Characterization of matrix metalloproteinase expressed by human embryonic kidney cells

Characterization of matrix metalloproteinase expressed by human embryonic kidney cells
复制标题

人胚胎肾细胞表达的基质金属蛋白酶的表征

DOI:
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发表时间:
2006
影响因子:
2.7
通讯作者:
Pel
Pel
中科院分区:
工程技术4区
文献类型:
--
作者:
Chi;Pel

文献摘要

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人胚肾(HEK)细胞表达的蛋白酶常用于重组蛋白的表达和腺病毒载体的制备,但关于HEK细胞表达的蛋白酶的信息很少。采用酶谱分析、mRNA分析、蛋白质印迹和蛋白质芯片等方法研究HEK细胞系中蛋白酶的表达谱。主要蛋白酶为明胶酶A [或基质金属蛋白酶(MMP)-2]。此外,HEK细胞还表达其他MMP,如MMP-1、MMP-2、MMP-3、MMP-8、MMP-9、MMP-10、MMP-13和膜型(MT)1-和3-MMP,以及金属蛋白酶组织抑制剂(TIMP)-1、TIMP-2和TIMP-3。HEK细胞表达MMP和TIMP谱的表征为重组蛋白和腺病毒载体在培养和纯化过程中的降解控制提供了基础。
There is little information available on the proteases expressed by human embryonic kidney (HEK) cells, which are often used for expression of recombinant proteins and production of adenovirus vector. The expression profile of proteases in HEK cell line was investigated using zymography, mRNA analysis, western blotting and protein array. The major protease was gelatinase A [or matrix metalloproteinase (MMP)-2]. Beside, other MMPs, such as MMP-1, -2, -3, -8, -9, -10, -13 and membrane type (MT) 1- and 3−MMP, as well as tissue inhibitors of metalloproteinase (TIMP)-1, -2 and -3, were also expressed by HEK cells. Characterization of MMP and TIMP profiles expressed by HEK cells provides the basis for degradation control of recombinant protein and adenovirus vector during culture and purification processes.