The human serum deprivation response gene (SDPR) maps to 2q32-q33 and codes for a phosphatidylserine-binding protein
The human serum deprivation response gene (SDPR) maps to 2q32-q33 and codes for a phosphatidylserine-binding protein
复制标题
DOI：
10.1006/geno.1998.5733
复制
发表时间：
1999-04-01
期刊：
影响因子：
4.4
通讯作者：
Schneider, C
中科院分区：
文献类型：
--
作者：
Gustincich, S;Vatta, P;Schneider, C
血清剥夺反应基因（SDPR，别名sdr）先前已被分离，其高mRNA表达在血清饥饿的细胞相比，接触抑制的NIH 3 T3细胞;这种调节是没有观察到在单癌基因转化的NIH 3 T3细胞后血清饥饿。最近，Sdpr已被确定为蛋白激酶C（PKC）的底物：这种相互作用决定了PKC与小窝的比较，小窝是一种质膜内陷，其中Sdpr是主要成分。在转化细胞中缺乏Sdpr-PKC相互作用已被认为与PKC亚细胞定位和底物特异性的改变有关。本文报道了人SDPR同源物（HGMW批准的符号SDPR）的克隆及其在人类基因组2 q32-q33的定位。与鼠系统类似，当人成纤维细胞血清饥饿时，SDPR mRNA表达增加，其在同步细胞周期再进入期间下调，但在接触抑制所抑制的细胞中不诱导。SDPR在人体组织中的表达分析揭示了一种几乎普遍存在的表达，在心脏和肺中发现了最高水平。我们发现，人类SDPR编码PS-p68，一个以前的特点是磷脂酰丝氨酸结合蛋白纯化的人血小板。因此，重组Sdpr能够在不存在Ca 2+的情况下特异性结合磷脂酰丝氨酸。SDPR与数据库中的两个基因同源。其中之一srbc在生长停滞期间受到类似的调节，并编码作为PKC底物的磷脂酰丝氨酸结合蛋白。(C)北京：科学出版社.
The serum deprivation response gene (SDPR, alias sdr) has been previously isolated for its high mRNA expression in serum-starved cells compared to contact-inhibited NIH3T3 cells; such regulation is not observed in single-oncogene transformed NIH3T3 cells after serum starvation. More recently Sdpr has been identified as a substrate of protein kinase C (PKC): this interaction determines the compartimentalization of PKC to caveolae, a plasma membrane invagination of which Sdpr is a major component. Lack of Sdpr-PKC interaction in transformed cells has been proposed to be involved in the alteration of PKC subcellular localization and substrate specificity, Here we report the cloning of the human SDPR homologue (HGMW-approved symbol SDPR) and its mapping to 2q32-q33 in the human genome. In analogy with the murine system, SDPR mRNA expression is increased when human fibroblasts are serum starved, it becomes down-regulated during synchronous cell-cycle reentry, but it is not induced in cells arrested by contact inhibition. Analysis of SDPR expression in human tissues reveals a near ubiquitous expression, with highest levels found in heart and lung. We show that human SDPR encodes PS-p68, a previously characterized phosphatidylserine-binding protein purified from human platelets. Accordingly, recombinant Sdpr is able to specifically bind phosphatidylserine in the absence of Ca2+. SDPR is homologous to two genes in the databank. one of which, srbc, is similarly regulated during growth arrest and encodes a phosphatidylserine-binding protein that is a substrate of PKC. (C) 1999 Academic Press.