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The effects of trypsin, plasmin, chymotrypsin and thrombin on human heart adenylate cyclase activity

G H Cros1, P A Chaptal, J J Serrano

  • 1Laboratoire de Pharmacodynamie, Faculte de Pharmacie, Montpellier, France.

Research Communications in Chemical Pathology and Pharmacology
|August 1, 1987
PubMed

Insights

Proteases like trypsin and plasmin inhibit human heart adenylate cyclase (HHAC) activity. Chymotrypsin shows a complex effect, stimulating then inhibiting HHAC, suggesting proteases regulate cardiac function.

Area of Science:

  • Cardiology
  • Biochemistry
  • Enzymology

Background:

  • Adenylate cyclase is a key enzyme in cardiac function.
  • Protease activity can influence cellular processes.

Purpose of the Study:

  • To investigate the effects of specific proteases on human heart adenylate cyclase (HHAC) activity.
  • To understand the potential role of proteases in regulating cardiac function.

Main Methods:

  • Incubation of human heart tissue with varying concentrations of trypsin, plasmin, chymotrypsin, and thrombin.
  • Measurement of adenylate cyclase activity using established biochemical assays.

Main Results:

  • Trypsin and plasmin demonstrated inhibitory effects on HHAC at higher concentrations.
  • Chymotrypsin exhibited a biphasic response: stimulation at moderate concentrations (0.5-10 µg/ml) and inhibition at higher levels.
  • Maximal stimulation by chymotrypsin reached 67.2 ± 5.4% at 3 µg/ml.
  • Thrombin showed no significant impact on HHAC activity up to 1 mg/ml.

Conclusions:

  • Proteases, particularly trypsin, plasmin, and chymotrypsin, can modulate human heart adenylate cyclase activity.
  • These findings suggest a regulatory role for proteases in cardiac physiology.
  • Further research is warranted to elucidate the precise mechanisms and physiological relevance.

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