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Volumn 1770, Issue 4, 2007, Pages 638-648

Alterations in proteoglycan synthesis selectively impair FSH-induced particulate cAMP-phosphodiesterase 4 (PDE4) activation in immature rat Sertoli cells

Author keywords

FSH; phosphodiesterase 4D (PDE4D); proteoglycan (PG); rat; Sertoli cell

Indexed keywords

4 NITROPHENYL BETA DEXTRO XYLOSIDE; CARBOHYDRATE DERIVATIVE; CYCLIC AMP; ENZYME VARIANT; FOLLITROPIN; ISOPROTEIN; PHOSPHODIESTERASE IV; PHOSPHODIESTERASE IV D1; PHOSPHODIESTERASE IV D8; PHOSPHODIESTERASE IV D9; PHOSPHOPROTEIN PHOSPHATASE; PROTEOGLYCAN; SODIUM CHLORATE; UNCLASSIFIED DRUG;

EID: 33847104597     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.12.006     Document Type: Article
Times cited : (5)

References (77)
  • 1
    • 0032130527 scopus 로고    scopus 로고
    • The central role of Sertoli cells in spermatogenesis
    • Griswold M.D. The central role of Sertoli cells in spermatogenesis. Semin. Cell Dev. Biol. 9 (1998) 411-416
    • (1998) Semin. Cell Dev. Biol. , vol.9 , pp. 411-416
    • Griswold, M.D.1
  • 2
    • 22544432534 scopus 로고    scopus 로고
    • FSH and testosterone signaling in Sertoli cells
    • Walker W.H., and Cheng J. FSH and testosterone signaling in Sertoli cells. Reproduction 130 (2005) 15-28
    • (2005) Reproduction , vol.130 , pp. 15-28
    • Walker, W.H.1    Cheng, J.2
  • 3
    • 0020117728 scopus 로고
    • Regulation of follicle-stimulating hormone and dibutyryl adenosine 3′,5′-monophosphate of a phosphodiesterase isoenzyme of the Sertoli cell
    • Conti M., Toscano M.V., Petrelli L., Geremia R., and Stefanini M. Regulation of follicle-stimulating hormone and dibutyryl adenosine 3′,5′-monophosphate of a phosphodiesterase isoenzyme of the Sertoli cell. Endocrinology 110 (1982) 1189-1196
    • (1982) Endocrinology , vol.110 , pp. 1189-1196
    • Conti, M.1    Toscano, M.V.2    Petrelli, L.3    Geremia, R.4    Stefanini, M.5
  • 4
    • 31144433061 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterase (PDE) superfamily: a new target for the development of specific therapeutic agents
    • Lugnier C. Cyclic nucleotide phosphodiesterase (PDE) superfamily: a new target for the development of specific therapeutic agents. Pharmacol. Ther. 109 (2006) 366-398
    • (2006) Pharmacol. Ther. , vol.109 , pp. 366-398
    • Lugnier, C.1
  • 5
    • 33748686575 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterases: molecular regulation to clinical use
    • Bender A.T., and Beavo J.A. Cyclic nucleotide phosphodiesterases: molecular regulation to clinical use. Pharmacol. Rev. 58 (2006) 488-520
    • (2006) Pharmacol. Rev. , vol.58 , pp. 488-520
    • Bender, A.T.1    Beavo, J.A.2
  • 6
    • 0037443097 scopus 로고    scopus 로고
    • PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization
    • Houslay M.D., and Adams D.R. PDE4 cAMP phosphodiesterases: modular enzymes that orchestrate signalling cross-talk, desensitization and compartmentalization. Biochem. J. 370 (2003) 1-18
    • (2003) Biochem. J. , vol.370 , pp. 1-18
    • Houslay, M.D.1    Adams, D.R.2
  • 7
    • 0037458648 scopus 로고    scopus 로고
    • Cyclic AMP-specific PDE4 phosphodiesterases as critical components of cyclic AMP signaling
    • Conti M., Richter W., Mehats C., Livera G., Park J.Y., and Jin C. Cyclic AMP-specific PDE4 phosphodiesterases as critical components of cyclic AMP signaling. J. Biol. Chem. 278 (2003) 5493-5496
    • (2003) J. Biol. Chem. , vol.278 , pp. 5493-5496
    • Conti, M.1    Richter, W.2    Mehats, C.3    Livera, G.4    Park, J.Y.5    Jin, C.6
  • 8
    • 21744442922 scopus 로고    scopus 로고
    • Splice variants of the cyclic nucleotide phosphodiesterase PDE4D are differentially expressed and regulated in rat tissue
    • Richter W., Jin S.L., and Conti M. Splice variants of the cyclic nucleotide phosphodiesterase PDE4D are differentially expressed and regulated in rat tissue. Biochem. J. (2005)
    • (2005) Biochem. J.
