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Ghrelin, a 28 amino acid peptide, has recently been isolated from the rat stomach as an endogenous ligand for the GH secretagogue receptor. The fact that administration of ghrelin, centrally or peripherally, stimulates both food intake and GH secretion suggests that stomach ghrelin has an important role in the growth of rats. We used immunohistochemistry… (More)
Ghrelin, a 28-amino-acid peptide, has recently been isolated from the rat stomach as an endogenous ligand for the GH secretagogue receptor. We have reported previously that central or peripheral administration of ghrelin stimulates food intake, and the secretion of GH and gastric acid in rats. In the present study, we investigated how much endogenous… (More)
Ghrelin, a novel growth-hormone-releasing acylated peptide, was recently isolated from rat and human stomachs. In rat, peripheral or central administration of ghrelin stimulates the secretion of growth hormone (GH) from the pituitary gland. Recent work suggests that ghrelin plays an important role in energy homeostasis, body weight, and food intake. We… (More)
Swine hemagglutinating encephalomyelitis virus (HEV) has been shown to have a capability to propagate via neural circuits to the central nervous system after peripheral inoculation, resulting in acute deadly encephalomyelitis in natural host piglets as well as in experimental younger rodents. This study has systematically examined the assembly and… (More)
Receptors and various molecules in neurons are localized at precise locations to perform their respective functions, especially in synaptic sites. Among synaptic molecules, PDZ domain proteins play major roles in scaffolding and anchoring membrane proteins for efficient synaptic transmission. In the present study, we isolated CIP98, a novel protein (98 kDa)… (More)
The recombinant hormone obtained by noncovalent interaction of the natural NH2-terminal fragment (consisting of 134 amino acid residues) with a synthetic COOH-terminal fragment of 52 amino acids of the reduced-carbamidomethylated human somatotropin molecule is found to exhibit full biological activity of the native hormone as evidenced by the tibia test.… (More)
Growth hormone isolated from human pituitaries has been demonstrated to be a good antigen in the rabbit. With the rabbit antiserum to human somatotropin, it is possible to detect as little as 0.1 microg of the hormone by precipitin test. The antiserum was also capable of neutralizing the growth-promoting activity of human somatotropin.
Cells which contain prolactin were clearly distinguished from those which contain growth hormone in adult monkey pituitary glands by means of histologic and fluorescent antibody techniques. The results indicate that in primates, as well as in other mammals, prolactin is immunochemically distinguishable from growth homone.