Search Results
You are looking at 1 - 8 of 8 items for
- Author: S Kato x
- Refine by access: All content x
Search for other papers by M. Kato in
Google Scholar
PubMed
Search for other papers by M. Hagiwara in
Google Scholar
PubMed
Search for other papers by Y. Nimura in
Google Scholar
PubMed
Search for other papers by S. Shionoya in
Google Scholar
PubMed
Search for other papers by H. Hidaka in
Google Scholar
PubMed
ABSTRACT
Calmodulin has been identified in parathyroid cells and is thought to play an important role in the production or secretion of parathyroid hormone. However, a detailed investigation of calmodulinbinding proteins in parathyroid glands has not been conducted. In this study, we attempted to determine the presence of calmodulin-binding protein in human parathyroid adenoma by affinity chromatography. The eluted protein from a calmodulin-coupled Sepharose 4B column with EGTA was analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis which revealed a major protein band of M r 50 000. A Ca2+/calmodulin-dependent protein kinase activity was detected at the protein peak using dephosphorylated casein as a substrate. The 50 kDa band was identified as calcium/calmodulin-dependent protein kinase II (CaM-kinase II) by immunoblotting. The substrate specificity, pH dependency and affinity for calmodulin of this enzyme were identical to those of CaM-kinase II from rat brain. Also, the kinase activity was sensitive to KN-62, a specific inhibitor of CaM-kinase II. In total, 0·48 mg of this kinase was purified from 3 g human parathyroid adenoma.
Journal of Endocrinology (1991) 131, 155–162
Search for other papers by Y Ninomiya in
Google Scholar
PubMed
Search for other papers by Y Arao in
Google Scholar
PubMed
Search for other papers by T Kometani in
Google Scholar
PubMed
Search for other papers by S Hiwatashi in
Google Scholar
PubMed
Search for other papers by T Yamasaki in
Google Scholar
PubMed
Search for other papers by T Erikawa in
Google Scholar
PubMed
Search for other papers by H Yamaguchi in
Google Scholar
PubMed
Search for other papers by T Hasegawa in
Google Scholar
PubMed
Search for other papers by S Masushige in
Google Scholar
PubMed
Search for other papers by S Kato in
Google Scholar
PubMed
Abstract
We examined vitamin A-deficient chicks to determine whether vitamin A affects the estrogen-induced development of the chick oviduct. When oviduct development was stimulated for 5 days with the synthetic estrogen, diethylstilbestrol, the wet weight of the oviduct in vitamin A-deficient chicks was only half that in control chicks. The DNA content in this tissue showed that the decreased oviduct weight in the vitamin A-deficient chicks was caused by the decreased proliferation of oviduct cells. However, the estrogen-induced expression of the ovalbumin gene was not affected by the vitamin A deficiency, suggesting that estrogen-induced cytodifferentiation is not affected by vitamin A. To clarify the vitamin A action on estrogen-induced development in the oviduct, transcripts of nuclear estrogen receptor (ER) and all-trans-retinoic acid (RARα, β and γ) receptors, which exert the effects of estrogen and vitamin A, were measured. The ER, RARα and RARβ genes, but not that of RARγ, were expressed during oviduct development, indicating that estrogen and vitamin A may control the expression of target genes through their cognate receptors. Thus, we have shown that vitamin A is involved in estrogen-induced cell proliferation but not in cytodifferentiation of the chicken oviduct.
