Atria1 natriurctic pptidc(ANP) nnd brnin nrtriurclic pcplidc @PIP) huvc diffcrcnt C-terminal tail ~tru~~~rcs compared with the rathsrconccrvativc ring structures whish consist of 17 umino acid r&dun, To cxrminc the diffcrcm effects ofthc tuil rlructum of ANPand BNP on their inlcraction with receptors. WC rynthcsizcd scvcrul pcptide tinvlasr und mcrr;urcd their biolosicnl uctionr in three difl'crcnt assay systems. D&ion of tk C-tclminnl tuil from rut BNP did not cffcct the ve~rclrrution nclivity rrgrrina rut aortu. but it promoicd cGMP praduction in cultured rat aortic smooth mu& ccllr (RASMC). Deletion of ihc CXcnninal tail from rat ANP diminirhcd both vusorcl;lxunt and cGMP producing activities. In Y binding competition artiy with .the competition activitiw of bolh ANP ond BNP wcrc grciatly rcduccd by Cmtcnninul dclcrion. In &Won. WC obtained ngonirtl with novel rcccplor selcrtivity.
Two dimeric forms of human a-atria1 natriuretic peptide (a-ANP) were synthesized by solution methods and compared with monomeric a-ANP in terms of some biological and immunochemical properties. The parallel form @'-ANP) and the antiparallel form (B-ANP) were equipotent in smooth muscle relaxant activity in isolated rat aorta and their ED,, values were estimated to be 1.7 x lo-* M and 1.6 x 10e8,M, respectively. Diuretic and natriuretic responses induced by fi-ANP and ,Y'-ANP in anesthetized rats were equally less potent but exhibited a significantly longer duration than those induced by a-ANP. fi-ANP and /3'-ANP possessed immunoreactivities of 6&100% and S&90% (a-ANP, 100% on a molar basis), respectively, with three different antisera raised against cc-ANP-related peptides.Peptide synthesis Atria1 natriureticpeptide Muscle relaxation Diuresis Natriuresis Immunoreactivity
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