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Related Experiment Videos

Plasminogen activator in bladder tumors.

S Mitsubayashi1, T Akiyama, T Kurita

  • 1Department of Urology, Kinki University, School of Medicine, Sayama, Japan.

Urological Research
|January 1, 1987
PubMed
Summary

Researchers isolated a novel plasminogen activator from bladder tumors. This enzyme, distinct from urokinase (UK) and tissue-type plasminogen activator (t-PA), shows unique substrate specificity and inhibition patterns.

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Area of Science:

  • Biochemistry
  • Oncology
  • Enzymology

Background:

  • Plasminogen activators (PAs) play crucial roles in physiological processes, including tissue remodeling and cancer progression.
  • Aberrant expression of PAs is frequently observed in various human malignancies, including bladder cancer.

Purpose of the Study:

  • To isolate and characterize the plasminogen activator present in human bladder tumors.
  • To determine if the bladder tumor-associated PA is related to known urokinase (UK) or tissue-type plasminogen activator (t-PA).

Main Methods:

  • Purification of plasminogen activator using ammonium sulfate precipitation, acid treatment, and concanavalin A-Sepharose affinity chromatography.
  • Enzymatic activity assays using chromogenic substrates S-2288 and S-2444.
  • Characterization of the purified enzyme's molecular weight, cofactor dependency, and inhibition profile.

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  • Immunological characterization using antibodies against UK and t-PA.

    • Main Results:

    • A plasminogen activator was purified from bladder tumors with an 80,000-fold increase in specific activity.
    • The purified enzyme exhibited a molecular weight of 55,000 and required plasminogen for activity.
    • The enzyme was inactivated by DFP and inhibited by basic pancreatic trypsin inhibitor and benzamidine.
    • Immunological assays indicated the purified PA did not react with antibodies against t-PA but showed cross-reactivity with UK antibodies.
    • Substrate specificity analysis revealed preferential cleavage of S-2288 over S-2444, differing from the typical substrate preference of UK.

    Conclusions:

    • The study successfully isolated and characterized a unique plasminogen activator from bladder tumors.
    • The enzyme's distinct properties, including substrate specificity and immunological reactivity, suggest it may represent a novel category of plasminogen activator.
    • Further investigation is warranted to elucidate the precise identity and functional significance of this bladder tumor-associated plasminogen activator.