S. Fayad

Vasoconstrictor components in the Arabian Gulf catfish (Arius thalassinus, Ruppell) proteinaceous skin secretion.

The Arabian Gulf catfish (Arius thalassinus, Ruppell) produces toxic substances from its skin and from venom glands located near the base of the pectoral fins. Investigation of the pharmacological properties of the skin toxin have previously shown cholinergic vasoconstrictor activity in umbilical arteries. Cholinergic vasoconstriction was confirmed in sheep renal arteries. This activity was partially blocked by atropine, while most of the residual contraction was eliminated by simultaneous addition of indomethacin. Skin toxin treatment of arterial specimens caused a release of prostaglandin (PGE2, TXB2 and 6-keto-PGF1 alpha) into the organ bath. Prostaglandin release was blocked by pretreatment with indomethacin. Heat denaturation of skin toxin caused a loss of only the indomethacin-sensitive muscle contraction activity; most of the residual activity was blocked by atropine.

Lipid composition of the epidermal gel secretion from the arabian gulf catfish (Arius thalassinus ruppell)

Lipids associated with a threat induced epidermal gel secretion from the catfish, Arius thalassinus, have been analyzed. Phospholipids, neutral lipids and glycolipids are all present and each of these subclasses has been analyzed by thin layer and gas chromatography with a general similarity with membrane lipids being noted. The epidermal gel lipids differed from total liver lipids of the catfish. Fatty acid analysis showed the gel lipid to be rich in the unsaturated fatty acids: oleate (omega 7, C18:1), arachidonate (omega 6, C20:4), and docosahexaenoate (omega 3, C22:6). Some prostaglandins were quantitated in lipid extracts from the epidermal gel.

Comparative biochemical and pharmacological properties of epidermal secretions from Ariid catfish of the Arabian Gulf

1. Comparative biochemical and pharmacological studies on epidermal secretions from three species of Ariid catfish were carried out to determine whether they share common properties. 2. Protein compositions are generally similar, but show some differences in size and numbers of proteins. 3. Lipids also differ. However, seasonal and dietary changes in lipid compositions exceed the differences among species. 4. Enzymes in the secretions appear common to each fish species, though some differences are noted in relative activities. 5. Toxicity responses of rabbits to injections with secretions from each of the catfish species indicated that two were lethal, with similar lethal dose levels when injected intravenously. 6. Secretions from all three catfish induced changes in plasma enzyme levels indicative of heart and liver damage, and also induced changes in blood glucose and cholesterol levels.

Purification of a toxic factor from Arabian Gulf catfish epidermal secretions.

The Arabian Gulf catfish, Arius bilineatus (Valenciennes) secretes a proteinaceous epidermal secretion when threatened or injured. A toxic factor has been isolated and purified from the crude extract (crude skin toxin) of these secretions by a combination of gel filtration on Sephacryl S-300 and preparative discontinuous polyacrylamide gel electrophoresis. The purified skin toxin has a molecular weight of 39,000 Da and an isoelectric point (pI) of 5.45. Injection of the purified skin toxin into rabbits i.v. and determination of the LD50 indicated that the protein had been purified approximately 30 fold by these procedures. Injection of the purified skin toxin into rabbits caused agitation, convulsions and death within 5 min. Analysis of plasma levels of lactate dehydrogenase, glutamate-oxaloacetate transaminase and glutamate pyruvate transaminase in injected rabbits indicated that the skin toxin caused cardiac and liver damage to the animals.

Prostanoid synthesis in whole blood cells from fish of the Arabian Gulf

The ability to synthesise prostaglandins and thromboxane from 14C-labelled arachidonic acid was investigated in 11 species of fish from the Arabian Gulf. Cyclooxygenase activity was assessed in washed whole blood cells. Arachidonic acid and its metabolites were extracted and separated on silicic acid columns and thin layer chromatography (silica gel G). Total capacity to convert [14C]arachidonic acid to prostanoids varied from 1 to 35% among the 11 fish species studied. Gray shark (Chiloscyllium griseum) blood cells had the highest capacity (37 +/- 0.4%) to convert arachidonate into prostanoids and two species of catfish (Arius bilineatus and A. thalassinus) exhibited greater than 10% capacity to convert [14C]arachidonate into prostanoids. The major prostanoid synthesised by the two catfish (A. bilineatus and A thalassinus) was 6-keto PGF1 alpha, a stable metabolite of prostacyclin, PGI2. In contrast, A. teunispinis synthesised thromboxane B2, a stable metabolite of thromboxane A2. Thromboxane B2 (TXB2) was the major product synthesised by all three species of shark studied (Chil. griseum, Carcharhinus plumbeus, Carch. melanopterus), with 6-keto PGF1 alpha a minor product. Other fish studied showed a varied pattern of prostanoid synthesis. The synthesis of these prostanoids was almost completely blocked by preincubation of the whole blood cells from catfish and shark with indomethacin (0.5 microM) suggesting the involvement of cyclooxygenase-mediated prostanoid synthesis.

Tyrosine specific esterase activity in the epidermal secretions from the Arabian Gulf catfish, Arius bilineatus (valenciennes)

Abstract 1. 1. The shock-induced epidermal secretions from the Arabian Gulf catfish, Arius bilineatus , contain two classes of esterase activities. 2. 2. One class of esterase activity catalyzes hydrolysis of the general esterase substrate, p -nitrophenyl acetate, and the second is specific of esters for tyrosine. 3. 3. The tyrosine specific esterase has been purified 322-fold and its physical and enzymic properties have been studied. 4. 4. The tyrosine specific esterase is a serine-type esterase with a molecular mass between 70,000 and 100,000 daltons. 5. 5. This enzyme has no measurable amidase activity, though tyrosine amides are effective inhibitors of its esterase activity.