Journal of Endocrinology (1996) 148, 257–265
Search for other papers by T Takahashi in
Google Scholar
PubMed
Search for other papers by K Sato in
Google Scholar
PubMed
Search for other papers by S Kato in
Google Scholar
PubMed
Search for other papers by T Yonezawa in
Google Scholar
PubMed
Search for other papers by Y Kobayashi in
Google Scholar
PubMed
Search for other papers by Y Ohtani in
Google Scholar
PubMed
Search for other papers by S Ohwada in
Google Scholar
PubMed
Search for other papers by H Aso in
Google Scholar
PubMed
Search for other papers by T Yamaguchi in
Google Scholar
PubMed
Search for other papers by S G Roh in
Google Scholar
PubMed
Search for other papers by K Katoh in
Google Scholar
PubMed
Ghrelin is a multifunctional peptide that promotes an increase of food intake and stimulates GH secretion. Ghrelin secretion is regulated by nutritional status and nutrients. Although a high-protein (HP) diet increases plasma ghrelin secretion in mammals, the mechanisms and the roles of the elevated ghrelin concentrations due to a HP diet have not been fully established. To clarify the roles of elevated acylated ghrelin upon intake of a HP diet, we investigated the regulation of ghrelin concentrations in plasma and tissues in wethers fed with either the HP diet or the control (CNT) diet for 14 days, and examined the action of the elevated plasma ghrelin by using a ghrelin-receptor antagonist. The HP diet gradually increased the plasma acylated-ghrelin concentrations, but the CNT diet did not. Although the GH concentrations did not vary significantly across the groups, an injection of ghrelin-receptor antagonist enhanced insulin levels in circulation in the HP diet group. In the fundus region of the stomach, the ghrelin levels did not differ between the HP and CNT diet groups, whereas ghrelin O-acyltransferase mRNA levels were higher in the group fed with HP diet than those of the CNT diet group were. These results indicate that the HP diet elevated the plasma ghrelin levels by increasing its synthesis; this elevation strongly suppresses the appearance of insulin in the circulation of wethers, but it is not involved in GH secretion. Overall, our findings indicate a role of endogenous ghrelin action in secretion of insulin, which acts as a regulator after the consumption of a HP diet.
Search for other papers by A. Nagasaka in
Google Scholar
PubMed
Search for other papers by S. Yoshida in
Google Scholar
PubMed
Search for other papers by A. Nakai in
Google Scholar
PubMed
Search for other papers by T. Ohyama in
Google Scholar
PubMed
Search for other papers by K. Iwase in
Google Scholar
PubMed
Search for other papers by S. Ohtani in
Google Scholar
PubMed
Search for other papers by H. Nakagawa in
Google Scholar
PubMed
Search for other papers by R. Masunaga in
Google Scholar
PubMed
Search for other papers by S. Kato in
Google Scholar
PubMed
Search for other papers by T. Kawabe in
Google Scholar
PubMed
Search for other papers by K. Kataoka in
Google Scholar
PubMed
ABSTRACT
Using hypophysectomized rats, it has been shown that DNA polymerase-β activity in the adrenal gland and testis is largely influenced by pituitary trophic hormones. Sucrose gradient centrifugation of thyroid extracts revealed three peaks of DNA polymerase-β activity sedimenting at 3·3S, 7·3S and 12S. Of these, hypophysectomy induced a decrease in the 3·3S DNA polymerase-β, whereas other molecular forms were affected only slightly. DNA polymerase-α and -γ activities were unaffected by hypophysectomy. These changes in DNA polymerase-β caused by hypophysectomy were reversed by daily i.p. injection of TSH. Furthermore, stimulation of the thyroid by excess TSH induced by the administration of 1-methyl-2-mercaptoimidazole resulted in an increase of all forms of thyroid DNA polymerase-β.
These results show that the level of DNA polymerase is relatively constant after hypophysectomy but that DNA polymerase-β in the rat thyroid gland is also modulated by TSH mainly through the change of activity of the polymerase-β which sediments at 3·3S.
