—

Print
Save
Email this link

Share Link

Copy this link, or click below to email it to a friend
Email this link
or copy the link directly:

https://joe.bioscientifica.com/search?f_0=author&q_0=M.+Hashimoto
The link was not copied. Your current browser may not support copying via this button.

Link copied successfully

Search Results

You are looking at 1 - 7 of 7 items for

Author: M. Hashimoto x

Refine by access: All content x

Clear All Modify Search

Bombesin and bradykinin increase inositol phosphates and cytosolic free Ca²⁺, and stimulate DNA synthesis in human endometrial stromal cells

T. Endo

T. Endo
Search for other papers by T. Endo in
Google Scholar
PubMed

H. Fukue

H. Fukue
Search for other papers by H. Fukue in
Google Scholar
PubMed

M. Kanaya

M. Kanaya
Search for other papers by M. Kanaya in
Google Scholar
PubMed

M. Mizunuma

M. Mizunuma
Search for other papers by M. Mizunuma in
Google Scholar
PubMed

M. Fujii

M. Fujii
Search for other papers by M. Fujii in
Google Scholar
PubMed

H. Yamamoto

H. Yamamoto
Search for other papers by H. Yamamoto in
Google Scholar
PubMed

S. Tanaka

S. Tanaka
Search for other papers by S. Tanaka in
Google Scholar
PubMed

, and

M. Hashimoto

M. Hashimoto
Search for other papers by M. Hashimoto in
Google Scholar
PubMed

ABSTRACT

The present studies were carried out to investigate the effect of several growth factors on human endometrial stromal cells.

In human endometrial stromal cells, bombesin and bradykinin provoked an increase in intracellular free Ca²⁺ and in labelled inositol phosphates when pre-incubated with [³H]myoinositol. Some or possibly all of the initial increase in intracellular free Ca²⁺ represented a mobilization of Ca²⁺ from intracellular stores and the second phase of the response depended on Ca²⁺ influx from the extracellular medium.

[³H]Thymidine was added to human cultured endometrial stromal cells with bombesin, bradykinin, epidermal growth factor (EGF), prostaglandin F_2α, vasopressin and platelet-derived growth factor. Bombesin, bradykinin and EGF stimulated the incorporation of [³H]thymidine into DNA in quiescent cells.

In conclusion, bombesin and bradykinin are growth factors which activate phospholipase C in human endometrial stromal cells, while EGF stimulates DNA synthesis without the activation of phospholipase C.

Journal of Endocrinology (1991) 131, 313–318

Article Type:: Research Article

DOI:: https://doi.org/10.1677/joe.0.1310313

Volume/Issue:: Volume 131: Issue 2

Restricted access

Prostaglandin F_2α- and phorbol 12-myristate-13-acetate-stimulated progesterone production by cultured human luteal cells in the mid-luteal phase: prostaglandin F_2α increases cytosolic Ca²⁺ and inositol phosphates

T. Endo

T. Endo
Search for other papers by T. Endo in
Google Scholar
PubMed

H. Watanabe

H. Watanabe
Search for other papers by H. Watanabe in
Google Scholar
PubMed

H. Yamamoto

H. Yamamoto
Search for other papers by H. Yamamoto in
Google Scholar
PubMed

S. Tanaka

S. Tanaka
Search for other papers by S. Tanaka in
Google Scholar
PubMed

, and

M. Hashimoto

M. Hashimoto
Search for other papers by M. Hashimoto in
Google Scholar
PubMed

ABSTRACT

While prostaglandin F_2α (PGF_2α) has been thought to be a natural luteolysin in non-primates, a luteolytic effect in the human corpus luteum is less evident. We therefore investigated the action of PGF_2α on monolayer cultures of human luteal cells obtained from mid-luteal phase corpora lutea.

PGF_2α increased basal and human chorionic gonadotrophin (hCG)-stimulated progesterone production by human cultured luteal cells. A potent tumour-promoting phorbol ester, phorbol 12-myristate-13-acetate (PMA), also stimulated progesterone production by cultured human luteal cells.

Although human luteal cells were incubated for 24 h with PMA, hCG was still able to stimulate the production of progesterone by PMA-pretreated cells. However, PMA pretreatment blocked the ability of PGF_2α to stimulate progesterone production. It is possible that the luteotrophic effect of PGF_2α may be mediated, in part, by the activation of protein kinase C.

