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Further evaluation of the biological activity of the unique gonadotropin-releasing hormone peptide in the guinea pig brain
被引:5
|作者:
Gao, Chang-Qing
[1
,2
,3
]
Fraeyman, Norbert
[3
]
Eertmans, Frank
[3
]
Dhooge, Willem
[3
]
Kaufman, Jean-Marc
[3
]
机构:
[1] Cent S Univ, XiangYa Hosp 3, Res Ctr Med Sci, Changsha 410013, Hunan, Peoples R China
[2] Cent S Univ, XiangYa Hosp 3, Dept Radiol, Changsha 410013, Hunan, Peoples R China
[3] Ghent Univ Hosp, Dept Endocrinol, B-9000 Ghent, Belgium
基金:
湖南省自然科学基金;
关键词:
Guinea pig;
GnRH;
Bioactivity;
Proteolytic degradation;
LUTEINIZING-HORMONE;
ENZYMATIC DEGRADATION;
LHRH;
ANALOGS;
PITUITARY;
CLEAVAGE;
RECEPTOR;
INVITRO;
GNRH;
D O I:
10.1016/j.neulet.2010.10.031
中图分类号:
Q189 [神经科学];
学科分类号:
071006 ;
摘要:
In this study we compared the biological activity of a unique form of gonadotropin-releasing hormone (GnRH) in the brain of the guinea pig (gpGnRH) with mammalian GnRH (mGnRH). In gpGnRH, the highly conserved histidine in position 2 (His(2)) and leucine in position 7 (Leu(7)) are substituted by tyrosine and valine, respectively. The gpGnRH was less potent than mGnRH in stimulating the release of luteinizing hormone (LH) in vivo in the guinea pig and displayed only low activity in the rat. The gpGnRH was more rapidly degraded by serum proteolytic enzymes than mGnRH. It is concluded that gpGnRH displays lower biological activity than mGnRH in both rat and guinea pig, which may be due in part to its greater susceptibility to proteolytic degradation besides differences in receptor affinity and/or activation. (C) 2010 Elsevier Ireland Ltd. All rights reserved.
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页码:246 / 249
页数:4
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