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Volumn 35, Issue 9, 2014, Pages 748-762

PKA tightly bound to human placental mitochondria participates in steroidogenesis and is not modified by cAMP

Author keywords

Human placenta; PKA activity; Protein phosphorylation; Steroidogenesis; Syncytiotrophoblast mitochondria

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME B; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE REGULATORY SUBUNIT IBETA; CYCLIC AMP DEPENDENT PROTEIN KINASE REGULATORY SUBUNIT IIBETA; CYTOCHROME B; PHOSPHORUS 32; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); PHOSPHORUS; PROGESTERONE;

EID: 84929297556     PISSN: 01434004     EISSN: 15323102     Source Type: Journal    
DOI: 10.1016/j.placenta.2014.06.005     Document Type: Article
Times cited : (7)

References (65)
  • 1
    • 27644505023 scopus 로고    scopus 로고
    • Multiple signaling pathways regulating steroidogenesis and steroidogenic acute regulatory protein expression: More complicated than we thought
    • D.M. Stocco, X. Wang, Y. Jo, and P.R. Manna Multiple signaling pathways regulating steroidogenesis and steroidogenic acute regulatory protein expression: more complicated than we thought Mol Endocrinol 19 2005 2647 2659
    • (2005) Mol Endocrinol , vol.19 , pp. 2647-2659
    • Stocco, D.M.1    Wang, X.2    Jo, Y.3    Manna, P.R.4
  • 2
    • 0024064517 scopus 로고
    • Molecular biology of steroid hormone synthesis
    • W.L. Miller Molecular biology of steroid hormone synthesis Endocr Rev 9 1988 295 318
    • (1988) Endocr Rev , vol.9 , pp. 295-318
    • Miller, W.L.1
  • 3
    • 0027096929 scopus 로고
    • Identification of positive and negative placenta-specific basal elements and a cyclic adenosine 3′,5′-monophosphate response element in the human gene for P450scc
    • C.C. Moore, D.W. Hum, and W.L. Miller Identification of positive and negative placenta-specific basal elements and a cyclic adenosine 3′,5′-monophosphate response element in the human gene for P450scc Mol Endocrinol 6 1992 2045 2058
    • (1992) Mol Endocrinol , vol.6 , pp. 2045-2058
    • Moore, C.C.1    Hum, D.W.2    Miller, W.L.3
  • 4
    • 0031453141 scopus 로고    scopus 로고
    • Phosphorylation of steroidogenic acute regulatory protein (StAR) modulates its steroidogenic activity
    • F. Arakane, S.R. King, Y. Du, C.B. Kallen, L.P. Walsh, and H. Watari et al. Phosphorylation of steroidogenic acute regulatory protein (StAR) modulates its steroidogenic activity J Biol Chem 272 1997 32656 32662
    • (1997) J Biol Chem , vol.272 , pp. 32656-32662
    • Arakane, F.1    King, S.R.2    Du, Y.3    Kallen, C.B.4    Walsh, L.P.5    Watari, H.6
  • 5
    • 84884530635 scopus 로고    scopus 로고
    • Steroid hormone synthesis in mitochondria
    • W.L. Miller Steroid hormone synthesis in mitochondria Mol Cell Endocrinol 379 2013 62 73
    • (2013) Mol Cell Endocrinol , vol.379 , pp. 62-73
    • Miller, W.L.1
  • 6
    • 70350025561 scopus 로고    scopus 로고
    • Novel isoform-specific interfaces revealed by PKA RII beta holoenzyme structures
    • S.H. Brown, J. Wu, C. Kim, K. Alberto, and S.S. Taylor Novel isoform-specific interfaces revealed by PKA RII beta holoenzyme structures J Mol Biol 393 2009 1070 1082
    • (2009) J Mol Biol , vol.393 , pp. 1070-1082
    • Brown, S.H.1    Wu, J.2    Kim, C.3    Alberto, K.4    Taylor, S.S.5
  • 7
    • 38149061122 scopus 로고    scopus 로고
    • Signaling through cAMP and cAMP-dependent protein kinase: Diverse strategies for drug design
