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Literature summary for 3.1.4.53 extracted from

  • Adderley, S.P.; Sprague, R.S.; Stephenson, A.H.; Hanson, M.S.
    Regulation of cAMP by phosphodiesterases in erythrocytes (2010), Pharmacol. Rep., 62, 475-482.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.53

Inhibitors

Inhibitors Comment Organism Structure
rolipram a selective inhibitor of PDE4 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol with the exception of one isoform PDE4A, PDE4 enzymes are primarily cytosolic enzymes Homo sapiens 5829
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membrane isozyme PDE4A Homo sapiens 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens recruitment of PDE4 to the beta2 adrenergic receptor ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein PDE4 activation is regulated via phosphorylation by PKA in the UCR or phosphorylation by ERK in the C-terminus, depending on the individual isoform Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
cardiac myocyte
-
 Homo sapiens
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erythrocyte
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenosine 3',5'-cyclic phosphate + H2O
-
 Homo sapiens adenosine 5'-phosphate
-
 ?
additional information recruitment of PDE4 to the beta2 adrenergic receptor Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
PDE4
-
 Homo sapiens

General Information

General Information Comment Organism
additional information PDE4 is a cAMP-specific PDE which has four subfamilies, A thru D, that include over 50 isoforms Homo sapiens
physiological function in cardiac myocytes coupling of PDE4 members to the beta2 adrenergic receptor regulates several aspects of beta2 adrenergic signaling. Inhibition of PDE4 increases cAMP in response to activation of beta2 adrenergic receptors, but has no effect on beta1 adrenergic signaling, demonstrating the selectivity of PDE association. Recruitment of PDE4 to the beta2 adrenergic receptor allows PDE4 to act locally and hydrolyze cAMP produced in response to activation of this receptor, modulating its downstream effects. PDE4 activation is regulated via phosphorylation by PKA in the UCR or phosphorylation by ERK in the C-terminus, depending on the individual isoform. The regulated release of ATP from erythrocytes occurs via a defined signaling pathway and requires increases in cAMP. It is well recognized that cAMP is a critical second messenger in diverse signaling pathways. In all cells increases in cAMP are localized and regulated by the activity of phosphodiesterases, PDEs. The subcellular localization of PDEs is recognized to be a key mechanism for compartmentalization of cyclic nucleotide signaling. PDEs within these cells regulate the compartmentalization of cAMP signaling allowing for specific cell responses. The subcellular location of PDEs is critical for coupling these enzymes to specific signal transduction pathways, which permit specific PDEs to regulate local increases in cAMP produced by activation of ligand specific receptor Homo sapiens