Abstract
This chapter discusses pineal indoles, its production, secretion, and actions. The biochemical events involved in the conversion of tryptophan to various pineal indole products have been clarified. After the amino acid is taken up by the pinealocyte from the systemic circulation, which provides a perfuse blood supply to the pineal gland, it is hydroxylated in the 5 position to 5-hydroxytryptophan by the enzyme tryptophan hydroxylase (L-tryptophan, tetrahydropteridine: oxygen oxireductase); this enzyme requires both molecular oxygen and reduced pteridine as cofactors. Blood levels of melatonin have been more difficult to quantitate than has the content of this compound in pineal tissue. The presence of melatonin in the blood and either its reduction after pinealectomy provided the proof that the indole was secreted from the gland and also assured the pineal endocrine status.
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