Addition of PGF_2α to suspensions of human luteal cells preincubated with myo-[2-³H]inositol promoted an increase in labelled inositol phosphates. PGF_2α also rapidly increased intracellular free Ca²⁺ in human luteal cells loaded with the fluorescent Ca²⁺ probe, fura-2.

We conclude that PGF_2α and PMA stimulate progesterone production and that PGF_2α increases the intracellular free calcium and inositol phosphates of human cultured luteal cells in the mid-luteal phase.

Journal of Endocrinology (1992) 133, 451–458

Article Type:: Research Article

DOI:: https://doi.org/10.1677/joe.0.1330451

Volume/Issue:: Volume 133: Issue 3

Restricted access

Effects of hyperprolactinaemia on reproduction in male mice

M. Nonomura

M. Nonomura
Search for other papers by M. Nonomura in
Google Scholar
PubMed

K. Hoshino

K. Hoshino
Search for other papers by K. Hoshino in
Google Scholar
PubMed

T. Harigaya

T. Harigaya
Search for other papers by T. Harigaya in
Google Scholar
PubMed

H. Hashimoto

H. Hashimoto
Search for other papers by H. Hashimoto in
Google Scholar
PubMed

, and

O. Yoshida

O. Yoshida
Search for other papers by O. Yoshida in
Google Scholar
PubMed

ABSTRACT

Hyperprolactinaemia induced by pituitary isografts in male host mice was confirmed by radioimmunoassay, but plasma testosterone levels determined by radioimmunoassay in these mice showed no changes. Immunoenzyme electron microscopic observations revealed large spherical-shaped immunoreactive prolactin granules in pituitary grafts in male hosts, regardless of the sex of the donor mice, indicating the disappearance of sexual dimorphism in prolactin-producing cells in hyperprolactinaemic mice. In hyperprolactinaemic host mice the male accessory sex glands, particularly the seminal vesicle and the ventral prostate, exhibited considerable proliferation and significant increase in weight. These phenomena do not seem to be mediated by the increased action of testosterone. Such biological effects in host mice were much greater when the donor was female rather than male, and were more noticeable in C57BL mice than in C3H mice.

J. Endocr. (1985) 107, 71–76

Article Type:: Research Article

DOI:: https://doi.org/10.1677/joe.0.1070071

Volume/Issue:: Volume 107: Issue 1

Restricted access

Suppressive effects of dehydroepiandrosterone and the nuclear factor-κB inhibitor parthenolide on corticotroph tumor cell growth and function in vitro and in vivo

T Taguchi

T Taguchi Department of Endocrinology, Metabolism and Nephrology, Kochi Medical School, Kochi University, Oko-cho, Kohasu, Nankoku 783-8505, Japan

Search for other papers by T Taguchi in
Google Scholar
PubMed

T Takao

T Takao Department of Endocrinology, Metabolism and Nephrology, Kochi Medical School, Kochi University, Oko-cho, Kohasu, Nankoku 783-8505, Japan

Search for other papers by T Takao in
Google Scholar
PubMed

Y Iwasaki

Y Iwasaki Department of Endocrinology, Metabolism and Nephrology, Kochi Medical School, Kochi University, Oko-cho, Kohasu, Nankoku 783-8505, Japan

Search for other papers by Y Iwasaki in
Google Scholar
PubMed

M Nishiyama

M Nishiyama Department of Endocrinology, Metabolism and Nephrology, Kochi Medical School, Kochi University, Oko-cho, Kohasu, Nankoku 783-8505, Japan

Search for other papers by M Nishiyama in
Google Scholar
PubMed

K Asaba

K Asaba Department of Endocrinology, Metabolism and Nephrology, Kochi Medical School, Kochi University, Oko-cho, Kohasu, Nankoku 783-8505, Japan

Search for other papers by K Asaba in
Google Scholar
PubMed

, and

K Hashimoto

K Hashimoto Department of Endocrinology, Metabolism and Nephrology, Kochi Medical School, Kochi University, Oko-cho, Kohasu, Nankoku 783-8505, Japan