J. Endocr. (1988) 119, 303–308
Search for other papers by A. Nakano in
Google Scholar
PubMed
Search for other papers by M. Terasawa in
Google Scholar
PubMed
Search for other papers by M. Watanabe in
Google Scholar
PubMed
Search for other papers by K. Okazaki in
Google Scholar
PubMed
Search for other papers by S. Inoue in
Google Scholar
PubMed
Search for other papers by M. Kato in
Google Scholar
PubMed
Search for other papers by Y. Nimura in
Google Scholar
PubMed
Search for other papers by N. Usuda in
Google Scholar
PubMed
Search for other papers by T. Morita in
Google Scholar
PubMed
Search for other papers by H. Hidaka in
Google Scholar
PubMed
ABSTRACT
Neurocalcin (molecular weight 23 000 and 24 000) is a Ca2+-binding protein with three putative Ca2+-binding domains and is present in large amounts in nervous tissues. Neurocalcin isoproteins separated by C18 reverse-phase column chromatography are insoluble in buffer solution and it is impossible to determine the dissociation constant of neurocalcin with Ca2+. To overcome this difficulty, recombinant neurocalcin was synthesized, based on one of the cDNAs of the neurocalcin isoproteins. Stoichiometric titration experiments, using recombinant neurocalcin, indicated that this protein bound 2 mol Ca2+/mol protein and that the apparent dissociation constant for Ca2+ was 2·2 μmol/l, suggesting that neurocalcin plays a physiological role in cellular function. Immunoblotting showed that neurocalcin is present in the bovine adrenal gland in addition to the nervous tissues. Neurocalcin, identified by immunoblotting, was purified from the bovine adrenal gland. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) of neurocalcin from the bovine brain showed 23 kDa and 24 kDa double bands, while SDS-PAGE of neurocalcin from the adrenal gland showed a single band of apparently 24 kDa, suggesting that the expression of neurocalcin isoproteins differs from tissue to tissue. The content of neurocalcin in the adrenal gland was 10 μg protein/100 g wet tissue. Immunohistochemical analysis showed the occurrence of neurocalcin in zona glomerulosa and adrenal medulla but not in zona fasciculata or zona reticularis. The restricted localization of neurocalcin in the adrenal gland suggests that a similar Ca2+ signal pathway may be present in zona glomerulosa and the adrenal medulla.
Journal of Endocrinology (1993) 138, 283–290
Search for other papers by Y Itoh in
Google Scholar
PubMed
Search for other papers by S Imamura in
Google Scholar
PubMed
Search for other papers by K Yamamoto in
Google Scholar
PubMed
Search for other papers by Y Ono in
Google Scholar
PubMed
Search for other papers by M Nagata in
Google Scholar
PubMed
Search for other papers by T Kobayashi in
Google Scholar
PubMed
Search for other papers by T Kato in
Google Scholar
PubMed
Search for other papers by M Tomita in
Google Scholar
PubMed
Search for other papers by A Nakai in
Google Scholar
PubMed
Search for other papers by M Itoh in
Google Scholar
PubMed
Search for other papers by A Nagasaka in
Google Scholar
PubMed
Endothelin-1 (ET-1) concentrations are increased in patients with diabetes mellitus, particularly those with diabetic retinopathy, or essential hypertension. We hypothesized that ET-1 might participate in the development and progression of diabetic microangiopathy. In this study, the effects of the angiotensin converting enzyme (ACE) inhibitor, enalapril maleate, on diabetic angiopathy were examined in streptozotocin (STZ)-induced diabetic (STZ-DM) rats by monitoring variations in renal function and ET-1 concentrations in blood and organ tissues. Significant increases in kidney weight and in concentrations of urinary albumin, N-acetyl-fl-d-glucosamidase (NAG) and serum ET-1 were observed in the STZ-DM rats as compared with the non-diabetic rats, and the concentration of ET-1 in the kidneys tended to be increased. Microscopic and electron microscopic analyses showed increased mesangial cell proliferation, matrix expansion and enlarged mesangial area in the kidney of the diabetic rats. After administration of the ACE inhibitor, increased concentrations of urinary albumin and NAG in the STZ-DM rats were reduced to the control values with a slight improvement in the electron microscopic changes. These data suggest that ET-1 may be involved in the development and progression of diabetic nephropathy and may explain, in part, why diabetes is liable to complicate hypertension. ACE inhibitor may help to restore diabetic nephropathy in the STZ-induced diabetic rats.
