Gene and precursor structure of porcine C-type natriuretic peptide
| Autor: | Kayoko Fuchimura, Yasunori Tawaragi, Naoto Minamino, Hiroshi Nakazato, Shoji Tanaka, Kenji Kangawa, Hisayuki Matsuo |
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| Rok vydání: | 1990 |
| Předmět: |
Signal peptide
Swine medicine.drug_class Genetic Vectors Molecular Sequence Data Restriction Mapping Biophysics Peptide Biology Transfection Biochemistry Cell Line Complementary DNA Natriuretic peptide medicine Animals Amino Acid Sequence RNA Messenger Cloning Molecular Protein Precursors Molecular Biology Peptide sequence chemistry.chemical_classification Genomic Library Base Sequence Nucleic acid sequence Intron Brain DNA Cell Biology Molecular biology NPR2 Genes chemistry Atrial Natriuretic Factor |
| Zdroj: | Biochemical and Biophysical Research Communications. 172:627-632 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(90)90720-8 |
| Popis: | Recently we isolated from porcine brain two related peptides, a 22-residue peptide (CNP-22) and its N-terminally elongated peptide (CNP-53; 53-residue), which belong to the third type of mammalian natriuretic peptide designated C-type natriuretic peptide family (CNP) (1,2). To elucidate the structure of their precursor form, we have now isolated the gene for this porcine CNP and prepared its cDNA from COS-1 cells transfected with the gene. Nucleotide sequence analyses have revealed that the gene consists of at least two exons and an intron and encodes the 126-residue CNP precursor (porcine prepro-CNP), in which a putative signal peptide and the CNP-53 sequence are located at the N- and C-terminus, respectively. The C-terminal cysteine codon of CNP-53 is directly followed by a termination codon, indicating that the C-terminus of porcine CNP is generated per se. |
| Databáze: | OpenAIRE |
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