    • Richter, W.1    Jin, S.L.2    Conti, M.3
  • 9
    • 0034616226 scopus 로고    scopus 로고
    • UCR1 and UCR2 domains unique to the cAMP-specific phosphodiesterase family form a discrete module via electrostatic interactions
    • Beard M.B., Olsen A.E., Jones R.E., Erdogan S., Houslay M.D., and Bolger G.B. UCR1 and UCR2 domains unique to the cAMP-specific phosphodiesterase family form a discrete module via electrostatic interactions. J. Biol. Chem. 275 (2000) 10349-10358
    • (2000) J. Biol. Chem. , vol.275 , pp. 10349-10358
    • Beard, M.B.1    Olsen, A.E.2    Jones, R.E.3    Erdogan, S.4    Houslay, M.D.5    Bolger, G.B.6
  • 10
    • 0030006920 scopus 로고    scopus 로고
    • Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase. Involvement of serine 54 in the enzyme activation
    • Sette C., and Conti M. Phosphorylation and activation of a cAMP-specific phosphodiesterase by the cAMP-dependent protein kinase. Involvement of serine 54 in the enzyme activation. J. Biol. Chem. 271 (1996) 16526-16534
    • (1996) J. Biol. Chem. , vol.271 , pp. 16526-16534
    • Sette, C.1    Conti, M.2
  • 11
    • 0032127768 scopus 로고    scopus 로고
    • cAMP-specific phosphodiesterase HSPDE4D3 mutants which mimic activation and changes in rolipram inhibition triggered by protein kinase A phosphorylation of Ser-54: generation of a molecular model
    • Hoffmann R., Wilkinson I.R., McCallum J.F., Engels P., and Houslay M.D. cAMP-specific phosphodiesterase HSPDE4D3 mutants which mimic activation and changes in rolipram inhibition triggered by protein kinase A phosphorylation of Ser-54: generation of a molecular model. Biochem. J. 333 (1998) 139-149
    • (1998) Biochem. J. , vol.333 , pp. 139-149
    • Hoffmann, R.1    Wilkinson, I.R.2    McCallum, J.F.3    Engels, P.4    Houslay, M.D.5
  • 13
    • 0031601339 scopus 로고    scopus 로고
    • The multienzyme PDE4 cyclic adenosine monophosphate-specific phosphodiesterase family: intracellular targeting, regulation, and selective inhibition by compounds exerting anti-inflammatory and antidepressant actions
    • Houslay M.D., Sullivan M., and Bolger G.B. The multienzyme PDE4 cyclic adenosine monophosphate-specific phosphodiesterase family: intracellular targeting, regulation, and selective inhibition by compounds exerting anti-inflammatory and antidepressant actions. Adv. Pharmacol. 44 (1998) 225-342
    • (1998) Adv. Pharmacol. , vol.44 , pp. 225-342
    • Houslay, M.D.1    Sullivan, M.2    Bolger, G.B.3
  • 14
    • 20444412702 scopus 로고    scopus 로고
    • Compartmentalisation of phosphodiesterases and protein kinase A: opposites attract
    • Baillie G.S., Scott J.D., and Houslay M.D. Compartmentalisation of phosphodiesterases and protein kinase A: opposites attract. FEBS Lett. 579 (2005) 3264-3270
    • (2005) FEBS Lett. , vol.579 , pp. 3264-3270
    • Baillie, G.S.1    Scott, J.D.2    Houslay, M.D.3
  • 15
    • 15044353649 scopus 로고    scopus 로고
    • Arrestin times for compartmentalised cAMP signalling and phosphodiesterase-4 enzymes
    • Baillie G.S., and Houslay M.D. Arrestin times for compartmentalised cAMP signalling and phosphodiesterase-4 enzymes. Curr. Opin. Cell Biol. 17 (2005) 129-134
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 129-134
    • Baillie, G.S.1    Houslay, M.D.2
  • 16
    • 0027295333 scopus 로고
    • Engineered deletion of the unique N-terminal domain of the cyclic AMP-specific phosphodiesterase RD1 prevents plasma membrane association and the attainment of enhanced thermostability without altering its sensitivity to inhibition by rolipram
    • Shakur Y., Pryde J.G., and Houslay M.D. Engineered deletion of the unique N-terminal domain of the cyclic AMP-specific phosphodiesterase RD1 prevents plasma membrane association and the attainment of enhanced thermostability without altering its sensitivity to inhibition by rolipram. Biochem. J. 292 Pt. 3 (1993) 677-686
    • (1993) Biochem. J. , vol.292 , Issue.PART 3 , pp. 677-686
    • Shakur, Y.1    Pryde, J.G.2    Houslay, M.D.3
  • 18
    • 0032584673 scopus 로고    scopus 로고
