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Molecular cloning of a novel variant of the rat soluble guanylate cyclase β2 subunit
- Source :
- The International Journal of Biochemistry & Cell Biology. 36:472-480
- Publication Year :
- 2004
- Publisher :
- Elsevier BV, 2004.
-
Abstract
- Soluble guanylate cyclases (sGCs) are heterodimeric enzymes consisting of alpha and beta subunits and catalyze the formation of cGMP from GTP. The beta1 subunit has been characterized in detail, whereas the function and physiological role of the beta2 subunit are poorly understood. In this study, I isolated two distinct cDNA fragments for the beta2 subunit of sGC (beta2a and beta2b) from a rat brain cDNA library by 3' rapid amplification of cDNA ends using degenerate sense primers based on amino acid sequences conserved among membrane-bound guanylate cyclases. The deduced amino acid sequence of beta2a is identical with the corresponding sequence of the previously described beta2 subunit, whereas that of beta2b is C-terminally shorter by 46 amino acids and thus does not contain a consensus sequence for isoprenylation/carboxymethylation. Reverse transcription-polymerase chain reaction (RT-PCR) analysis demonstrated that both variants are expressed in various tissues, including kidney, liver, and brain. Although the functional significance of the C-terminal region containing the consensus sequence for isoprenylation/carboxymethylation of beta2a remains unclear yet, it is likely that these beta2 subunits play some physiological or pathophysiological role in various tissues.
- Subjects :
- GUCY1B3
DNA, Complementary
Molecular Sequence Data
Gene Expression
Biology
Biochemistry
Rats, Sprague-Dawley
Rapid amplification of cDNA ends
Complementary DNA
Consensus sequence
Animals
Amino Acid Sequence
RNA, Messenger
Cloning, Molecular
Peptide sequence
Gene Library
GUCY1A2
Base Sequence
Reverse Transcriptase Polymerase Chain Reaction
cDNA library
GUCY1A3
Brain
Cell Biology
Molecular biology
Rats
Blotting, Southern
Guanylate Cyclase
Female
Sequence Alignment
Subjects
Details
- ISSN :
- 13572725
- Volume :
- 36
- Database :
- OpenAIRE
- Journal :
- The International Journal of Biochemistry & Cell Biology
- Accession number :
- edsair.doi.dedup.....47d3456f629a0f51685a6b4a8e0a08d9