Search for other papers by M Makino in
Google Scholar
PubMed
Search for other papers by N Oda in
Google Scholar
PubMed
Search for other papers by N Miura in
Google Scholar
PubMed
Search for other papers by S Imamura in
Google Scholar
PubMed
Search for other papers by K Yamamoto in
Google Scholar
PubMed
Search for other papers by T Kato in
Google Scholar
PubMed
Search for other papers by K Fujiwara in
Google Scholar
PubMed
Search for other papers by Y Sawai in
Google Scholar
PubMed
Search for other papers by K Iwase in
Google Scholar
PubMed
Search for other papers by A Nagasaka in
Google Scholar
PubMed
Search for other papers by M Itoh in
Google Scholar
PubMed
Thyroid hormones affect reactions in almost all pathways of lipid metabolism. It has been reported that plasma free fatty acid (FFA) concentration in hypothyroidism is generally within the normal range. In this study, however, we show that plasma FFA concentration in some hypothyroid patients is higher than the normal range. Symptoms of thyroid dysfunction in these individuals were less severe than those of patients with lower plasma FFA concentrations. From these findings we hypothesized that the change in FFA concentration must correlate with thyroid function. Using an animal model, we then examined the effect of highly purified eicosapentaenoic acid ethyl ester (EPA-E), a n-3 polyunsaturated fatty acid derived from fish oil, on thyroid function in 1-methyl-2-imidazolethiol (MMI)-induced hypothyroid rats. Oral administration of EPA-E inhibited reduction of thyroid hormone levels and the change of thyroid follicles in MMI-induced hypothyroid rats. These findings suggest that FFA may affect thyroid functions and EPA-E may prevent MMI-induced hypothyroidism.
Search for other papers by RA Medina in
Google Scholar
PubMed
Search for other papers by AM Meneses in
Google Scholar
PubMed
Search for other papers by JC Vera in
Google Scholar
PubMed
Search for other papers by C Guzman in
Google Scholar
PubMed
Search for other papers by F Nualart in
Google Scholar
PubMed
Search for other papers by F Rodriguez in
Google Scholar
PubMed
Search for other papers by M de los Angeles Garcia in
Google Scholar
PubMed
Search for other papers by S Kato in
Google Scholar
PubMed
Search for other papers by N Espinoza in
Google Scholar
PubMed
Search for other papers by C Monso in
Google Scholar
PubMed
Search for other papers by A Carvajal in
Google Scholar
PubMed
Search for other papers by M Pinto in
Google Scholar
PubMed
Search for other papers by GI Owen in
Google Scholar
PubMed
Estrogen replacement therapy and other unopposed estrogen treatments increase the incidence of endometrial abnormalities, including cancer. However, this effect is counteracted by the co-administration of progesterone. In the endometrium, glucose transporter (GLUT) expression and glucose transport are known to fluctuate throughout the menstrual cycle. Here, we determined the effect of estrogen and progesterone on the expression of GLUT1-4 and on the transport of deoxyglucose in Ishikawa endometrial cancer cells. Cells were incubated with estrogen, progesterone or combined estrogen and progesterone for 24 h and the effect on the expression of GLUT1-4 and on deoxyglucose transport was determined. We show that GLUT1 expression is upregulated by estrogen and progesterone individually, but that combined estrogen and progesterone treatment reverses this increase. Hormonal treatments do not affect GLUT2, GLUT3 or GLUT4 expression. Transport studies demonstrate that estrogen increases deoxyglucose transport at Michaelis-Menten constants (Kms) corresponding to GLUT1/4, an effect which disappears when progesterone is added concomitantly. These data demonstrate that different hormonal treatments differentially regulate GLUT expression and glucose transport in this endometrial cancer cell line. This regulation mirrors the role played by estrogen and progesterone on the incidence of cancer in this tissue and suggests that GLUT1 may be utilized by endometrial cancer cells to fuel their demand for increased energy requirement.