    • Subcellular localization of rolipram-sensitive, cAMP-specific phosphodiesterases. Differential targeting and activation of the splicing variants derived from the PDE4D gene
    • Jin S.L., Bushnik T., Lan L., and Conti M. Subcellular localization of rolipram-sensitive, cAMP-specific phosphodiesterases. Differential targeting and activation of the splicing variants derived from the PDE4D gene. J. Biol. Chem. 273 (1998) 19672-19678
    • (1998) J. Biol. Chem. , vol.273 , pp. 19672-19678
    • Jin, S.L.1    Bushnik, T.2    Lan, L.3    Conti, M.4
  • 19
    • 0029151222 scopus 로고
    • Identification, characterization and regional distribution in brain of RPDE-6 (RNPDE4A5), a novel splice variant of the PDE4A cyclic AMP phosphodiesterase family
    • McPhee I., Pooley L., Lobban M., Bolger G., and Houslay M.D. Identification, characterization and regional distribution in brain of RPDE-6 (RNPDE4A5), a novel splice variant of the PDE4A cyclic AMP phosphodiesterase family. Biochem. J. 310 (1995) 965-974
    • (1995) Biochem. J. , vol.310 , pp. 965-974
    • McPhee, I.1    Pooley, L.2    Lobban, M.3    Bolger, G.4    Houslay, M.D.5
  • 20
    • 0028904409 scopus 로고
    • Inhibition of proteoglycan synthesis induces an increase in follicle stimulating hormone (FSH)-stimulated estradiol production by immature rat Sertoli cells
    • Phamantu N.T., Bonnamy P.J., Bouakka M., and Bocquet J. Inhibition of proteoglycan synthesis induces an increase in follicle stimulating hormone (FSH)-stimulated estradiol production by immature rat Sertoli cells. Mol. Cell. Endocrinol. 109 (1995) 37-45
    • (1995) Mol. Cell. Endocrinol. , vol.109 , pp. 37-45
    • Phamantu, N.T.1    Bonnamy, P.J.2    Bouakka, M.3    Bocquet, J.4
  • 21
    • 0032910505 scopus 로고    scopus 로고
    • Sodium chlorate induces undersulfation of cellular proteoglycans and increases in FSH-stimulated estradiol production in immature rat Sertoli cells
    • Phamantu N.T., Fagnen G., Godard F., Bocquet J., and Bonnamy P.J. Sodium chlorate induces undersulfation of cellular proteoglycans and increases in FSH-stimulated estradiol production in immature rat Sertoli cells. J. Androl. 20 (1999) 241-250
    • (1999) J. Androl. , vol.20 , pp. 241-250
    • Phamantu, N.T.1    Fagnen, G.2    Godard, F.3    Bocquet, J.4    Bonnamy, P.J.5
  • 22
    • 0033975514 scopus 로고    scopus 로고
    • Synthesis and sorting of proteoglycans
    • Prydz K., and Dalen K.T. Synthesis and sorting of proteoglycans. J. Cell. Sci. 113 Pt. 2 (2000) 193-205
    • (2000) J. Cell. Sci. , vol.113 , Issue.PART 2 , pp. 193-205
    • Prydz, K.1    Dalen, K.T.2
  • 23
    • 0033959545 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans on the cell surface: versatile coordinators of cellular functions
    • Tumova S., Woods A., and Couchman J.R. Heparan sulfate proteoglycans on the cell surface: versatile coordinators of cellular functions. Int. J. Biochem. Cell Biol. 32 (2000) 269-288
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 269-288
    • Tumova, S.1    Woods, A.2    Couchman, J.R.3
  • 25
    • 0030660196 scopus 로고    scopus 로고
    • Syndecans: multifunctional cell-surface co-receptors
    • Carey D.J. Syndecans: multifunctional cell-surface co-receptors. Biochem. J. 327 Pt. 1 (1997) 1-16
    • (1997) Biochem. J. , vol.327 , Issue.PART 1 , pp. 1-16
    • Carey, D.J.1
  • 26
    • 0035210065 scopus 로고    scopus 로고
    • Syndecan-4-mediated signalling
    • Simons M., and Horowitz A. Syndecan-4-mediated signalling. Cell Signal. 13 (2001) 855-862
    • (2001) Cell Signal. , vol.13 , pp. 855-862
    • Simons, M.1    Horowitz, A.2
  • 27
    • 16244380777 scopus 로고    scopus 로고
    • Syndecans: new kids on the signaling block
    • Tkachenko E., Rhodes J.M., and Simons M. Syndecans: new kids on the signaling block. Circ. Res. 96 (2005) 488-500
    • (2005) Circ. Res. , vol.96 , pp. 488-500
    • Tkachenko, E.1    Rhodes, J.M.2    Simons, M.3
  • 28
    • 0345169052 scopus 로고    scopus 로고
    • Syndecans: proteoglycan regulators of cell-surface microdomains?
