Guanylate-cyclase-inhibitory protein is a frog retinal Ca2+-binding protein related to mammalian guanylate-cyclase-activating proteins

被引:42
作者
Li, N
Fariss, RN
Zhang, K
Otto-Bruc, A
Haeseleer, F
Bronson, D
Qin, N
Yamazaki, A
Subbaraya, I
Milam, AH
Palczewski, K
Baehr, W
机构
[1] Univ Utah, Hlth Sci Ctr, Moran Eye Ctr, Salt Lake City, UT 84132 USA
[2] Baylor Coll Med, Dept Biochem, Houston, TX 77030 USA
[3] Univ Washington, Sch Med, Dept Ophthalmol, Seattle, WA 98195 USA
[4] Baylor Coll Med, Dept Physiol & Biophys, Houston, TX 77030 USA
[5] Baylor Coll Med, Dept Ophthalmol, Houston, TX 77030 USA
[6] Wayne State Univ, Sch Med, Kresge Eye Inst, Dept Ophthalmol, Detroit, MI 48202 USA
[7] Wayne State Univ, Sch Med, Kresge Eye Inst, Dept Pharmacol, Detroit, MI 48202 USA
[8] Univ Washington, Sch Med, Dept Pharmacol, Seattle, WA 98195 USA
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1998年 / 252卷 / 03期
关键词
calcium-binding protein; guanylate-cyclase-activating protein; photoreceptor; frog retina;
D O I
10.1046/j.1432-1327.1998.2520591.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Two guanylate-cyclase-activating proteins (GCAP) encoded by a tail-to-tail gene array have been characterized in the mammalian retina. Using frog retina as a model, we obtained evidence for the presence of a photoreceptor Ca2+-binding protein closely related to GCAP. This protein (206 amino acids) does not stimulate guanylate cyclase (GC) in low [Ca2+], but inhibits GC in high [Ca2+], and is therefore termed guanylate-cyclase-inhibitory protein (GCIP). Sequence analysis indicates that GCIP and GCAP1 and GCAP2 have diverged substantially, but conserved domains present in all vertebrate GCAP are present in GCIP. Moreover, partial characterization of the GCIP gene showed that the positions of two introns in the GCIP gene are identical to positions of corresponding introns of the mammalian GCAP gene array. As to the major differences between GCIP and GCAP, the fourth EF hand Ca2+-binding motif of GCIP is disabled for Ca2+ binding, and GCIP does not stimulate GC. Monoclonal and polyclonal antibodies raised against recombinant GCIP identified high levels of GCIP in the inner segments, somata and synaptic terminals of frog cone photoreceptors. The results suggest that GCIP is a Ca2+-binding protein of the GCAP/recoverin subfamily. Its localization in frog cones closely resembles that of GC in mammalian cones. GCIP inhibits GC at high free [Ca2+], competing with GCAP1 and GCAP2 for GC regulatory sites.
引用
收藏
页码:591 / 599
页数:9
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