    • S.S. Taylor, C. Kim, C.Y. Cheng, S.H. Brown, J. Wu, and N. Kannan Signaling through cAMP and cAMP-dependent protein kinase: diverse strategies for drug design Biochim Biophys Acta 1784 2008 16 26
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 16-26
    • Taylor, S.S.1    Kim, C.2    Cheng, C.Y.3    Brown, S.H.4    Wu, J.5    Kannan, N.6
  • 8
    • 67449105851 scopus 로고    scopus 로고
    • Selectivity in enrichment of cAMP-dependent protein kinase regulatory subunits type i and type II and their interactors using modified cAMP affinity resins
    • T.T. Aye, S. Mohammed, H.W. van den Toorn, T.A. van Veen, M.A. van der Heyden, and A. Scholten et al. Selectivity in enrichment of cAMP-dependent protein kinase regulatory subunits type I and type II and their interactors using modified cAMP affinity resins Mol Cell Proteomics 8 2009 1016 1028
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1016-1028
    • Aye, T.T.1    Mohammed, S.2    Van Den Toorn, H.W.3    Van Veen, T.A.4    Van Der Heyden, M.A.5    Scholten, A.6
  • 9
    • 0001508003 scopus 로고    scopus 로고
    • Specificity in the cAMP/PKA signaling pathway. Differential expression, regulation, and subcellular localization of subunits of PKA
    • B.S. Skålhegg, and K. Taskén Specificity in the cAMP/PKA signaling pathway. Differential expression, regulation, and subcellular localization of subunits of PKA Front Biosci 2 1997 d331 42
    • (1997) Front Biosci , vol.2 , pp. 331-342
    • Skålhegg, B.S.1    Taskén, K.2
  • 11
    • 65549149476 scopus 로고    scopus 로고
    • Regulation of the steroidogenic acute regulatory protein gene expression: Present and future perspectives
    • P.R. Manna, M.T. Dyson, and D.M. Stocco Regulation of the steroidogenic acute regulatory protein gene expression: present and future perspectives Mol Hum Reprod 15 2009 321 333
    • (2009) Mol Hum Reprod , vol.15 , pp. 321-333
    • Manna, P.R.1    Dyson, M.T.2    Stocco, D.M.3
  • 12
    • 0034993923 scopus 로고    scopus 로고
    • Protein phosphorylation in mitochondria from human placenta
    • M. Corso, and M. Thomson Protein phosphorylation in mitochondria from human placenta Placenta 22 2001 432 439
    • (2001) Placenta , vol.22 , pp. 432-439
    • Corso, M.1    Thomson, M.2
  • 13
    • 0036183196 scopus 로고    scopus 로고
    • Evidence of undiscovered cell regulatory mechanisms: Phosphoproteins and protein kinases in mitochondria
    • M. Thomson Evidence of undiscovered cell regulatory mechanisms: phosphoproteins and protein kinases in mitochondria Cell Mol Life Sci 59 2002 213 219
    • (2002) Cell Mol Life Sci , vol.59 , pp. 213-219
    • Thomson, M.1
  • 15
    • 0024384105 scopus 로고
    • Diurnal variation of plasma and saliva oestrogen, progesterone, cortisol and plasma dehydroepiandrosterone sulphate in late pregnancy
    • F.J. Darne, H.H. McGarrigle, and G.C. Lachelin Diurnal variation of plasma and saliva oestrogen, progesterone, cortisol and plasma dehydroepiandrosterone sulphate in late pregnancy Eur J Obstet Gynecol Reprod Biol 32 1989 57 66
    • (1989) Eur J Obstet Gynecol Reprod Biol , vol.32 , pp. 57-66
    • Darne, F.J.1    McGarrigle, H.H.2    Lachelin, G.C.3
  • 16
    • 0029030626 scopus 로고
    • Human steroidogenic acute regulatory protein: Functional activity in COS-1 cells, tissue-specific expression, and mapping of the structural gene to 8p11.2 and pseudogene to chromosome 13