    • Couchman J.R. Syndecans: proteoglycan regulators of cell-surface microdomains?. Nat. Rev., Mol. Cell Biol. 4 (2003) 926-937
    • (2003) Nat. Rev., Mol. Cell Biol. , vol.4 , pp. 926-937
    • Couchman, J.R.1
  • 29
    • 0025922316 scopus 로고
    • Biological functions of proteoglycans: use of specific inhibitors of proteoglycan synthesis
    • Carey D.J. Biological functions of proteoglycans: use of specific inhibitors of proteoglycan synthesis. Mol. Cell. Biochem. 104 (1991) 21-28
    • (1991) Mol. Cell. Biochem. , vol.104 , pp. 21-28
    • Carey, D.J.1
  • 30
    • 0022897789 scopus 로고
    • Chlorate-a potent inhibitor of protein sulfation in intact cells
    • Baeuerle P.A., and Huttner W.B. Chlorate-a potent inhibitor of protein sulfation in intact cells. Biochem. Biophys. Res. Commun. 141 (1986) 870-877
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 870-877
    • Baeuerle, P.A.1    Huttner, W.B.2
  • 31
    • 0027468962 scopus 로고
    • Proteases are implicated in the changes in the Sertoli cell cytoskeleton elicited by follicle-stimulating hormone or by dibutyryl cyclic AMP
    • Tung P.S., Burdzy K., and Fritz I.B. Proteases are implicated in the changes in the Sertoli cell cytoskeleton elicited by follicle-stimulating hormone or by dibutyryl cyclic AMP. J. Cell. Physiol. 155 (1993) 139-148
    • (1993) J. Cell. Physiol. , vol.155 , pp. 139-148
    • Tung, P.S.1    Burdzy, K.2    Fritz, I.B.3
  • 32
    • 0019428582 scopus 로고
    • Hormonal induced changes in Sertoli cell glycoproteins
    • Galdieri M., and Zani B. Hormonal induced changes in Sertoli cell glycoproteins. Cell Biol. Int. Rep. 5 (1981) 111
    • (1981) Cell Biol. Int. Rep. , vol.5 , pp. 111
    • Galdieri, M.1    Zani, B.2
  • 33
    • 0023339254 scopus 로고
    • Alkaline phosphatase histochemistry discriminates peritubular cells in primary rat testicular cell culture
    • Chapin R.E., Phelps J.L., Miller B.E., and Gray T.J. Alkaline phosphatase histochemistry discriminates peritubular cells in primary rat testicular cell culture. J. Androl. 8 (1987) 155-161
    • (1987) J. Androl. , vol.8 , pp. 155-161
    • Chapin, R.E.1    Phelps, J.L.2    Miller, B.E.3    Gray, T.J.4
  • 34
    • 0026628026 scopus 로고
    • Development and cytodifferentiation of peritubular myoid cells in the rat testis
    • Palombi F., Farini D., Salanova M., de Grossi S., and Stefanini M. Development and cytodifferentiation of peritubular myoid cells in the rat testis. Anat. Rec. 233 (1992) 32-40
    • (1992) Anat. Rec. , vol.233 , pp. 32-40
    • Palombi, F.1    Farini, D.2    Salanova, M.3    de Grossi, S.4    Stefanini, M.5
  • 35
    • 0024450836 scopus 로고
    • Cellular localization of fibronectin gene expression in the seminiferous tubule
    • Skinner M.K., Stallard B., Anthony C.T., and Griswold M.D. Cellular localization of fibronectin gene expression in the seminiferous tubule. Mol. Cell. Endocrinol. 66 (1989) 45-52
    • (1989) Mol. Cell. Endocrinol. , vol.66 , pp. 45-52
    • Skinner, M.K.1    Stallard, B.2    Anthony, C.T.3    Griswold, M.D.4
  • 36
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 (1987) 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 37
    • 0028036970 scopus 로고
    • Identification of two splice variant forms of type-IVB cyclic AMP phosphodiesterase, DPD (rPDE-IVB1) and PDE-4 (rPDE-IVB2) in brain: selective localization in membrane and cytosolic compartments and differential expression in various brain regions
    • Lobban M., Shakur Y., Beattie J., and Houslay M.D. Identification of two splice variant forms of type-IVB cyclic AMP phosphodiesterase, DPD (rPDE-IVB1) and PDE-4 (rPDE-IVB2) in brain: selective localization in membrane and cytosolic compartments and differential expression in various brain regions. Biochem. J. 304 (1994) 399-406
    • (1994) Biochem. J. , vol.304 , pp. 399-406
    • Lobban, M.1    Shakur, Y.2    Beattie, J.3    Houslay, M.D.4
  • 38
    • 0020581179 scopus 로고
    • Reactive thiol groups in calf-intestinal alkaline phosphatase
