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

I. I. Senin1*, 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
Antibodies AB60-72 and AB80-92 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 AB60-72 or AB80-92 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 AB60-72 or AB80-92 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.
KEY WORDS: Ca2+-dependent antibodies, Ca2+-myristoyl switch, cancer associated retinopathy, recoverin

DOI: 10.1134/S0006297911030060