    • T. Sugawara, J.A. Holt, D. Driscoll, J.F. Strauss III, D. Lin, and W.L. Miller et al. Human steroidogenic acute regulatory protein: functional activity in COS-1 cells, tissue-specific expression, and mapping of the structural gene to 8p11.2 and pseudogene to chromosome 13 Proc Natl Acad Sci U S A 92 1995 4778 4782
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 4778-4782
    • Sugawara, T.1    Holt, J.A.2    Driscoll, D.3    Strauss III, J.F.4    Lin, D.5    Miller, W.L.6
  • 17
    • 0030737565 scopus 로고    scopus 로고
    • MLN64 contains a domain with homology to the steroidogenic acute regulatory protein (StAR) that stimulates steroidogenesis
    • H. Watari, F. Arakane, C. Moog-Ltz, C.B. Kallen, C. Tomasetto, and G.L. Gerton et al. MLN64 contains a domain with homology to the steroidogenic acute regulatory protein (StAR) that stimulates steroidogenesis Proc Natl Acad Sci U S A 94 1997 8462 8467
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8462-8467
    • Watari, H.1    Arakane, F.2    Moog-Ltz, C.3    Kallen, C.B.4    Tomasetto, C.5    Gerton, G.L.6
  • 18
    • 0034718451 scopus 로고    scopus 로고
    • N-218 MLN64, a protein with StAR-like steroidogenic activity, is folded and cleaved similarly to StAR
    • H.S. Bose, R.M. Whittal, M.C. Huang, M.A. Baldwin, and W.L. Miller N-218 MLN64, a protein with StAR-like steroidogenic activity, is folded and cleaved similarly to StAR Biochemistry 39 2000 1722 1731
    • (2000) Biochemistry , vol.39 , pp. 1722-1731
    • Bose, H.S.1    Whittal, R.M.2    Huang, M.C.3    Baldwin, M.A.4    Miller, W.L.5
  • 19
    • 0033642725 scopus 로고    scopus 로고
    • Providing progesterone for pregnancy: Control of cholesterol flux to the side-chain cleavage system
    • J.F. Strauss III, L.K. Christenson, L. Devoto, and F. Martinez Providing progesterone for pregnancy: control of cholesterol flux to the side-chain cleavage system J Reprod Fertil Suppl 55 2000 3 12
    • (2000) J Reprod Fertil Suppl , vol.55 , pp. 3-12
    • Strauss III, J.F.1    Christenson, L.K.2    Devoto, L.3    Martinez, F.4
  • 20
    • 16844378285 scopus 로고    scopus 로고
    • Progesterone synthesis by the human placenta
    • R.C. Tuckey Progesterone synthesis by the human placenta Placenta 26 2005 273 281
    • (2005) Placenta , vol.26 , pp. 273-281
    • Tuckey, R.C.1
  • 23
    • 84860672626 scopus 로고    scopus 로고
    • Protein kinase A subunit α catalytic and A kinase anchoring protein 79 in human placental mitochondria
    • M.P. Ma, and M. Thomson Protein kinase A subunit α catalytic and A kinase anchoring protein 79 in human placental mitochondria Open Biochem J 6 2012 23 30
    • (2012) Open Biochem J , vol.6 , pp. 23-30
    • Ma, M.P.1    Thomson, M.2
  • 24
    • 0030933167 scopus 로고    scopus 로고
    • Structural and functional changes in mitochondria associated with trophoblast differentiation: Methods to isolate enriched preparations of syncytiotrophoblast mitochondria
    • F. Martinez, M. Kiriakidou, and J.F. Strauss III Structural and functional changes in mitochondria associated with trophoblast differentiation: methods to isolate enriched preparations of syncytiotrophoblast mitochondria Endocrinology 138 1997 2172 2183
    • (1997) Endocrinology , vol.138 , pp. 2172-2183
    • Martinez, F.1    Kiriakidou, M.2    Strauss III, J.F.3
  • 26
    • 0026447151 scopus 로고
    • Subcellular localization and properties of adenosine diphosphatase in human placenta
