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N Nishimura

Publications and source records attributed to N Nishimura.

At least 19 recordsLinked to original sources

[Endocrine function before and after treatment in patients with anorexia nervosa (author's transl)].

In order to investigate changes in endocrine function, various tests were performed on eleven patients with anorexia nervosa. In two of them, endocrine function before and after treatment was also studied. The responses of plasma LH and FSH to LH-RH were decreased in the patients as were plasma LH-RH, and LH and FSH responses to the oral administration of clomiphene citrate. In more than half of the cases, plasma TSH showed a delayed response to TRH. The basal levels of plasma GH were elevated, and plasma GH responses to hypoglycemia or 1-arginine were lowered in half of the patients. Plasma GH showed a paradoxical rise after glucose load in three out of six cases. Plasma IRI responses to 1-arginine load were decreased in some cases, but plasma IRG responses to 1-arginine were rather excessive. Plasma IRI after glucose load showed low or delayed responses in most of the cases. After the body weight was increased to normal levels by the treatment, pituitary and pancreatic endocrine functions were normalized. These findings indicate that hypothalamic function is primarily impaired in this disease and causes nutritional disorder followed by the dysfunction of some endocrine organs. Such a possibility could be supported by the improvement of endocrine function after body weight has been recovered.

Adolescent

The control of phosphoprotein phosphatase by the second-site phosphorylation of a substrate. Studies with H2B histone as model substrate.

The phosphorylation of Ser-32, in addition to Ser-36 of H2B histone, stimulated the rate of Pi release from Ser-36 by the small form (Mr 31 000) of pig heart phosphoprotein phosphatase both in the absence and presence of 50 mM magnesium acetate. By phosphorylation at Ser-32, the Km value for Ser-36 phosphate in H2B histone was increased from 0.38 microM to 1.16 microM in the absence of magnesium acetate, but not significantly changed (from 37.4 microM to 26.2 microM) in the presence of magnesium acetate. With the large form (Mr 224000) of the phosphoprotein phosphatase, however, the phosphorylation at Ser-32 suppressed the rate of Pi release from Ser-36 both in the absence and presence of magnesium acetate. The Km value of the large form for Ser-36 phosphatase in H2B histone was nevertheless increased by phosphorylation at Ser-32, from 1.2 microM to 5.3 microM in the presence of magnesium acetate, but not changed (from 0.26 microM to 0.23 microM) in the absence of magnesium acetate.

Animals