Phosphodiesterases 4D and 7A splice variants in the response of HUVEC cells to TNF-α

Biochemical and Biophysical Research Communications

Volumn 274, Issue 2, 2000, Pages 415-421

  Miró, Xavier ^a   Casacuberta, Josep M ^a   Gutiérrez López, María D ^b   De Landázuri, Manuel O ^b   Puigdomènech, Pere ^a  

^a INSTITUT DE BIOLOGIA MOLECULAR DE BARCELONA   (Spain)

^b UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

Author keywords

Alternative splicing; cAMP phosphodiesterase; Endothelium; Gene expression; Inflammation; Tumor necrosis factor

Indexed keywords

ISOENZYME; MESSENGER RNA; PHOSPHODIESTERASE; PHOSPHODIESTERASE IV; PHOSPHODIESTERASE VII; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

ARTICLE; ENDOTHELIUM CELL; ENZYME REGULATION; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA SPLICING; UMBILICAL VEIN;

EID: 0034596252     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.3146     Document Type: Article

References (32)

1. Houslay M. D., Milligan G. Tailoring cAMP-signalling responses through isoform multiplicity. Trends Biochem. 22:1997;217-224.
2. Conti M., Jin S. L. The molecular biology of cyclic nucleotide phosphodiesterases. Prog. Nucleic Acid Res. Mol. Biol. 63:1999;1-38.
3. Fawcett L., Baxendale R., Stacey P., McGrouther C., Harrow I., Soderling S., Hetman J., Beavo J. A., Phillips S. C. Molecular cloning and characterization of a distinct human phosphodiesterase gene family: PDE11A. Proc. Natl. Acad. Sci. USA. 97:2000;3702-3707.
4. Houslay M. D., Sullivan M., 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.
5. Hetman J. M., Soderling S. H., Glavas N. A., Beavo J. A. Cloning and characterization of PDE7B, a cAMP-specific phosphodiesterase. Proc. Natl. Acad. Sci. USA. 97:2000;472-476.
6. Texeira M. M., Gristwood R. W., Cooper N., Hellewell P. G. Phosphodiesterase (PDE)4 inhibitors: Anti-inflammatory drugs of the future? Trends Pharmacol. Sci. 18:1997;164-170.
7. Barnette M. S., Christensen S. B., Essayan D. M., Grous M., Prabhakar U., Rush J. A., Kagey-Sobotka A., Torphy T. J. SB 207499 (Ariflo), a potent and selective second-generation phosphodiesterase 4 inhibitor: In vitro anti-inflammatory actions. J. Pharmacol. Exp. Ther. 284:1998;420-426.
8. Duplantier A. J., Biggers M. S., Chambers R. J., Cheng J. B., Cooper K., Damon D. B., Eggler J. F., Kraus K. G., Marfat A., Masamune H., Pillar J. S., Shirley J. T., Umland J. P., Watson J. W. Biarylcarboxylic acids and -amides: Inhibition of phosphodiesterase type IV versus [3H]rolipram binding activity and their relationship to emetic behavior in the ferret. J. Med. Chem. 39:1996;120-125.
9. Alvarez R., Sette C., Yang D., Eglen R. M., Wilhelm R., Shelton E. R., Conti M. Activation and selective inhibition of a cyclic AMP-specific phosphodiesterase, PDE-4D3. Mol. Pharmacol. 48:1995;616-622.
10. Martínez A., Castro A., Gil C., Miralpeix M., Segarra V., Domènech T., Beleta J., Palacios J. M., Ryder H., Miró X., Bonet C., Casacuberta J. M., Azorín F., Piña B., Puigdomènech P. Benzyl derivatives of 2,1,3-benzo- and benzothieno[3,2-a]thiadiazine 2,2-dioxides: First phosphodiesterase 7 inhibitors. J. Med. Chem. 43:2000;683-689.
11. Li L., Yee C., Beavo J. A. CD3- and CD28-dependent induction of PDE7 required for T cell activation. Science. 283:1999;848-851.
12. Muñoz C., Castellanos M. C., Alfranca A., Vara A., Esteban M. A., Redondo J. M., O. de Landazuri M. Transcriptional up-regulation of intracellular adhesion molecule-1 in human endothelial cells by the antioxidant pyrrolidine dithiocarbamate involves the activation of activating protein-1. J. Immunol. 157:1996;3587-3597.
13. Erdogan S., Houslay M. D. Challenge of human Jurkat T-cells with the adenylate cyclase activator forskolin elicits major changes in cAMP phosphodiesterase (PDE) expression by up-regulating PDE3 and inducing PDE4D1 and PDE4D2 splice variants as well as down-regulating a novel PDE4A splice variant. Biochem. J. 321:1997;165-175.
14. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
15. Pompeiano M., Palacios J. M., Mengod G. Distribution of the serotonin 5-HT2 receptor family mRNAs: Comparison between 5-HT2A and 5-HT2C receptors. Mol. Brain Res. 23:1994;163-178.
16. Vilaro M. T., Wiederhold K. H., Palacios J. M., Mengod G. Muscarinic M2 receptor mRNA expression and receptor binding in cholinergic and non-cholinergic cells in the rat brain: A correlative study using in situ hybridization histochemistry and receptor autoradiography. Neuroscience. 47:1992;367-393.
17. Carlos T. M., Harlan J. M. Leukocyte-endothelial adhesion molecules. Blood. 84:1994;2068-2101.
18. Michaeli T., Bloom T. J., Martins T., Loughney K., Ferguson K., Riggs M., Rodgers L., Beavo J. A., Wigler M. Isolation and characterization of a previously undetected human cAMP phosphodiesterase by complementation of cAMP phosphodiesterase-deficient Saccharomyces cerevisiae. J. Biol. Chem. 268:1993;12925-12932.
19. Sullivan M., Rena G., Begg F., Gordon L., Olsen A. S., Houslay M. D. Identification and characterization of the human homologue of the short PDE4A cAMP-specific phosphodiesterase RD1 (PDE4A1) by analysis of the human HSPDE4A gene locus located at chromosome 19p13.2. Biochem. J. 333:1998;693-703.
20. Monaco L., Vicini E., Conti M. Structure of two rat genes coding for closely related rolipram-sensitive cAMP phosphodiesterases. Multiple mRNA variants originate from alternative splicing and multiple start sites. J. Biol. Chem. 269:1994;347-357.
21. Springer T. A. Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm. Cell. 76:1994;301-314.
22. Bevilacqua M. P., Stengelin S., Gimbrone J. M. A., Seed B. Endothelial leukocyte adhesion molecule 1: An inducible receptor for neutrophils related to complement regulatory proteins and lectins. Science. 243:1989;1160-1165.
23. Osborn L., Hession C., Tizard R., Vassallo C., Luhowskyj S., Chi-Rosso G., Lobb R. Direct expression cloning of vascular cell adhesion molecule 1, a cytokine-induced endothelial protein that binds to lymphocytes. Cell. 59:1989;1203-1211.
24. Jin S. C., Bushnik T., Lan L., Conti M. Impaired growth and fertility of cAMP-specific phosphodiesterase PDE4D-deficient mice. J. Biol. Chem. 273:1998;19672-19678.
25. Yarwood S. J., Steele M. R., Scotland G., Houslay M. D., Bolger G. B. The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform. J. Biol. Chem. 274:1999;14909-14917.
26. Beard M. B., O'Connell J. C., Bolger G. B., Houslay M. D. The unique N-terminal domain of the cAMP phosphodiesterase PDE4D4 allows for interaction with specific SH3 domains. FEBS Lett. 460:1999;173-177.
27. Bolger G., Michaeli T., Martins T., St John T., Steiner B., Rodgers L., Riggs M., Wigler M., Ferguson K. A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol. Cell. Biol. 13:1993;6558-6571.
28. Horton Y. M., Sullivan M., Houslay M. D. Molecular cloning of a novel splice variant of human type IVA (PDE-IVA) cyclic AMP phosphodiesterase and localization of the gene to the p13.2-q12 region of human chromosome 19. Biochem. J. 308:1995;683-691.
29. Baker B. S. Sex in flies: The splice of life. Nature. 340:1989;521-524.
30. Richardson A., Parsons J. T. A mechanism for regulation of the adhesion-associated proteintyrosine kinase pp125FAK. Nature. 380:1996;538-540.
31. Nakabeppu Y., Nathans D. A naturally occurring truncated form of FosB that inhibits Fos/Jun transcriptional activity. Cell. 64:1991;751-759.
32. Behrends S., Harteneck C., Schultz G., Koesling D. A variant of the alpha 2 subunit of soluble guanylyl cyclase contains an insert homologous to a region within adenylyl cyclases and functions as a dominant negative protein. J. Biol. Chem. 270:1995;21109-21113.