    • Abdolrazaghi Z., and Butterworth P.J. Reactive thiol groups in calf-intestinal alkaline phosphatase. Enzyme 30 (1983) 12-20
    • (1983) Enzyme , vol.30 , pp. 12-20
    • Abdolrazaghi, Z.1    Butterworth, P.J.2
  • 39
    • 0019177378 scopus 로고
    • Serum lactic dehydrogenase (LDH) levels in acute leukemia: marked elevations in lymphoblastic leukemia
    • Kornberg A., and Polliack A. Serum lactic dehydrogenase (LDH) levels in acute leukemia: marked elevations in lymphoblastic leukemia. Blood 56 (1980) 351-355
    • (1980) Blood , vol.56 , pp. 351-355
    • Kornberg, A.1    Polliack, A.2
  • 40
    • 0015231739 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterase activities from rat brain
    • Thompson W.J., and Appleman M.M. Multiple cyclic nucleotide phosphodiesterase activities from rat brain. Biochemistry 10 (1971) 311-316
    • (1971) Biochemistry , vol.10 , pp. 311-316
    • Thompson, W.J.1    Appleman, M.M.2
  • 41
    • 0020000847 scopus 로고
    • Characteristic behavioural alterations in rats induced by rolipram and other selective adenosine cyclic 3′, 5′-monophosphate phosphodiesterase inhibitors
    • Wachtel H. Characteristic behavioural alterations in rats induced by rolipram and other selective adenosine cyclic 3′, 5′-monophosphate phosphodiesterase inhibitors. Psychopharmacology (Berl) 77 (1982) 309-316
    • (1982) Psychopharmacology (Berl) , vol.77 , pp. 309-316
    • Wachtel, H.1
  • 42
    • 0025853852 scopus 로고
    • Effects of beta-xylosides on proteoglycan biosynthesis and morphology of PC12 pheochromocytoma cells and primary cultures of rat cerebellum
    • Margolis R.K., Goossen B., Tekotte H., Hilgenberg L., and Margolis R.U. Effects of beta-xylosides on proteoglycan biosynthesis and morphology of PC12 pheochromocytoma cells and primary cultures of rat cerebellum. J. Cell. Sci. 99 Pt. 2 (1991) 237-246
    • (1991) J. Cell. Sci. , vol.99 , Issue.PART 2 , pp. 237-246
    • Margolis, R.K.1    Goossen, B.2    Tekotte, H.3    Hilgenberg, L.4    Margolis, R.U.5
  • 43
    • 0026010201 scopus 로고
    • Properties and hormonal regulation of two structurally related cAMP phosphodiesterases from the rat Sertoli cell
    • Swinnen J.V., Tsikalas K.E., and Conti M. Properties and hormonal regulation of two structurally related cAMP phosphodiesterases from the rat Sertoli cell. J. Biol. Chem. 266 (1991) 18370-18377
    • (1991) J. Biol. Chem. , vol.266 , pp. 18370-18377
    • Swinnen, J.V.1    Tsikalas, K.E.2    Conti, M.3
  • 44
    • 0029061008 scopus 로고
    • Characterization of a hormone-inducible, high affinity adenosine 3′-5′-cyclic monophosphate phosphodiesterase from the rat Sertoli cell
    • Conti M., Iona S., Cuomo M., Swinnen J.V., Odeh J., and Svoboda M.E. Characterization of a hormone-inducible, high affinity adenosine 3′-5′-cyclic monophosphate phosphodiesterase from the rat Sertoli cell. Biochemistry 34 (1995) 7979-7987
    • (1995) Biochemistry , vol.34 , pp. 7979-7987
    • Conti, M.1    Iona, S.2    Cuomo, M.3    Swinnen, J.V.4    Odeh, J.5    Svoboda, M.E.6
  • 45
    • 0028911420 scopus 로고
    • Stage and cell-specific expression of the adenosine 3′,5′ monophosphate-phosphodiesterase genes in the rat seminiferous epithelium
    • Morena A.R., Boitani C., de Grossi S., Stefanini M., and Conti M. Stage and cell-specific expression of the adenosine 3′,5′ monophosphate-phosphodiesterase genes in the rat seminiferous epithelium. Endocrinology 136 (1995) 687-695
    • (1995) Endocrinology , vol.136 , pp. 687-695
    • Morena, A.R.1    Boitani, C.2    de Grossi, S.3    Stefanini, M.4    Conti, M.5
  • 47
    • 0030665303 scopus 로고    scopus 로고
    • Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene
    • Bolger G.B., Erdogan S., Jones R.E., Loughney K., Scotland G., Hoffmann R., Wilkinson I., Farrell C., and Houslay M.D. Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene. Biochem. J. 328 (1997) 539-548
    • (1997) Biochem. J. , vol.328 , pp. 539-548
