Characterization of matrix metalloproteinase expressed by human embryonic kidney cells.
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.
Liu
Chi-Hsien
CH
Graduate Institute of Biochemical and Biomedical Engineering, Chang Gung University, Taoyuan, Taiwan. chl@mail.cgu.edu.tw
Wu
Pel-Shan
PS
D002478:Cells, Cultured; D004622:Embryo, Mammalian / Q000166:cytology / Q000378:metabolism; D006801:Humans; D007668:Kidney / Q000166:cytology / Q000378:metabolism; D020782:Matrix Metalloproteinases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D040081:Protein Array Analysis; D019714:Tissue Inhibitor of Metalloproteinases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D019714:Tissue Inhibitor of Metalloproteinases; D020782:Matrix Metalloproteinases