    • F. Martinez, R. Moncada, F.J. Barcenas, and T. Espinosa-García Subcellular localization and properties of adenosine diphosphatase in human placenta Placenta 13 1992 463 473
    • (1992) Placenta , vol.13 , pp. 463-473
    • Martinez, F.1    Moncada, R.2    Barcenas, F.J.3    Espinosa-García, T.4
  • 27
    • 0033134704 scopus 로고    scopus 로고
    • Differences in cholesterol incorporation into mitochondria from hepatoma AS-30D and human term placenta
    • J. Navarrete, O. Flores-Herrera, A. Uribe, and F. Martinez Differences in cholesterol incorporation into mitochondria from hepatoma AS-30D and human term placenta Placenta 20 1999 285 291
    • (1999) Placenta , vol.20 , pp. 285-291
    • Navarrete, J.1    Flores-Herrera, O.2    Uribe, A.3    Martinez, F.4
  • 30
    • 0242501535 scopus 로고    scopus 로고
    • Contact sites from human placental mitochondria: Characterization and role in progesterone synthesis
    • A. Uribe, J.F. Strauss III, and F. Martínez Contact sites from human placental mitochondria: characterization and role in progesterone synthesis Arch Biochem Biophys 413 2003 172 181
    • (2003) Arch Biochem Biophys , vol.413 , pp. 172-181
    • Uribe, A.1    Strauss III, J.F.2    Martínez, F.3
  • 31
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • R.B. Pearson, and B.E. Kemp Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations Methods Enzymol 200 1991 62 81
    • (1991) Methods Enzymol , vol.200 , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 35
    • 0036668577 scopus 로고    scopus 로고
    • CAMP-dependent transcription of steroidogenic genes in the human adrenal cortex requires a dual-specificity phosphatase in addition to protein kinase A
    • M.B. Sewer, and M.R. Waterman cAMP-dependent transcription of steroidogenic genes in the human adrenal cortex requires a dual-specificity phosphatase in addition to protein kinase A Mol Endocrinol 29 2002 163 174
    • (2002) Mol Endocrinol , vol.29 , pp. 163-174
    • Sewer, M.B.1    Waterman, M.R.2
  • 36
    • 38149123363 scopus 로고    scopus 로고
    • Regulating gene transcription in response to cyclic AMP elevation
    • W.A. Sands, and T.M. Palmer Regulating gene transcription in response to cyclic AMP elevation Cell Signal 20 2008 460 466
    • (2008) Cell Signal , vol.20 , pp. 460-466
    • Sands, W.A.1    Palmer, T.M.2
  • 37
    • 84856023360 scopus 로고    scopus 로고
    • Review:Spatiotemporal dynamics of hCG/cAMP signaling and regulation of placental function
    • M.S. Weedon-Fekjær, and K. Taskén Review:Spatiotemporal dynamics of hCG/cAMP signaling and regulation of placental function Placenta 33 2012 S87 S91
    • (2012) Placenta , vol.33
    • Weedon-Fekjær, M.S.1    Taskén, K.2
  • 38
    • 0033031288 scopus 로고    scopus 로고
    • CAMP-dependent protein kinase and phosphoproteins in mammalian mitochondria. An extension of the cAMP-mediated intracellular signal transduction
    • S. Papa, A.M. Sardanelli, S. Scacco, and Z. Technikova-Dobrova cAMP-dependent protein kinase and phosphoproteins in mammalian mitochondria. An extension of the cAMP-mediated intracellular signal transduction FEBS Lett 444 1999 245 249
    • (1999) FEBS Lett , vol.444 , pp. 245-249
    • Papa, S.1    Sardanelli, A.M.2    Scacco, S.3    Technikova-Dobrova, Z.4
  • 39
    • 0024995690 scopus 로고
    • Localization of catalytic and regulatory subunits of cyclic AMP-dependent protein kinases in mitochondria from various rat tissues