    • Bolger, G.B.1    Erdogan, S.2    Jones, R.E.3    Loughney, K.4    Scotland, G.5    Hoffmann, R.6    Wilkinson, I.7    Farrell, C.8    Houslay, M.D.9
  • 48
    • 0033306841 scopus 로고    scopus 로고
    • Type 4 cyclic adenosine monophosphate-specific phosphodiesterases are expressed in discrete subcellular compartments during rat spermiogenesis
    • Salanova M., Chun S.Y., Iona S., Puri C., Stefanini M., and Conti M. Type 4 cyclic adenosine monophosphate-specific phosphodiesterases are expressed in discrete subcellular compartments during rat spermiogenesis. Endocrinology 140 (1999) 2297-2306
    • (1999) Endocrinology , vol.140 , pp. 2297-2306
    • Salanova, M.1    Chun, S.Y.2    Iona, S.3    Puri, C.4    Stefanini, M.5    Conti, M.6
  • 49
    • 0032875809 scopus 로고    scopus 로고
    • Activation of protein kinase C increases proteoglycan synthesis in immature rat Sertoli cells
    • Fagnen G., Phamantu N.T., Bocquet J., and Bonnamy P.J. Activation of protein kinase C increases proteoglycan synthesis in immature rat Sertoli cells. Biochim. Biophys. Acta 1472 (1999) 250-261
    • (1999) Biochim. Biophys. Acta , vol.1472 , pp. 250-261
    • Fagnen, G.1    Phamantu, N.T.2    Bocquet, J.3    Bonnamy, P.J.4
  • 51
    • 0034714376 scopus 로고    scopus 로고
    • Expression of phosphodiesterase 4D (PDE4D) is regulated by both the cyclic AMP-dependent protein kinase and mitogen-activated protein kinase signaling pathways. A potential mechanism allowing for the coordinated regulation of PDE4D activity and expression in cells
    • Liu H., Palmer D., Jimmo S.L., Tilley D.G., Dunkerley H.A., Pang S.C., and Maurice D.H. Expression of phosphodiesterase 4D (PDE4D) is regulated by both the cyclic AMP-dependent protein kinase and mitogen-activated protein kinase signaling pathways. A potential mechanism allowing for the coordinated regulation of PDE4D activity and expression in cells. J. Biol. Chem. 275 (2000) 26615-26624
    • (2000) J. Biol. Chem. , vol.275 , pp. 26615-26624
    • Liu, H.1    Palmer, D.2    Jimmo, S.L.3    Tilley, D.G.4    Dunkerley, H.A.5    Pang, S.C.6    Maurice, D.H.7
  • 52
    • 34248333795 scopus 로고    scopus 로고
    • Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5, BMC
    • Bolger G.B., McCahill A., Yarwood S.J., Steele M.S., Warwicker J., and Houslay M.D. Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5, BMC. Biochem 3 (2002) 24
    • (2002) Biochem , vol.3 , pp. 24
    • Bolger, G.B.1    McCahill, A.2    Yarwood, S.J.3    Steele, M.S.4    Warwicker, J.5    Houslay, M.D.6
  • 53
    • 1542572127 scopus 로고    scopus 로고
    • The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins
    • Bolger G.B., McCahill A., Huston E., Cheung Y.F., McSorley T., Baillie G.S., and Houslay M.D. The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins. J. Biol. Chem. 278 (2003) 49230-49238
    • (2003) J. Biol. Chem. , vol.278 , pp. 49230-49238
    • Bolger, G.B.1    McCahill, A.2    Huston, E.3    Cheung, Y.F.4    McSorley, T.5    Baillie, G.S.6    Houslay, M.D.7
  • 54
    • 0033178807 scopus 로고    scopus 로고
    • Phosphorylation and activation of phosphodiesterase type 3B (PDE3B) in adipocytes in response to serine/threonine phosphatase inhibitors: deactivation of PDE3B in vitro by protein phosphatase type 2A
    • Resjo S., Oknianska A., Zolnierowicz S., Manganiello V., and Degerman E. Phosphorylation and activation of phosphodiesterase type 3B (PDE3B) in adipocytes in response to serine/threonine phosphatase inhibitors: deactivation of PDE3B in vitro by protein phosphatase type 2A. Biochem. J. 341 Pt. 3 (1999) 839-845
    • (1999) Biochem. J. , vol.341 , Issue.PART 3 , pp. 839-845
    • Resjo, S.1    Oknianska, A.2    Zolnierowicz, S.3    Manganiello, V.4    Degerman, E.5
  • 55
    • 0035840446 scopus 로고    scopus 로고
    • Role of serine/threonine protein phosphatase 2A in cancer
    • Schonthal A.H. Role of serine/threonine protein phosphatase 2A in cancer. Cancer Lett. 170 (2001) 1-13
    • (2001) Cancer Lett. , vol.170 , pp. 1-13