Search for other papers by K Hashimoto in
Google Scholar
PubMed

Dehydroepiandrosterone (DHEA) is believed to have an anti-tumor effect, as well as anti-inflammatory, antioxidant, and anti-aging effects. To clarify the possible inhibitory action of DHEA on pituitary tumor cells, we tested the effects of DHEA, alone or in combination with the nuclear factor-κB (NF-κB) inhibitor parthenolide (PRT), on AtT20 corticotroph cell growth and function both in vitro and in vivo. We found that, in vitro, DHEA and PRT had potent inhibitory effects on pro-opiomelanocortin and NF-κB-dependent gene expression. They also suppressed the transcription activity of survivin, a representative anti-apoptotic factor, and induced apoptosis in this cell line. Furthermore, using BALB/C nude mice with xenografts of AtT20 cells in vivo, we found that the combined administration of DHEA and PRT significantly attenuated tumor growth and survivin expression. The treatment also decreased the elevated plasma corticosterone levels and ameliorated the malnutrition induced by tumor growth. Altogether, these results suggested that combined treatments of DHEA and PRT potently inhibit the growth and function of corticotroph tumor cells both in vitro and in vivo. This effect may, at least partly, be caused by the suppressive effects of these compounds, such as survivin and other inhibitor of apoptosis proteins, on NF-κB-mediated gene transcription.

Article Type:: Research Article

DOI:: https://doi.org/10.1677/joe.1.06418

Volume/Issue:: Volume 188: Issue 2

Free access

Enzyme-linked immunosorbent assay for human insulin-like growth factor-I using monoclonal and polyclonal antibodies with defined epitope recognition

K. Tamura

K. Tamura
Search for other papers by K. Tamura in
Google Scholar
PubMed

M. Kobayashi

M. Kobayashi
Search for other papers by M. Kobayashi in
Google Scholar
PubMed

S. Suzuki

S. Suzuki
Search for other papers by S. Suzuki in
Google Scholar
PubMed

Y. Ishii

Y. Ishii
Search for other papers by Y. Ishii in
Google Scholar
PubMed

S. Koyama

S. Koyama
Search for other papers by S. Koyama in
Google Scholar
PubMed

H. Yamada

H. Yamada
Search for other papers by H. Yamada in
Google Scholar
PubMed

K. Hashimoto

K. Hashimoto
Search for other papers by K. Hashimoto in
Google Scholar
PubMed

M. Niwa

M. Niwa
Search for other papers by M. Niwa in
Google Scholar
PubMed

, and

F. Shibayama

F. Shibayama
Search for other papers by F. Shibayama in
Google Scholar
PubMed

ABSTRACT

Monoclonal antibodies (McAb) and polyclonal antibodies (PcAb) against human insulin-like growth factor-I (somatomedin C; hIGF-I) were produced. Using these two antibodies, an enzyme-linked immunosorbent assay (ELISA) system for hIGF-I was established. The ELISA system was able to detect hIGF-I at a range of 1–25 μg/l, compared with the range of 1–50 μg/l detected by radioimmunoassay (RIA). Human IGF-II and human insulin could not be recognized in this system. The plasma concentrations of IGF-I found using the ELISA agreed well with those found using RIA after conventional Sep-Pak C₁₈ cartridge pretreatment. Epitopes of hIGF-I to McAb and PcAb were investigated by enzymatic digestion of hIGF-I followed by comparing the affinity of the antibodies to the peptides obtained proteolytically. The epitope to McAb was found to be a peptide containing Leu¹⁰-Val¹¹-Asp¹² (epitope 2). Five epitopes to PcAb containing the following key fragments were identified: a conformational structure formed by the disulphide bonds between Cys⁶ and Cys⁴⁸, and between Cys⁴⁷ and Cys⁵² (epitope 1), Leu¹⁰-Val¹¹-Asp¹² (epitope 2), Val¹⁷-Cys¹⁸-Gly¹⁹-Asp²⁰ (epitope 3), Arg²¹-Gly²²-Phe²³-Tyr²⁴ (epitope 4) and Lys⁶⁸-Ser⁶⁹-Ala⁷⁰ (epitope 5). Of these, the peptide containing epitope 5 showed the highest affinity to PcAb. The results indicated that our ELISA system combined recognition by epitope 2 of McAb and recognition by epitope 5 of PcAb to obtain its good specificity.

