THE RELEASE OF PROSTAGLANDINS AND THROMBOXANES FROM GUINEA‐PIG LUNG BY SLOW REACTING SUBSTANCE OF ANAPHYLAXIS, AND ITS INHIBITION

Article date: October 1978

By: DINAZ M. ENGINEER, H.R. MORRIS, PRISCILLA J. PIPER, P. SIROIS in Volume 64, Issue 2, pages 211-218

Rabbit aorta contracting substance (RCS; consisting mainly of thromboxane A2) and prostaglandin‐like material were released from guinea‐pig isolated perfused lungs by injection of slow reacting substance of anaphylaxis (SRS‐A).

SRS‐A was resistant to boiling and proteolytic enzymes and was therefore distinguished from rabbit aorta contracting substance releasing factor (RCS‐RF).

The release of RCS and prostaglandin‐like material by SRS‐A was anatagonized by indomethacin (1 μg/ml), betamethasone and dexamethasone (4 to 50 μg/ml).

Imidazole (200 μg/ml) inhibited the formation of thromboxane A2 but not that of prostaglandins.

The activity of SRS‐A on guinea‐pig ileum and its ability to release RCS and prostaglandins were destroyed by incubation with arylsulphatase (0.83 μg to 1 mg/ml) and with lipoxidase (16.5 to 50 μg/ml): SRS‐A lost activity on incubation with bovine serum albumin (9 μg/ml) due to protein binding.

Rabbit aorta contracting substance (RCS; consisting mainly of thromboxane A2) and prostaglandin‐like material were released from guinea‐pig isolated perfused lungs by injection of slow reacting substance of anaphylaxis (SRS‐A).

SRS‐A was resistant to boiling and proteolytic enzymes and was therefore distinguished from rabbit aorta contracting substance releasing factor (RCS‐RF).

The release of RCS and prostaglandin‐like material by SRS‐A was anatagonized by indomethacin (1 μg/ml), betamethasone and dexamethasone (4 to 50 μg/ml).

Imidazole (200 μg/ml) inhibited the formation of thromboxane A2 but not that of prostaglandins.

The activity of SRS‐A on guinea‐pig ileum and its ability to release RCS and prostaglandins were destroyed by incubation with arylsulphatase (0.83 μg to 1 mg/ml) and with lipoxidase (16.5 to 50 μg/ml): SRS‐A lost activity on incubation with bovine serum albumin (9 μg/ml) due to protein binding.

DOI: 10.1111/j.1476-5381.1978.tb17291.x

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