Hofmann S L, Goldstein J L, Orth K, Moomaw C R, Slaughter C A, Brown M S
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
J Biol Chem. 1989 Oct 25;264(30):18083-90.
We reported previously the purification of a 165-kDa muscle-specific protein identified by virtue of its ability to bind 125I-labeled low density lipoprotein with high affinity after sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Hoffmann, S. L., Brown, M. S., Lee, E., Pathak, R. K., Anderson, R. G. W., and Goldstein, J. J. (1989) J. Biol. Chem. 264, 8260-8270). The protein is located in the lumen of the sarcoplasmic reticulum, where it has no access to plasma lipoproteins. It binds to 45Ca2+ on nitrocellulose blots and stains metachromatically blue with Stains-all, a cationic dye that stains Ca2+-binding proteins. In the current paper, we have isolated a full-length rabbit cDNA clone for the 165-kDa protein. The deduced amino acid sequence reveals a 852-amino acid protein with the following structural features: 1) an NH2-terminal 27-residue putative signal sequence; 2) a highly repetitive region containing nine nearly identical tandem repeats of 29 residues, each consisting of a histidine-rich sequence HRHRGH, a stretch of 10-11 acidic amino acids, and a sequence containing 2 serines and a threonine in a negatively charged context; 3) a 13-residue stretch of polyglutamic acid; and 4) a COOH-terminal cluster of 14 closely spaced cysteine residues with the repeating pattern of Cys-X-X-Cys suggestive of a heavy metal binding domain. Histidine, aspartic acid, and glutamic acid accounted, respectively, for 13, 12, and 19% of the amino acids. The protein does not share any significant sequence homology with the cell surface low density lipoprotein receptor. Stretches of acidic amino acids are a feature of two other luminal sarcoplasmic reticulum proteins, suggesting that these may be a general feature of luminal sarcoplasmic reticulum proteins. We suggest that the histidine-rich Ca2+-binding protein described in the current study be designated HCP. The role of HCP in Ca2+ homeostasis in the sarcoplasmic reticulum of skeletal and cardiac muscle remains to be determined.
我们先前报道过一种165kDa的肌肉特异性蛋白的纯化,该蛋白是通过在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳后,凭借其能与125I标记的低密度脂蛋白高亲和力结合的能力而鉴定出来的(霍夫曼,S.L.,布朗,M.S.,李,E.,帕塔克,R.K.,安德森,R.G.W.,以及戈尔茨坦,J.J.(1989年)《生物化学杂志》264卷,8260 - 8270页)。该蛋白位于肌浆网腔中,在此处它无法接触到血浆脂蛋白。它在硝酸纤维素印迹上能结合45Ca2+,并用阳离子染料“全染剂”进行异染呈蓝色,“全染剂”可对Ca2+结合蛋白进行染色。在当前论文中,我们分离出了该165kDa蛋白的全长兔cDNA克隆。推导的氨基酸序列显示该蛋白由852个氨基酸组成,具有以下结构特征:1)一个NH2末端的27个残基的假定信号序列;2)一个高度重复区域,包含9个几乎相同的29个残基的串联重复序列,每个重复序列由富含组氨酸的序列HRHRGH、一段10 - 11个酸性氨基酸以及一个在带负电荷环境中包含2个丝氨酸和1个苏氨酸的序列组成;3)一段13个残基的聚谷氨酸序列;4)一个COOH末端的由14个紧密排列的半胱氨酸残基组成的簇,其半胱氨酸的重复模式为Cys - X - X - Cys,提示存在一个重金属结合结构域。组氨酸、天冬氨酸和谷氨酸分别占氨基酸的13%、12%和19%。该蛋白与细胞表面低密度脂蛋白受体没有任何显著的序列同源性。酸性氨基酸序列片段是另外两种肌浆网腔蛋白的特征,这表明这些可能是肌浆网腔蛋白的普遍特征。我们建议将本研究中描述的富含组氨酸的Ca2+结合蛋白命名为HCP。HCP在骨骼肌和心肌肌浆网中Ca2+稳态中的作用仍有待确定。