ATRIAL-NATRIURETIC-PEPTIDE BINDS TO ANP-R(1) RECEPTORS IN NEUROBLASTOMA-CELLS OR IS DEGRADED EXTRACELLULARLY AT THE SER-PHE BOND

被引:23
作者
DELPORTE, C [1 ]
POLOCZEK, P [1 ]
TASTENOY, M [1 ]
WINAND, J [1 ]
CHRISTOPHE, J [1 ]
机构
[1] UNIV LIBRE BRUXELLES,SCH MED,DEPT BIOCHEM & NUTR,BLDG G-E,CP 611,ROUTE LENNIK 808,B-1070 BRUSSELS,BELGIUM
来源
EUROPEAN JOURNAL OF PHARMACOLOGY-MOLECULAR PHARMACOLOGY SECTION | 1992年 / 227卷 / 03期
关键词
ANP-R(1) RECEPTORS; CGMP; NEUTRAL METALLOENDOPEPTIDASE; HUMAN NEUROBLASTOMA CELL LINE NB-OK1;
D O I
10.1016/0922-4106(92)90002-D
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
ANP-R1 receptors for atrial natriuretic peptide (ANP) showed the following rank order of affinity in intact human neuroblastoma cells NB-OK-1: human ANP-(99-126) almost-equal-to human ANP-(102-126) almost-equal-to rat ANP-(99-126) (K(I) 17-32 pM) > human ANP-(103-126) > porcine brain natriuretic peptide (BNP). Analogues truncated at the C-terminal extremity or devoid of a disulphide bridge, such as rat ANP-(103-123), rat C-ANP-(102-121), rat ANP-(111-126), rat ANP-(99-109) and rat [desCys105,Cys121]ANP-(104-126) and chicken C-type natriuretic peptide, were not recognized. The occupancy of these high affinity ANP-R1 receptors led to marked cyclic GMP accumulation in the presence of 3-isobutyl 1-methylxanthine. An ectoenzymic activity, partly shed in the incubation medium, provoked the stepwise release of Phe-Arg-[I-125]Tyr, Arg-[I-125]Tyr and [I-125]Tyr from rat [I-125]ANP-(99-126), at an optimal pH of 7.0. Its inhibition by 1,10-phenanthroline, EDTA and bacitracin but not by thiorphan suggests the contribution of at least one neutral metalloendopeptidase, distinct from EC 3.4.24.11, for which ANP showed high affinity.
引用
收藏
页码:247 / 256
页数:10
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