Uptake and transport activity of the median eminence of the hypothalamus.
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Biomedical subjects
Publications and source records attributed to K M Knigge.
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Using an immunohistochemical technique at the electron microscopic level, we have observed that within the axon terminals of the guinea pig neurohypophysis neurophysin is present in the large neurosecretory granules, as well as in the axoplasm. A description of a freeze-substitution technique for neural lobe is also present.
The effect of hypothalamic deafferentation upon levels of LH-RH in brain, cerebrospinal fluid, and plasma was studied in adult male rats. Deafferentation produced a significant increase in the LH-RH concentration of third ventricular CSF (from 140.6 to 343.9 pg/microl), while there was no change in median eminence or hypothalamic content. LH-RH in the pineal gland and the posterior pituitary was also elevated by hypothalamic isolation.
The reaction products of plasma enzyme degradation of TRH were identified by thin layer chromatography. The enzyme in normal rat plasma yields proline and pGlu-His as major reaction products. High concentrations of proline decrease peptide cleavage, resulting in greater amounts of acid TRH. The apparent Km of the enzyme is 4.1 X 10(-6) M. LHRH and neurotensin are competitive inhibitors with Ki of 5 X 10(-6) M and 1.5 X 10(-5) M, respectively. Somatostatin, MIF, oxytocin, arg-vasopressin, arg-vasotocin, neurophysin II and glucagon do not compete; and pGlu-His-Pro-OH, Glu-His-Pro-OH, pGlu-His, His-Pro-NH2, and Pro-NH2 do not affect enzyme activity. These data suggest that the substrated requires pGlu and a terminal or internal amide to complex with the enzyme. The enzyme is markedly inhibited by Cu++, Bal, benzamadine, p-(chloromercuri)-benzoic acid, moderately affected by EDTA and puromycin, and unaffected by mercaptoethanol. TSH does not affect enzyme activity while LH inhibits it moderately at high concentrations (300-600 pg/ml).
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