Amino Acid Sequences of Two Immune-Dominant Epitopes of Recoverin Are Involved in Ca²⁺/Recoverin-Dependent Inhibition of Phosphorylation of Rhodopsin

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I. I. Senin^1*, N. K. Tikhomirova¹, V. A. Churumova¹, I. I. Grigoriev¹, T. A. Kolpakova¹, D. V. Zinchenko², P. P. Philippov¹, and E. Yu. Zernii¹

¹Department of Cell Signaling, Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: (495) 939-2344; E-mail: senin@belozersky.msu.ru

²Laboratory of Protein Chemistry, Pushchino Branch of the Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, 142290 Pushchino, Moscow Region, Russia

^* To whom correspondence should be addressed.

Received November 11, 2010; Revision received November 19, 2010

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Antibodies AB^60-72 and AB^80-92 against two immune-dominant epitopes of photoreceptor Ca²⁺-binding protein recoverin, 60-DPKAYAQHVFRSF-72 and 80-LDFKEYVIALHMT-92, which can be exposed in a Ca²⁺-dependent manner, were obtained. The presence of AB^60-72 or AB^80-92 results in a slight increase in Ca²⁺-affinity of recoverin and does not affect significantly a Ca²⁺-myristoyl switch mechanism of the protein. However in the presence of AB^60-72 or AB^80-92 recoverin loses its ability to interact with rhodopsin kinase and consequently to perform a function of Ca²⁺-sensitive inhibitor of rhodopsin phosphorylation in photoreceptor cells.

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KEY WORDS: Ca²⁺-dependent antibodies, Ca²⁺-myristoyl switch, cancer associated retinopathy, recoverin

DOI: 10.1134/S0006297911030060

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