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淋巴母细胞中钙调蛋白及钙调蛋白结合蛋白的表达

Expression of calmodulin and calmodulin binding proteins in lymphoblastoid cells.

作者信息

Colomer J, Agell N, Engel P, Bachs O

机构信息

Departament de Biologia Cellular, Facultat de Medicina, Universitat de Barcelona, Spain.

出版信息

J Cell Physiol. 1994 Jun;159(3):542-50. doi: 10.1002/jcp.1041590318.

Abstract

Calmodulin is encoded in vertebrates by three different genes: CALM1, CALM2, and CALM3. We have examined the mRNAs expressed from these three genes in eight lines of human lymphoblastoid cells (Namalwa, Raji, Ramos, JY, Molt-4, Jurkat, CEM, and HPB-ALL). We found that all these cell lines (except Ramos) overexpressed CALM3 transcripts, which led to an increase of total CaM protein with respect to quiescent normal T lymphocytes. The nuclear concentration of calmodulin was measured in two of these lymphoblastoid cell lines (JY and HPB-ALL) and compared to quiescent and phytohemagglutinin-activated T lymphocytes. Activated lymphocytes showed a 2-fold increase of nuclear calmodulin with respect to quiescent cells, whereas in the two lymphoblastoid cell lines, nuclear calmodulin remained similar to that of quiescent cells. The levels of a calmodulin-binding protein of 150 kDa in the homogenates of the eight lymphoblastoid lines was found to be higher than those of quiescent and activated lymphocytes. Likewise, the amount of three calmodulin-binding proteins of 240, 200, and 170 kDa was also increased in several of the cell lines, but not in all of them. The 170-kDa protein was only expressed by activated lymphocytes and lymphoblastoid cells, suggesting that it could be specific for proliferating cells. In the nuclei of activated lymphocytes and lymphoblastoid cells, a decrease of a calmodulin-binding protein of 110 kDa and increases of three other of 240, 180 and 170 kDa were also detected.

摘要

在脊椎动物中,钙调蛋白由三个不同的基因编码:CALM1、CALM2和CALM3。我们检测了这三个基因在八个人类淋巴母细胞系(Namalwa、Raji、Ramos、JY、Molt-4、Jurkat、CEM和HPB-ALL)中表达的mRNA。我们发现,所有这些细胞系(除Ramos外)均过度表达CALM3转录本,这导致相对于静止的正常T淋巴细胞,总钙调蛋白水平增加。在其中两个淋巴母细胞系(JY和HPB-ALL)中测量了钙调蛋白的核浓度,并与静止的和经植物血凝素激活的T淋巴细胞进行了比较。激活的淋巴细胞与静止细胞相比,核钙调蛋白增加了两倍,而在这两个淋巴母细胞系中,核钙调蛋白水平与静止细胞相似。发现八个淋巴母细胞系匀浆中150 kDa的钙调蛋白结合蛋白水平高于静止和激活的淋巴细胞。同样,几个细胞系中240、200和170 kDa的三种钙调蛋白结合蛋白的量也增加了,但并非所有细胞系都如此。170 kDa的蛋白仅在激活的淋巴细胞和淋巴母细胞中表达,这表明它可能是增殖细胞特有的。在激活的淋巴细胞和淋巴母细胞的细胞核中,还检测到110 kDa的钙调蛋白结合蛋白减少,以及另外三种240、180和170 kDa的蛋白增加。

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