Molecular Cloning of a cDNA Encoding the Precursor of Adenoregulin from Frog Skin: Relationships with the Vertebrate Defensive Peptides, Dermaseptins

• Published in: Biochemical and biophysical research communications Vol. 191; no. 3; pp. 983 - 990
• Main Authors: Amiche, M., Ducancel, F., Lajeunesse, E., Boulain, J.C., Menez, A., Nicolas, P.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 31.03.1993; Elsevier
• Subjects: Amino Acid Sequence; Amphibian Proteins; Animals; Antimicrobial Cationic Peptides; Base Sequence; Biological and medical sciences; Cloning, Molecular; DNA - genetics; Fundamental and applied biological sciences. Psychology; Genes. Genome; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Peptides - chemistry; Peptides - genetics; Protein Structure, Secondary; Ranidae - genetics; Sequence Alignment; Solubility; Vertebrata; Complementary DNA; Peptides; Nucleotide sequence; Amphibia; Salientia; Skin; Molecular cloning; Antimicrobial agent; Aminoacid sequence
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1993.1314

Adenoregulin has recently been isolated from Phyllomedusa skin as a 33 amino acid residues peptide which enhanced binding of agonists to the A1 adenosine receptor. In order to study the structure of the precursor of adenoregulin we constructed a cDNA library fom mRNAs extracted from the skin of Phyllomedusa bicolor. We detected the complete nucleotide sequence of a cDNA encoding the adenoregulin biosynthetic precursor. The deduced sequence of the precursor is 81 amino acids long, exhibits a putative signal sequence at the NH2 terminus and contains a single copy of the biologically active peptide at the COOH terminus. Structural and conformational homologies that are observed between adenoregulin and the dermaseptins, antimicrobial peptides exhibiting strong membranolytic activities against various pathogenic agents, suggest that adenoregulin is an additional member of the growing family of cytotropic antimicrobial peptides that allow vertebrate animals to defend themselves against microorganisms. As such, the adenosine receptor regulating activity of adenoregulin could be due to its ability to interact with and disrupt membranes lipid bilayers.