Griffiths E C, Hooper K C, Jeffcoate S L, White N
Acta Endocrinol (Copenh). 1975 Jun;79(2):209-16. doi: 10.1530/acta.0.0790209.
Peptidases capable of inactivating thyrotrophin-releasing hormone (TRH) have been demonstrated in the hypothalamus. With the development of a specific radioimmunoassay for TRH, this method was used to further study the enzymes acting on the releasing hormone. Whole hypothalamic homogenates from male and female rats inactivated TRH, with greater peptidase activity being found in the female animals. Separation of the homogenates into particulate (microsomal and mitochondrial) and supernatant (soluble/cytoplasmic) fractions showed approximately the same amounts of enzyme activity in both fractions, while dialysis of the fractions slightly reduced the TRH peptidase activity present, suggesting that a diffusible co-factor might be partially involved in the releasing hormone's degradation. These results confirm the presence of TRH-inactivating peptidases in the rat hypothalamus and suggest that the enzymes may be involved in some way in the mechanisms by which the brain controls thyrotrophin release by the anterior pituitary.
已证实在下丘脑存在能够使促甲状腺激素释放激素(TRH)失活的肽酶。随着TRH特异性放射免疫测定法的发展,该方法被用于进一步研究作用于释放激素的酶。雄性和雌性大鼠的全下丘脑匀浆可使TRH失活,且在雌性动物中发现了更高的肽酶活性。将匀浆分离为颗粒(微粒体和线粒体)和上清液(可溶性/细胞质)部分,结果显示两部分中的酶活性大致相同,而对这些部分进行透析会使存在的TRH肽酶活性略有降低,这表明一种可扩散的辅助因子可能部分参与了释放激素的降解。这些结果证实了大鼠下丘脑中存在TRH失活肽酶,并表明这些酶可能以某种方式参与大脑控制垂体前叶促甲状腺激素释放的机制。