| Autor: |
Wechsler, Jeremy, Choi, Young-Hun, Krall, Judith, Ahmad, Faiyaz, Manganiello, Vincent C., Movsesian, Matthew A. |
| Zdroj: |
Journal of Biological Chemistry; October 2002, Vol. 277 Issue: 41 p38072-38078, 7p |
| Abstrakt: |
PDE3A cyclic nucleotide phosphodiesterases regulate cAMP- and cGMP-mediated intracellular signaling in cardiac myocytes. We used antibodies to different regions of PDE3A to demonstrate the presence of three PDE3A isoforms in these cells. These isoforms, whose apparent molecular weights are 136,000, 118,000, and 94,000 (“PDE3A-136,” “PDE3A-118,” and “PDE3A-94”), are identical save for the deletion of different lengths of N-terminal sequence containing two membrane-association domains and sites for phosphorylation/activation by protein kinase B (“PK-B”) and protein kinase A (“PK-A”). PDE3A-136 contains both membrane-association domains and the PK-B and PK-A sites. PDE3A-118 contains only the downstream membrane-association domain and the PK-A sites. PDE3A-94 lacks both membrane localization domains and the PK-B and PK-A sites. The three isoforms are translated from two mRNAs derived from thePDE3A1gene: PDE3A-136 is translated from PDE3A1 mRNA, whereas PDE3A-118 and PDE3A-94 are translated from PDE3A2 mRNA. Experiments involving in vitrotranscription/translation indicate that PDE3A-118 and PDE3A-94 may be translated from different AUGs in PDE3A2 mRNA. These findings suggest that alternative transcriptional and post-transcriptional processing of thePDE3Agene results in the generation of two mRNAs and three protein isoforms in cardiac myocytes that differ with respect to intracellular localization and may be regulated through different signaling pathways. |
| Databáze: |
Supplemental Index |
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