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Alternative Splicing of the High Affinity cAMP-Specific Phosphodiesterase (PDE7A) mRNA in Human Skeletal Muscle and Heart
- Source :
- Journal of Biological Chemistry. 272:16152-16157
- Publication Year :
- 1997
- Publisher :
- Elsevier BV, 1997.
-
Abstract
- To further our understanding of the structure and function of phosphodiesterases of the newly identified family of high affinity cAMP-specific phosphodiesterases (PDE7), we identified and characterized the isozyme expressed in human skeletal muscle and the protein product of the previously isolated isozyme HCP1 (designated HSPDE7A1). We report the isolation of a cDNA encoding the full-length skeletal muscle isoform of human PDE7A (HSPDE7A2). The DNA sequence of this skeletal muscle cDNA indicates thatPDE7A2 is a novel 5′ splice variant of PDE7Aencoding an isoform with a novel, hydrophobic N terminus. The 456-amino acid PDE7A2 protein is detected on Western blots as a band with an apparent mobility of 50 kDa. PDE7A2 is a high affinity cAMP-specific PDE (K m = 0.1 μm), which is localized to particulate cellular fractions. The PDE7A1 (HCP1) isozyme is detected on Western blots as a band with an apparent mobility of 57 kDa, demonstrating that the previously isolated HCP1cDNA encodes the full-length PDE7A1 protein. The even distribution of PDE7A mRNA among fetal tissues and the relative abundance of its two mRNAs strongly suggest that the expression ofPDE7A is regulated throughout development.
- Subjects :
- Gene isoform
DNA, Complementary
Molecular Sequence Data
Biology
Biochemistry
Isozyme
Complementary DNA
medicine
Humans
RNA, Messenger
Muscle, Skeletal
Molecular Biology
Messenger RNA
Base Sequence
Myocardium
Alternative splicing
Gene Expression Regulation, Developmental
Phosphodiesterase
Skeletal muscle
Cell Biology
Molecular biology
Isoenzymes
Blot
Alternative Splicing
medicine.anatomical_structure
3',5'-Cyclic-AMP Phosphodiesterases
Subjects
Details
- ISSN :
- 00219258
- Volume :
- 272
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry
- Accession number :
- edsair.doi.dedup.....880233fde52322f71f440df6b6e9caa0