Abstract
ON the basis of its activity as a thyrotropin-releasing factor, the tripeptide pyroGlu-His-Pro-NH2 (TRH) has been isolated from the hypothalamus1,2. Subsequently, the tripeptide was found in extrahypothalamic tissues of vertebrates and invertebrates and its activity as a prolactin-releasing factor and as a neurotropin has been recognised (for review see ref. 3). However, the way in which these different activities are elicited at different sites is still unknown. According to the concept of limited proteolysis4, distinct functions at different sites could emerge if TRH were susceptible to specific enzymatic attack. Degrading enzymes might therefore not only be responsible for the regulation of TRH concentration5–7, which in turn controls both the degree and the duration of the stimulatory effects of the tripeptide, but could also give rise to new activities. We report here the degradation of TRH by enzymes in serum, hypothalamus, pituitary and brain and the identification of the degradation products. We have also studied a presumptive metabolite, histidyl-proline-diketopiperazine, which seems to inhibit prolactin release.
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BAUER, K., KLEINKAUF, H., GRÄF, K. et al. Inhibition of prolactin secretion by histidyl-proline-diketopiperazine. Nature 274, 174–175 (1978). https://doi.org/10.1038/274174a0
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DOI: https://doi.org/10.1038/274174a0
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