    • G. Schwoch, B. Trinczek, and C. Bode Localization of catalytic and regulatory subunits of cyclic AMP-dependent protein kinases in mitochondria from various rat tissues Biochem J 270 1990 181 188
    • (1990) Biochem J , vol.270 , pp. 181-188
    • Schwoch, G.1    Trinczek, B.2    Bode, C.3
  • 40
    • 0027527671 scopus 로고
    • Movement of the free catalytic subunit of cAMP-dependent protein kinase into and out of the nucleus can be explained by diffusion
    • A.T. Harootunian, S.R. Adams, W. Wen, J.L. Meinkoth, S.S. Taylor, and R.Y. Tsien Movement of the free catalytic subunit of cAMP-dependent protein kinase into and out of the nucleus can be explained by diffusion Mol Biol Cell 4 1993 993 1002
    • (1993) Mol Biol Cell , vol.4 , pp. 993-1002
    • Harootunian, A.T.1    Adams, S.R.2    Wen, W.3    Meinkoth, J.L.4    Taylor, S.S.5    Tsien, R.Y.6
  • 41
    • 84878882913 scopus 로고    scopus 로고
    • Probes of the mitochondrial cAMP-dependent protein kinase
    • J.R. Shell, and D.S. Larence Probes of the mitochondrial cAMP-dependent protein kinase Biochim Biophys Acta 1834 2013 1359 1363
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 1359-1363
    • Shell, J.R.1    Larence, D.S.2
  • 42
    • 62749164774 scopus 로고    scopus 로고
    • Protein kinase A regulatory subunits in human adipose tissue: Decreased R2B expression and activity in adipocytes from obese subjects
    • G. Mantovani, S. Bondioni, L. Alberti, L. Gilardini, C. Invitti, and S. Corbetta et al. Protein kinase A regulatory subunits in human adipose tissue: decreased R2B expression and activity in adipocytes from obese subjects Diabetes 58 2009 620 626
    • (2009) Diabetes , vol.58 , pp. 620-626
    • Mantovani, G.1    Bondioni, S.2    Alberti, L.3    Gilardini, L.4    Invitti, C.5    Corbetta, S.6
  • 43
    • 0027454488 scopus 로고
    • Novel isozymes of cAMP-dependent protein kinase exist in human cells due to formation of RI alpha-RI beta heterodimeric complexes
    • K. Taskén, B.S. Skålhegg, R. Solberg, K.B. Andersson, S.S. Taylor, and T. Lea et al. Novel isozymes of cAMP-dependent protein kinase exist in human cells due to formation of RI alpha-RI beta heterodimeric complexes J Biol Chem 268 1993 21276 21283
    • (1993) J Biol Chem , vol.268 , pp. 21276-21283
    • Taskén, K.1    Skålhegg, B.S.2    Solberg, R.3    Andersson, K.B.4    Taylor, S.S.5    Lea, T.6
  • 44
    • 9644262531 scopus 로고    scopus 로고
    • CAMP-PKA signaling to the mitochondria: Protein scaffolds, mRNA and phosphatases
    • A. Feliciello, M.E. Gottesman, and E.V. Avvedimento cAMP-PKA signaling to the mitochondria: protein scaffolds, mRNA and phosphatases Cell Signal 17 2005 279 287
    • (2005) Cell Signal , vol.17 , pp. 279-287
    • Feliciello, A.1    Gottesman, M.E.2    Avvedimento, E.V.3
  • 45
    • 82755186479 scopus 로고    scopus 로고
    • An entirely specific type i A-kinase anchoring protein that can sequester two molecules of protein kinase A at mitochondria
    • C.K. Means, B. Lygren, L.K. Langeberg, A. Jain, R.E. Dixon, and A.L. Vega et al. An entirely specific type I A-kinase anchoring protein that can sequester two molecules of protein kinase A at mitochondria Proc Natl Acad Sci U S A 108 2011 E1227 E1235
    • (2011) Proc Natl Acad Sci U S A , vol.108
    • Means, C.K.1    Lygren, B.2    Langeberg, L.K.3    Jain, A.4    Dixon, R.E.5    Vega, A.L.6
  • 46
    • 0027265948 scopus 로고
    • The genetic subtypes of cAMP-dependent protein kinase - Functionally different or redundant?