Journal of Endocrinology (1990) 125, 327–335

Article Type:: Research Article

DOI:: https://doi.org/10.1677/joe.0.1250327

Volume/Issue:: Volume 125: Issue 2

Restricted access

Central and peripheral cardiovascular actions of adrenomedullin 5, a novel member of the calcitonin gene-related peptide family, in mammals

Y Takei

Y Takei
Search for other papers by Y Takei in
Google Scholar
PubMed

H Hashimoto

H Hashimoto Ocean Research Institute, Department of Physiology, Department of Pharmacology, Peptide Institute Inc., University of Tokyo, Nakano, Tokyo 164-8639, Japan

Search for other papers by H Hashimoto in
Google Scholar
PubMed

K Inoue

K Inoue
Search for other papers by K Inoue in
Google Scholar
PubMed

T Osaki

T Osaki Ocean Research Institute, Department of Physiology, Department of Pharmacology, Peptide Institute Inc., University of Tokyo, Nakano, Tokyo 164-8639, Japan

Search for other papers by T Osaki in
Google Scholar
PubMed

K Yoshizawa-Kumagaye

K Yoshizawa-Kumagaye Ocean Research Institute, Department of Physiology, Department of Pharmacology, Peptide Institute Inc., University of Tokyo, Nakano, Tokyo 164-8639, Japan

Search for other papers by K Yoshizawa-Kumagaye in
Google Scholar
PubMed

M Tsunemi

M Tsunemi Ocean Research Institute, Department of Physiology, Department of Pharmacology, Peptide Institute Inc., University of Tokyo, Nakano, Tokyo 164-8639, Japan

Search for other papers by M Tsunemi in
Google Scholar
PubMed

T X Watanabe

T X Watanabe Ocean Research Institute, Department of Physiology, Department of Pharmacology, Peptide Institute Inc., University of Tokyo, Nakano, Tokyo 164-8639, Japan

Search for other papers by T X Watanabe in
Google Scholar
PubMed

M Ogoshi

M Ogoshi
Search for other papers by M Ogoshi in
Google Scholar
PubMed

N Minamino

N Minamino Ocean Research Institute, Department of Physiology, Department of Pharmacology, Peptide Institute Inc., University of Tokyo, Nakano, Tokyo 164-8639, Japan

Search for other papers by N Minamino in
Google Scholar
PubMed

, and

Y Ueta

Y Ueta Ocean Research Institute, Department of Physiology, Department of Pharmacology, Peptide Institute Inc., University of Tokyo, Nakano, Tokyo 164-8639, Japan

Search for other papers by Y Ueta in
Google Scholar
PubMed

Adrenomedullin 5 (AM5) is a new member of the calcitonin gene-related peptide (CGRP) family identified in teleost fish. Although its presence was suggested in the genome database of mammals, molecular identity and biological function of AM5 have not been examined yet. In this study, we cloned a cDNA encoding AM5 in the pig and examined its cardiovascular and renal effects. Putative mature AM5 was localized in the middle of prohormone and had potential signals for intermolecular ring formation and C-terminal amidation. The AM5 gene was expressed most abundantly in the spleen and thymus. Several AM5 genes were newly identified in the database of mammals, which revealed that the AM5 gene exists in primates, carnivores, and undulates but could not be identified in rodents. In primates, nucleotide deletion occurred in the mature AM5 sequence in anthropoids (human and chimp) during transition from the rhesus monkey. Synthetic mature AM5 injected intravenously into rats induced dose-dependent decreases in arterial pressure at 0.1–1 nmol/kg without apparent changes in heart rate. The decrease was maximal in 1 min and AM5 was approximately half as potent as AM. AM5 did not cause significant changes in urine flow and urine Na⁺ concentration at any dose. In contrast to the peripheral vasodepressor action, AM5 injected into the cerebral ventricle dose-dependently increased arterial pressure and heart rate at 0.1–1 nmol. The increase reached maximum more quickly after AM5 (5 min) than AM (15–20 min). AM5 added to the culture cells expressing calcitonin receptor-like receptor (CLR) or calcitonin receptor (CTR) together with one of the receptor activity-modifying proteins (RAMPs), the combination of which forms major receptors for the CGRP family, did not induce appreciable increases in cAMP production in any combination, although AM increased it at 10⁻ ¹⁰–10⁻ ⁹ M when added to the CLR and RAMP2/3 combination. These data indicate that AM5 seems to act on as yet unknown receptor(s) for AM5, other than CLR/CTR+RAMP, to exert central and peripheral cardiovascular actions in mammals.