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Related Experiment Videos

Protease activity induced by nicotine in human cells.

X L Wang1, K Kita, S Takahashi

  • 1Department of Oral Surgery, Chiba University School of Medicine, Chuo-ku, Chiba 260-8670, Japan.

International Journal of Molecular Medicine
|October 27, 1999
PubMed
Summary

Nicotine exposure can increase fibrinolytic protease activity in human cells. This study identified serine proteases as the key enzymes induced by nicotine, particularly in APr-1 cells.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Pharmacology

Background:

  • Nicotine exerts diverse biological effects.
  • Proteases play crucial roles in biological processes.
  • Understanding nicotine's impact on protease activity is important.

Purpose of the Study:

  • To investigate if nicotine induces proteolytic protease activity.
  • To identify the specific human cell lines responsive to nicotine-induced protease activity.
  • To characterize the nature of these nicotine-induced proteases.

Main Methods:

  • Assessed plasminogen activator-like fibrinolytic protease activity using 125I-fibrin and plasminogen.
  • Treated 16 human cell lines with and without nicotine.
  • Partially purified induced proteases using HPLC gel filtration (TSKG2000SW).

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  • Utilized protease inhibitors for characterization.
  • Main Results:

    • Nicotine induced significant fibrinolytic protease activity in APr-1 cells, the highest among 16 cell lines tested.
    • Partially purified proteases were obtained via HPLC gel filtration.
    • Protease inhibitor tests revealed the induced proteases are serine proteases.

    Conclusions:

    • Nicotine can induce fibrinolytic protease activity in human cell cultures.
    • APr-1 cells exhibit the highest response to nicotine-induced protease activity.
    • The induced proteases are characterized as serine proteases.