|
Using separate genomic strategies, two groups recently discovered the same novel peptide. Originally, five adrenomedullins (AM1-5) were cloned and identified from the pufferfish, Takifugu rubripes. Three of these [AM1/4/5] are counterparts of well-known mammalian adrenomedullins (AM) (Code PAD-4278-s and PAD-4281-s), but the other two peptides [AM2/3] were unidentified in mammals (1). Takei and coworkers attempted to detect cDNA encoded mammalian peptides corresponding to the previously identified adrenomedullins (AMs). As a result, they successfully discovered human and rat adrenomedullin 2 (AM2) as a 47-residue peptide (2). Another group utilized a phylogenetic profiling approach which led them to identify human and rat intermedin (IMD) which happened to also be a 47 amino acid peptide of these species (IMDL, named after long form of intermedin) (3), which is identical to AM2. Roh and coworkers also predicted IMDS (IMD short) as another possible product processed at the single Arg-residue, located at 7th amino acid residue downstream from the amino-terminus of IMDL. The synthetic cognate peptides of AM2 and IMD showed the following biological activities: i) dose-dependent hypotensive effects at doses between 0.1-10 nmol/kg in mice (AM2) and at 10 and 50 nM in normal and SHR rats (IMD), respectively, the efficacy of which seems to be higher than that of AM, ii) antidiuretic and antinatriuretic activities in mice (AM2), and iii) anorexic activity in fasted mice through gastric emptying suppression (IDM). It has been suggested that these activities may be regulated through its own specific receptor or through shared calcitonin receptor-like receptor (CRLR) and related proteins, such as receptor activity modifying protein (RAMP) complexes. These newly discovered AM2 peptides may serve diverse, multifunctional purposes.
Future studies should clarify AM2's role as it relates to AM function and
its family of peptides. 1) M. Ogoshi, K. Inoue, and Y. Takei, Biochem. Biophys. Res. Commun., 311, 1072 (2003). (Takifugu rubripes adrenomedullins) 2) Y. Takei, K. Inoue, M. Ogoshi, T. Kawahara, H. Bannai, and S. Miyano, FEBS Lett., 556, 53 (2004). (Original; Adrenomedullin 2) 3) J. Roh, C.L. Chang, A. Bhalla, C. Klein, and S.Y.T. Hsu, J. Biol. Chem., 279, 7264 (2004). (Original; Intermedin) |
|
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| space | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Please contact our technical sales specialists to discuss your project needs and for custom inquiries. |
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Please contact Peptides International for ordering information. |
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||