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If I'm reading this correctly, female platelets have a greater tendency to clot. What explains greater female longevity, all the extra stress that males have to endure?
Thanks for posting that.
Thanks for the ping.
NO THAT IS NOT THE ONLY WAY ASPIRIN WORKS! Aspirin = salicylate
SALICYLATE [salicylate] , any of a group of analgesics , or painkilling drugs, that are derivatives of salicylic acid. The best known is acetylsalicylic acid, or aspirin . Now often made synthetically, they were originally derived from salicin, the active ingredient in willow bark, used for centuries in the treatment of pain and fever. Salicylates also occur naturally in many plants used as foods (e.g., strawberries, almonds, tomatoes). LINK
NOW WE HAVE THIS ARTICLE;
1: Br J Pharmacol. 1982 May;76(1):211-3.
Mechanisms of elevation of rat brain tryptophan concentration by various doses of salicylate.
Badawy AA.
1 The roles of inhibition of liver tryptophan pyrrolase activity and of displacement of tryptophan from its binding sites on serum proteins have been investigated in relation to the increase in rat brain tryptophan concentration after administration of various doses of sodium salicylate. 2 The elevation of brain tryptophan concentration by sodium salicylate (0.5 mg/kg) was caused by inhibition of liver pyrrolase activity, whereas that by doses of the drug of 50 mg/kg and above was achieved mainly by tryptophan displacement. Both tryptophan displacement of pyrrolase inhibition caused the increase in brain tryptophan concentration by sodium salicylate at 10 mg/kg. 3 The smallest dose of salicylate capable of displacing serum-protein-bound tryptophan was 2.5 mg/kg.
PMID: 7082905 [PubMed - indexed for MEDLINE]
So aspirin works in TWO DIFFERENT WAYS NOT MENTIONED IN THE ABOVE ARTICLE BY 1. SLOWING TRYPTOPHAN PYRROLASE (OXYGENASE) ACTIVITY AND 2. DISPLACING BOUND TRYPTOPHAN FROM ALBUMIN MAKING THE TRYPTOPHAN FREE (THE EFFECTIVE FORM).
ANYONE TAKE VALIUM OR XANAX? READ BELOW;
1: Naunyn Schmiedebergs Arch Pharmacol. 1975 May 6;288(1):17-27.
Benzodiazepines: specific competitors for the binding of L-tryptophan to human serum albumin.
Muller WE, Wollert U.
By means of the gel filtration technique, the effect of nine benzodiazepine derivatives on the binding of L-tryptophan to human serum albumin was investigated. Using equimolar tryptophan and benzodiazepine concentrations, all benzodiazepines with binding constants higher than 10(4) (M(-1), displace L-tryptophan from its binding site to a high degree. The mechanism of the displacement was characterized as a competition for a common binding site. Some of the benzodiazepines displace L-tryptophan to a greater extent than salicylic acid. The benzostereospecific binding to human serum albumin. This study shows that there is only one binding site on the human serum albumin molecule, which binds tryptophan and the benzodiazepines in a highly stereospecific manner. Therefore it is concluded that the benzodiazepines and L-tryptophan must have similarities in their molecular structure, so that both can bind to the common binding site in such specific manner. These considerations are discussed in regard to the known influence of benzodiazepine derivatives on the L-tryptophan metabolism in brain. A direct involvement of the reported displacement in the pharmacological actions of the drugs seems not to be relevant because of their small therapeutical plasma levels.
PMID: 1161041 [PubMed - indexed for MEDLINE]LINK
SO VALIUM WORKS LIKE ASPIRIN IN THE DISPLACEMENT OF TRYPTOPHAN TURNING IT INTO THE EFFECTIVE FREE FORM.
TRYPTOPHAN WAS PULLED FROM THE MARKET IN 1989 MAKING IT AN ORPHAN DRUG. REBUTTAL?