Protease activity induced by nicotine in human cells.
Nicotine has a wide range of biological effects, and proteases have been extensively studied for their biological roles in living creatures. The aim of this study is to determine whether nicotine can induce proteolytic protease activity in cultures of various human cell lines. Plasminogen activator-like fibrinolytic protease activity, using 125I-fibrin as substrate in the presence of plasminogen, was estimated in cells with and without nicotine treatment. Among 16 cell lines tested, APr-1 cells were found to have the highest induced protease activity. Partial purification of the proteases was carried out by high performance liquid chromatography gel filtration on TSKG2000SW. Protease inhibitor tests indicated that the proteases induced by nicotine are serine proteases.
Wang
X L
XL
Department of Oral Surgery, Chiba University School of Medicine, Chuo-ku, Chiba 260-8670, Japan.
Kita
K
K
Takahashi
S
S
Hasegawa
R
R
Chi
X J
XJ
Yamamori
H
H
Nakajima
N
N
Yokoe
H
H
Tanzawa
H
H
Suzuki
N
N
D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D004305:Dose-Response Relationship, Drug; D010450:Endopeptidases / Q000187:drug effects* / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D009538:Nicotine / Q000494:pharmacology*; D018722:Nicotinic Agonists / Q000494:pharmacology*; D010960:Plasminogen Activators / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism
D018722:Nicotinic Agonists; D011480:Protease Inhibitors; D009538:Nicotine; D010450:Endopeptidases; D010960:Plasminogen Activators