    • Schonthal, A.H.1
  • 56
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens V., and Goris J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 353 (2001) 417-439
    • (2001) Biochem. J. , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 57
    • 0028331438 scopus 로고
    • J Differential activities of protein phosphatase types 1 and 2A in cytosolic and particulate fractions from rat forebrain
    • Sim A.T., Ratcliffe E., Mumby M.C., Villa-Moruzzi E., and Rostas J.A. J Differential activities of protein phosphatase types 1 and 2A in cytosolic and particulate fractions from rat forebrain. Neurochem 62 (1994) 1552-1559
    • (1994) Neurochem , vol.62 , pp. 1552-1559
    • Sim, A.T.1    Ratcliffe, E.2    Mumby, M.C.3    Villa-Moruzzi, E.4    Rostas, J.A.5
  • 58
    • 0037071542 scopus 로고    scopus 로고
    • Fibroblast growth factor-specific modulation of cellular response by syndecan-4
    • Horowitz A., Tkachenko E., and Simons M. Fibroblast growth factor-specific modulation of cellular response by syndecan-4. J. Cell Biol. 157 (2002) 715-725
    • (2002) J. Cell Biol. , vol.157 , pp. 715-725
    • Horowitz, A.1    Tkachenko, E.2    Simons, M.3
  • 59
    • 0347359224 scopus 로고    scopus 로고
    • Localized effects of cAMP mediated by distinct routes of protein kinase A
    • Tasken K., and Aandahl E.M. Localized effects of cAMP mediated by distinct routes of protein kinase A. Physiol. Rev. 84 (2004) 137-167
    • (2004) Physiol. Rev. , vol.84 , pp. 137-167
    • Tasken, K.1    Aandahl, E.M.2
  • 60
    • 33747727571 scopus 로고    scopus 로고
    • Syndecan-1 expression in epithelial cells is induced by TGFbeta through a PKA-dependent pathway
    • Hayashida K., Johnston D.R., Goldberger O., and Park P.W. Syndecan-1 expression in epithelial cells is induced by TGFbeta through a PKA-dependent pathway. J. Biol. Chem. (2006) 24365-24374
    • (2006) J. Biol. Chem. , pp. 24365-24374
    • Hayashida, K.1    Johnston, D.R.2    Goldberger, O.3    Park, P.W.4
  • 61
    • 0032514263 scopus 로고    scopus 로고
    • Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses
    • Hsueh Y.P., Yang F.C., Kharazia V., Naisbitt S., Cohen A.R., Weinberg R.J., and Sheng M. Direct interaction of CASK/LIN-2 and syndecan heparan sulfate proteoglycan and their overlapping distribution in neuronal synapses. J. Cell Biol. 142 (1998) 139-151
    • (1998) J. Cell Biol. , vol.142 , pp. 139-151
    • Hsueh, Y.P.1    Yang, F.C.2    Kharazia, V.3    Naisbitt, S.4    Cohen, A.R.5    Weinberg, R.J.6    Sheng, M.7
  • 62
    • 0032514259 scopus 로고    scopus 로고
    • Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells
    • Cohen A.R., Woods D.F., Marfatia S.M., Walther Z., Chishti A.H., and Anderson J.M. Human CASK/LIN-2 binds syndecan-2 and protein 4.1 and localizes to the basolateral membrane of epithelial cells. J. Cell Biol. 142 (1998) 129-138
    • (1998) J. Cell Biol. , vol.142 , pp. 129-138
    • Cohen, A.R.1    Woods, D.F.2    Marfatia, S.M.3    Walther, Z.4    Chishti, A.H.5    Anderson, J.M.6
  • 63
    • 0344182430 scopus 로고    scopus 로고
    • Calcyclin is differentially expressed in rat testicular cells
    • Konrad L., and Aumuller G. Calcyclin is differentially expressed in rat testicular cells. Biochim. Biophys. Acta 1489 (1999) 440-444
    • (1999) Biochim. Biophys. Acta , vol.1489 , pp. 440-444
    • Konrad, L.1    Aumuller, G.2
  • 64
    • 33745739734 scopus 로고    scopus 로고
    • The role of the MAGUK protein CASK in neural development and synaptic function
    • Hsueh Y.P. The role of the MAGUK protein CASK in neural development and synaptic function. Curr Med Chem 13 (2006) 1915-1927
    • (2006) Curr Med Chem , vol.13 , pp. 1915-1927
    • Hsueh, Y.P.1
  • 65
    • 0036369804 scopus 로고    scopus 로고
    • Genetic studies define MAGUK proteins as regulators of epithelial cell polarity
    • Caruana G. Genetic studies define MAGUK proteins as regulators of epithelial cell polarity. Int J Dev Biol 46 (2002) 511-518
    • (2002) Int J Dev Biol , vol.46 , pp. 511-518
