A

Adenosine 3′,5′-cyclic monophosphate (cAMP), acting via protein kinase A, increases transport maximum of Na+-taurocholate cotransport within 15 min in hepatocytes (S. Grüne, L. R. Engelking, and M. S. Anwer. J. Biol. Chem. 268: 17734–17741, 1993); the mechanism of this short-term stimulation was investigated. Cycloheximide inhibited neither basal nor cAMP-induced increases in taurocholate uptake in rat hepatocytes, indicating that cAMP does not stimulate transporter synthesis. Studies in plasma membrane vesicles showed that taurocholate uptake was not stimulated by the catalytic subunit of protein kinase A but was higher when hepatocytes were pretreated with cAMP. Immunoblot studies with anti-fusion protein antibodies to the cloned Na+-taurocholate cotransport polypeptide (Ntcp) showed that pretreatment of hepatocytes with cAMP increased Ntcp content in plasma membranes but not in homogenates. Ntcp was detected in microsomes, endosomes, and Golgi fractions, and cAMP pretreatment resulted in a decrease only in endosomal Ntcp content. It is proposed that cAMP increases transport maximum of Na+-taurocholate cotransport, at least in part, by translocating Ntcp from endosomes to plasma membranes.

scholarly journals Regulation of transforming growth factor β-induced responses by protein kinase A in pancreatic acinar cells

2008 ◽  
Vol 295 (1) ◽  
pp. G170-G178 ◽  
Author(s):  
Huibin Yang ◽  
Cheong J. Lee ◽  
Lizhi Zhang ◽  
Maria Dolors Sans ◽  
Diane M. Simeone
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Transforming Growth Factor ◽  
Acinar Cells ◽  
Lung Epithelial Cells ◽  
Pancreatic Acinar Cells ◽  
Intracellular Camp ◽  
Physical Interaction ◽  
Pancreatic Acini ◽  
Kinase A

TGF-β is an important regulator of growth and differentiation in the pancreas and has been implicated in pancreatic tumorigenesis. We have recently demonstrated that TGF-β can activate protein kinase A (PKA) in mink lung epithelial cells (Zhang L, Duan C, Binkley C, Li G, Uhler M, Logsdon C, Simeone D. Mol Cell Biol 24: 2169–2180, 2004). In this study, we sought to determine whether TGF-β activates PKA in pancreatic acinar cells, the mechanism by which PKA is activated, and PKA's role in TGF-β-mediated growth regulatory responses. TGF-β rapidly activated PKA in pancreatic acini while having no effect on intracellular cAMP levels. Coimmunoprecipitation experiments demonstrated a physical interaction between a Smad3/Smad4 complex and the regulatory subunits of PKA. TGF-β also induced activation of the PKA-dependent transcription factor CREB. Both the specific PKA inhibitor H89 and PKI peptide significantly blocked TGF-β's ability to activate PKA and CREB. TGF-β-mediated growth inhibition and TGF-β-induced p21 and SnoN expression in pancreatic acinar cells were blocked by H89 and PKI peptide. This study demonstrates that this novel cross talk between TGF-β and PKA signaling pathways may play an important role in regulating TGF-β signaling in the pancreas.

scholarly journals Differential regulation of human papillomavirus E6 by protein kinase A: conditional degradation of human discs large protein by oncogenic E6

Oncogene ◽  
2000 ◽  
Vol 19 (51) ◽  
pp. 5884-5891 ◽  
Author(s):  
Christian Kühne ◽  
Daniela Gardiol ◽  
Corrado Guarnaccia ◽  
Heinz Amenitsch ◽  
Lawrence Banks
Keyword(s):  
Human Papillomavirus ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Differential Regulation ◽  
Large Protein ◽  
Discs Large ◽  
Kinase A

Phosphorylation of the salivary Na+-K+-2Cl− cotransporter

2002 ◽  
Vol 282 (4) ◽  
pp. C817-C823 ◽  
Author(s):  
Kinji Kurihara ◽  
Nobuo Nakanishi ◽  
Marilyn L. Moore-Hoon ◽  
R. James Turner
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Acinar Cells ◽  
Good Evidence ◽  
Protein Kinase Activity ◽  
Adrenergic Stimulation ◽  
Parotid Acinar Cells ◽  
Rat Parotid ◽  
Phosphopeptide Mapping ◽  
Kinase A

We studied the phosphorylation of the secretory Na+-K+-2Cl− cotransporter (NKCC1) in rat parotid acinar cells. We have previously shown that NKCC1 activity in these cells is dramatically upregulated in response to β-adrenergic stimulation and that this upregulation correlates with NKCC1 phosphorylation, possibly due to protein kinase A (PKA). We show here that when ATP is added to purified acinar basolateral membranes (BLM), NKCC1 is phosphorylated as a result of membrane-associated protein kinase activity. Additional NKCC1 phosphorylation is seen when PKA is added to BLMs, but our data indicate that this is due to an effect of PKA on endogenous membrane kinase or phosphatase activities, rather than its direct phosphorylation of NKCC1. Also, phosphopeptide mapping demonstrates that these phosphorylations do not take place at the site associated with the upregulation of NKCC1 by β-adrenergic stimulation. However, this upregulatory phosphorylation can be mimicked by the addition of cAMP to permeabilized acini, and this effect can be blocked by a specific PKA inhibitor. These latter results provide good evidence that PKA is indeed involved in the upregulatory phosphorylation of NKCC1 and suggest that an additional factor present in the acinar cell but absent from isolated membranes is required to bring about the phosphorylation.

Differential Regulation of Histone Deacetylase 4 by CaM Kinase II and Protein Kinase A in Response to Cardiac Beta-Adrenergic Signaling

Circulation ◽  
2007 ◽  
Vol 116 (suppl_16) ◽  
Author(s):  
Johannes Backs
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Histone Deacetylase ◽  
Medical Center ◽  
Differential Regulation ◽  
Cam Kinase Ii ◽  
Cam Kinase ◽  
Adrenergic Signaling ◽  
Histone Deacetylase 4 ◽  
Kinase A

Abstract 281 Johannes Backs, David Patrick, Thea Backs, Svetlana Bezprozvannaya, Xiaoxia Qi, Joseph A Hill, Eric N Olson, UT Southwestern Medical Center at Dallas, Dallas, TX Johannes Backs, 2007 Finalist and Presenting Author

Differential regulation of aquaporin-5 and -9 expression in astrocytes by protein kinase A

2002 ◽  
Vol 104 (1) ◽  
pp. 96-102 ◽  
Author(s):  
Naoki Yamamoto ◽  
Kazuya Sobue ◽  
Masataka Fujita ◽  
Hirotada Katsuya ◽  
Kiyofumi Asai
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Differential Regulation ◽  
Aquaporin 5 ◽  
Kinase A
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