    • S.O. Døskeland, E. Maronde, and B.T. Gjertsen The genetic subtypes of cAMP-dependent protein kinase - functionally different or redundant? Biochim Biophys Acta 1178 1993 249 258
    • (1993) Biochim Biophys Acta , vol.1178 , pp. 249-258
    • Døskeland, S.O.1    Maronde, E.2    Gjertsen, B.T.3
  • 47
    • 2442603839 scopus 로고    scopus 로고
    • Differential effects of substrate on type i and type II PKA holoenzyme dissociation
    • D. Vigil, D.K. Blumenthal, S. Brown, S.S. Taylor, and J. Trewhella Differential effects of substrate on type I and type II PKA holoenzyme dissociation Biochemistry 43 2004 5629 5636
    • (2004) Biochemistry , vol.43 , pp. 5629-5636
    • Vigil, D.1    Blumenthal, D.K.2    Brown, S.3    Taylor, S.S.4    Trewhella, J.5
  • 48
    • 48849116430 scopus 로고    scopus 로고
    • Pharmacological PKA inhibition: All may not be what it seems
    • A.J. Murray Pharmacological PKA inhibition: all may not be what it seems Sci Signal 1 2008 re4
    • (2008) Sci Signal , vol.1 , pp. 4
    • Murray, A.J.1
  • 49
    • 32844467975 scopus 로고    scopus 로고
    • Protein kinase inhibitor peptide (PKI): A family of endogenous neuropeptides that modulate neuronal cAMP-dependent protein kinase function
    • G.D. Dalton, and W.L. Dewey Protein kinase inhibitor peptide (PKI): a family of endogenous neuropeptides that modulate neuronal cAMP-dependent protein kinase function Neuropeptides 40 2006 23 34
    • (2006) Neuropeptides , vol.40 , pp. 23-34
    • Dalton, G.D.1    Dewey, W.L.2
  • 50
    • 29144523190 scopus 로고    scopus 로고
    • Peptide inhibitors of protein kinases-discovery, characterisation and use
    • M.A. Bogoyevitch, R.K. Barr, and A.J. Ketterman Peptide inhibitors of protein kinases-discovery, characterisation and use Biochim Biophys Acta 1754 2005 79 99
    • (2005) Biochim Biophys Acta , vol.1754 , pp. 79-99
    • Bogoyevitch, M.A.1    Barr, R.K.2    Ketterman, A.J.3
  • 51
    • 34547446738 scopus 로고    scopus 로고
    • Constitutive steroidogenesis in ovine large luteal cells may be mediated by tonically active protein kinase A
    • R.L. Bogan, and G.D. Niswender Constitutive steroidogenesis in ovine large luteal cells may be mediated by tonically active protein kinase A Biol Reprod 77 2007 209 216
    • (2007) Biol Reprod , vol.77 , pp. 209-216
    • Bogan, R.L.1    Niswender, G.D.2
  • 52
    • 0028330527 scopus 로고
    • Retinoblastoma protein is rapidly dephosphorylated by elevated cyclic adenosine monophosphate levels in human B-lymphoid cells
    • J. Christoffersen, E.B. Smeland, T. Stokke, K. Taskén, K.B. Andersson, and H.K. Blomhoff Retinoblastoma protein is rapidly dephosphorylated by elevated cyclic adenosine monophosphate levels in human B-lymphoid cells Cancer Res 54 1994 2245 2250
    • (1994) Cancer Res , vol.54 , pp. 2245-2250
    • Christoffersen, J.1    Smeland, E.B.2    Stokke, T.3    Taskén, K.4    Andersson, K.B.5    Blomhoff, H.K.6
  • 54
    • 67650710788 scopus 로고    scopus 로고
    • Role of protein phosphatase-1 inhibitor-1 in cardiac physiology and pathophysiology
    • P. Nicolaou, R.J. Hajjar, and E.G. Kranias Role of protein phosphatase-1 inhibitor-1 in cardiac physiology and pathophysiology J Mol Cell Cardiol 47 2009 365 371
    • (2009) J Mol Cell Cardiol , vol.47 , pp. 365-371
    • Nicolaou, P.1    Hajjar, R.J.2    Kranias, E.G.3
  • 55
    • 79952000271 scopus 로고    scopus 로고
    • The large isoforms of A-kinase anchoring protein 18 mediate the phosphorylation of inhibitor-1 by protein kinase A and the inhibition of protein phosphatase 1 activity
    • A. Singh, J.M. Redden, M.S. Kapiloff, and K.L. Dodge-Kafka The large isoforms of A-kinase anchoring protein 18 mediate the phosphorylation of inhibitor-1 by protein kinase A and the inhibition of protein phosphatase 1 activity Mol Pharmacol 79 2011 533 540
    • (2011) Mol Pharmacol , vol.79 , pp. 533-540