    • Caruana, G.1
  • 67
    • 0026549693 scopus 로고
    • Transforming growth factor beta 1 inhibits gonadotropin action in cultured porcine Sertoli cells
    • Morera A.M., Esposito G., Ghiglieri C., Chauvin M.A., Hartmann D.J., and Benahmed M. Transforming growth factor beta 1 inhibits gonadotropin action in cultured porcine Sertoli cells. Endocrinology 130 (1992) 831-836
    • (1992) Endocrinology , vol.130 , pp. 831-836
    • Morera, A.M.1    Esposito, G.2    Ghiglieri, C.3    Chauvin, M.A.4    Hartmann, D.J.5    Benahmed, M.6
  • 68
    • 0034095211 scopus 로고    scopus 로고
    • Ezrin links syndecan-2 to the cytoskeleton
    • Granes F., Urena J.M., Rocamora N., and Vilaro S. Ezrin links syndecan-2 to the cytoskeleton. J. Cell. Sci. 113 Pt. 7 (2000) 1267-1276
    • (2000) J. Cell. Sci. , vol.113 , Issue.PART 7 , pp. 1267-1276
    • Granes, F.1    Urena, J.M.2    Rocamora, N.3    Vilaro, S.4
  • 70
    • 0028575371 scopus 로고
    • Analysis of transport and targeting of syndecan-1: effect of cytoplasmic tail deletions
    • Miettinen H.M., Edwards S.N., and Jalkanen M. Analysis of transport and targeting of syndecan-1: effect of cytoplasmic tail deletions. Mol. Biol. Cell 5 (1994) 1325-1339
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1325-1339
    • Miettinen, H.M.1    Edwards, S.N.2    Jalkanen, M.3
  • 71
  • 72
    • 0030059066 scopus 로고    scopus 로고
    • Anti-human FSH receptor monoclonal antibodies: immunochemical and immunocytochemical characterization of the receptor
    • Vannier B., Loosfelt H., Meduri G., Pichon C., and Milgrom E. Anti-human FSH receptor monoclonal antibodies: immunochemical and immunocytochemical characterization of the receptor. Biochemistry 35 (1996) 1358-1366
    • (1996) Biochemistry , vol.35 , pp. 1358-1366
    • Vannier, B.1    Loosfelt, H.2    Meduri, G.3    Pichon, C.4    Milgrom, E.5
  • 73
    • 0029005076 scopus 로고
    • Loss of cell surface syndecan-1 causes epithelia to transform into anchorage-independent mesenchyme-like cells
    • Kato M., Saunders S., Nguyen H., and Bernfield M. Loss of cell surface syndecan-1 causes epithelia to transform into anchorage-independent mesenchyme-like cells. Mol. Biol. Cell 6 (1995) 559-576
    • (1995) Mol. Biol. Cell , vol.6 , pp. 559-576
    • Kato, M.1    Saunders, S.2    Nguyen, H.3    Bernfield, M.4
  • 74
    • 0026558931 scopus 로고
    • Syndecan expression regulates cell morphology and growth of mouse mammary epithelial tumor cells
    • Leppa S., Mali M., Miettinen H.M., and Jalkanen M. Syndecan expression regulates cell morphology and growth of mouse mammary epithelial tumor cells. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 932-936
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 932-936
    • Leppa, S.1    Mali, M.2    Miettinen, H.M.3    Jalkanen, M.4
  • 75
    • 0030065003 scopus 로고    scopus 로고
    • The role of syndecan-1 in malignancies
    • Inki P., and Jalkanen M. The role of syndecan-1 in malignancies. Ann. Med. 28 (1996) 63-67
    • (1996) Ann. Med. , vol.28 , pp. 63-67
    • Inki, P.1    Jalkanen, M.2
  • 76
    • 0018169211 scopus 로고
    • Changes in cyclic AMP responses to FSH in isolated rat Sertoli cells during sexual maturation
    • Steinberger A., Hintz M., and Heindel J.J. Changes in cyclic AMP responses to FSH in isolated rat Sertoli cells during sexual maturation. Biol. Reprod. 19 (1978) 566-572
    • (1978) Biol. Reprod. , vol.19 , pp. 566-572
    • Steinberger, A.1    Hintz, M.2    Heindel, J.J.3
  • 77
    • 0017588828 scopus 로고
    • Effects of FSH on cyclic nucleotide accumulation in testes of rats of various ages
    • Heindel J.J., Hintz M.I., Steinberger E., and Strada S.J. Effects of FSH on cyclic nucleotide accumulation in testes of rats of various ages. Endocr. Res. Commun. 4 (1977) 311-328
    • (1977) Endocr. Res. Commun. , vol.4 , pp. 311-328
    • Heindel, J.J.1    Hintz, M.I.2    Steinberger, E.3    Strada, S.J.4


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