Somatostatin-28 encoded in a cloned cDNA obtained from a rat medullary thyroid carcinoma
Autor: | John W. Jacobs, P C Dee, Joel F. Habener, Richard H. Goodman |
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Rok vydání: | 1982 |
Předmět: |
chemistry.chemical_classification
endocrine system Hybridization probe Nucleic acid sequence Cell Biology Biology Biochemistry Molecular biology Homology (biology) Amino acid Somatostatin chemistry Complementary DNA Somatostatin-28 Molecular Biology Peptide sequence hormones hormone substitutes and hormone antagonists |
Zdroj: | Journal of Biological Chemistry. 257:1156-1159 |
ISSN: | 0021-9258 |
DOI: | 10.1016/s0021-9258(19)68167-6 |
Popis: | We have constructed and cloned in bacteria complementary DNAs derived from a transplantable rat medullary thyroid carcinoma. Using a hybridization probe encoding an anglerfish islet pre-prosomatostatin, a precursor of the tetradecapeptide somatostatin, we have identified and isolated a clone containing a 400-base pair complementary DNA encoding most of the rat carcinoma pre-prosomatostatin. The amino acid sequence of the tetradecapeptide somatostatin and of the amino-terminally extended form, somatostatin-28 was deduced from the nucleotide sequence of the complementary DNA. Somatostatin-28 was found at the COOH terminus of a polypeptide of at least 80 amino acids indicating that somatostatin-28 arises by cleavage from a large precursor. The sequences of somatostatin-28 and somatostatin-14 are strictly conserved between the rat and other mammals. Such conservation of these sequences indicates strong selective pressures during evolution to maintain the sequence and suggests that somatostatin-28 may serve some essential biologic functions apart from, or in addition to, the important regulatory actions of somatostatin-14. Additionally, we found a high degree of homology in the amino acid sequences of the NH2-terminal extension peptides in the anglerfish islet and the rat carcinoma pre-prosomatostatins pointing further to a possible biologic function of these extension peptides. |
Databáze: | OpenAIRE |
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