    • Singh, A.1    Redden, J.M.2    Kapiloff, M.S.3    Dodge-Kafka, K.L.4
  • 56
    • 0034282660 scopus 로고    scopus 로고
    • Mechanism of activation of cAMP-dependent protein kinase: In Mucor rouxii the apparent specific activity of the cAMP-activated holoenzyme is different than that of its free catalytic subunit
    • V. Zaremberg, A. Donella-Deana, and S. Moreno Mechanism of activation of cAMP-dependent protein kinase: in Mucor rouxii the apparent specific activity of the cAMP-activated holoenzyme is different than that of its free catalytic subunit Arch Biochem Biophys 381 2000 74 82
    • (2000) Arch Biochem Biophys , vol.381 , pp. 74-82
    • Zaremberg, V.1    Donella-Deana, A.2    Moreno, S.3
  • 57
    • 0023741277 scopus 로고
    • Modulation of steroidogenesis in choriocarcinoma cells by cholera toxin, phorbol ester, epidermal growth factor and insulin-like growth factor i
    • O. Ritvos Modulation of steroidogenesis in choriocarcinoma cells by cholera toxin, phorbol ester, epidermal growth factor and insulin-like growth factor I Mol Cell Endocrinol 59 1988 125 133
    • (1988) Mol Cell Endocrinol , vol.59 , pp. 125-133
    • Ritvos, O.1
  • 59
    • 0031394997 scopus 로고    scopus 로고
    • Regulation of progesterone biosynthesis in the human placenta by estradiol 17 beta and progesterone
    • Y.G. Shanker, and A.J. Rao Regulation of progesterone biosynthesis in the human placenta by estradiol 17 beta and progesterone Biochem Mol Biol Int 43 1997 591 599
    • (1997) Biochem Mol Biol Int , vol.43 , pp. 591-599
    • Shanker, Y.G.1    Rao, A.J.2
  • 61
    • 0346434149 scopus 로고    scopus 로고
    • Rapid accumulation of Akt in mitochondria following phosphatidylinositol 3-kinase activation
    • G.N. Bijur, and R.S. Jope Rapid accumulation of Akt in mitochondria following phosphatidylinositol 3-kinase activation J Neurochem 87 2003 1427 1435
    • (2003) J Neurochem , vol.87 , pp. 1427-1435
    • Bijur, G.N.1    Jope, R.S.2
  • 62
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signaling pathways: Insights into insulin action
    • C.M. Taniguchi, B. Emanuelli, and C.R. Kahn Critical nodes in signaling pathways: insights into insulin action Nat Rev Mol Cell Biol 7 2006 85 96
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 85-96
    • Taniguchi, C.M.1    Emanuelli, B.2    Kahn, C.R.3
  • 63
    • 79953225915 scopus 로고    scopus 로고
    • Phosphodiesterases catalyze hydrolysis of cAMP-bound to regulatory subunit of protein kinase A and mediate signal termination
    • 10.1074/mcp.M110.002295 M110.002295
    • B.S. Moorthy, Y. Gao, and G.S. Anand Phosphodiesterases catalyze hydrolysis of cAMP-bound to regulatory subunit of protein kinase A and mediate signal termination Mol Cell Proteomics 10 2 2011 10.1074/mcp.M110.002295 M110.002295
    • (2011) Mol Cell Proteomics , vol.10 , Issue.2
    • Moorthy, B.S.1    Gao, Y.2    Anand, G.S.3
  • 64
    • 34147170091 scopus 로고    scopus 로고
    • Parathyroid hormone stimulates endothelial expression of atherosclerotic parameters through protein kinase pathways
    • G. Rashid, J. Bernheim, J. Green, and S. Benchetrit Parathyroid hormone stimulates endothelial expression of atherosclerotic parameters through protein kinase pathways Am J Physiol Renal Physiol 292 2007 F1215 F1218
    • (2007) Am J Physiol Renal Physiol , vol.292
    • Rashid, G.1    Bernheim, J.2    Green, J.3    Benchetrit, S.4
  • 65
    • 84884227999 scopus 로고    scopus 로고
    • The inner and outer compartments of mitochondria are sites of distinct cAMP/PKA signaling dynamics
    • K. Lefkimmiatis, D. Leronni, and A.M. Hofer The inner and outer compartments of mitochondria are sites of distinct cAMP/PKA signaling dynamics J Cell Biol 202 2013 453 462
    • (2013) J Cell Biol , vol.202 , pp. 453-462
    • Lefkimmiatis, K.1    Leronni, D.2    Hofer, A.M.3


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