Zakharov Vladislav V, Capony Jean-Paul, Derancourt Jean, Kropolova Ekaterina S, Novitskaya Vera A, Bogdanova Marina N, Mosevitsky Mark I
Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute of Russian Academy of Sciences, 188300 Gatchina, Leningrad District,
Biochim Biophys Acta. 2003 Jun 20;1622(1):14-9. doi: 10.1016/s0304-4165(03)00099-0.
BASP1 (also known as CAP-23 and NAP-22) is a novel myristoylated calmodulin-binding protein, abundant in nerve terminals. It is considered as a signal protein participating in neurite outgrowth and synaptic plasticity. BASP1 is also present in significant amounts in kidney, testis, and lymphoid tissues. In this study, we show that BASP1 is accompanied by at least six BASP1 immunologically related proteins (BIRPs), which are present in all animal species studied (rat, bovine, human, chicken). BIRPs have lower molecular masses than that of BASP1. Similarly to BASP1, they are myristoylated. Peptide mapping and partial sequencing have shown that BIRPs represent a set of BASP1 N-terminal fragments devoid of C-terminal parts of different length. In a definite species, the same set of BASP1 fragments is present in both brain and other tissues. The sum amount of the fragments is about 50% of the BASP1 amount in a tissue. Obligatory accompanying of BASP1 by a set of specific fragments indicates that these fragments are of physiological significance.
BASP1（也称为CAP-23和NAP-22）是一种新的肉豆蔻酰化钙调蛋白结合蛋白，在神经末梢中含量丰富。它被认为是一种参与神经突生长和突触可塑性的信号蛋白。BASP1在肾脏、睾丸和淋巴组织中也大量存在。在本研究中，我们发现BASP1至少伴随着六种与BASP1免疫相关的蛋白（BIRPs），这些蛋白存在于所有研究的动物物种（大鼠、牛、人、鸡）中。BIRPs的分子量比BASP1低。与BASP1类似，它们也被肉豆蔻酰化。肽图谱分析和部分测序表明，BIRPs代表一组不含不同长度C末端部分的BASP1 N末端片段。在特定物种中，同一组BASP1片段存在于大脑和其他组织中。这些片段的总量约为组织中BASP1含量的50%。BASP1由一组特定片段必然伴随，这表明这些片段具有生理意义。
