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Dive into the research topics where H Yamashita is active.

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Featured researches published by H Yamashita.


British Journal of Cancer | 1996

Bone morphogenetic protein type IB receptor is progressively expressed in malignant glioma tumours.

N. Yamada; Mitsuyasu Kato; P ten Dijke; H Yamashita; T K Sampath; C H Heldin; Kohei Miyazono; Keiko Funa

The distribution of bone morphogenetic protein (BMP) type I receptors and the activin type I receptor (ActR-I) was investigated in 16 cases of human glioma and five cases of non-tumourous gliosis tissue by immunohistochemical technique. Both BMP type IA (BMPR-IA) and the type IB (BMPR-IB) receptors were detected in human glioma cells. A significant increase in BMPR-IB in tumour cells was observed in malignant glioma compared with both low-grade astrocytomas (n=16, P<0.005) and gliosis (n=13, P<0.001). However, enhancement of BMPR-IA staining was moderate and ActR-I staining was only weakly expressed in the malignant glioma tumours. Osteogenic protein (OP)-1/BMP-7, which is known to bind BMPR-IA, BMPR-IB and ActR-I, was expressed in nervous tissue and was also detected in anaplastic areas of malignant glioma. In contrast to the tissue materials, BMPR-IA was expressed to a stronger degree than BMPR-IB in human glioma cell lines; the growth of these cells was suppressed by OP-1. These results suggest the presence of BMP receptors and a functional role for BMPs in malignant glioma.


Archive | 1997

Regulation of Angiogenesis by TGF- β Superfamily

H Yamashita; Akira Shimizu; Mituyasu Kato; Hideki Nishitoh; Hidenori Ichijo; Kohei Miyazono

The angiogenesis process is regulated by many growth factors and cytokines, including transforming growth factor-beta (TGF-β) (1–3). The TGF-β superfamily, which contains the TGF-β family, the activin family, and the bone morphogenetic protein (BMP) family (4), exerts various effects on vascular cells. The effects of TGF-β differ between in vitro and in vivo (1–3). In this study, to investigate the mechanisms of regulation of angiogenesis by TGF-β superfamily members, angiogenic activity in vivo and the effects on cultured endothelial cells in vitro of TGF-β 1 activin A, and BMP-2 were examined.


Journal of Biological Chemistry | 1994

Identification of type I receptors for osteogenic protein-1 and bone morphogenetic protein-4.

P ten Dijke; H Yamashita; T K Sampath; A. H. Reddi; M Estevez; D L Riddle; Hidenori Ichijo; C H Heldin; Kohei Miyazono


Proceedings of the National Academy of Sciences of the United States of America | 1995

Cloning and characterization of a human type II receptor for bone morphogenetic proteins.

Bradley Rosenzweig; Takeshi Imamura; Toshihide Okadome; G N Cox; H Yamashita; P ten Dijke; C H Heldin; Kohei Miyazono


Journal of Cell Biology | 1995

Osteogenic protein-1 binds to activin type II receptors and induces certain activin-like effects.

H Yamashita; P ten Dijke; Danny Huylebroeck; T K Sampath; Maria Andries; James C. Smith; C H Heldin; Kohei Miyazono


Journal of Biological Chemistry | 1994

Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta.

H Yamashita; P ten Dijke; Petra Franzen; Kohei Miyazono; C H Heldin


Journal of Biological Chemistry | 1994

Endoglin forms a heteromeric complex with the signaling receptors for transforming growth factor-beta.

H Yamashita; Hidenori Ichijo; Susanne Grimsby; Anita Morén; P ten Dijke; Kohei Miyazono


Journal of Biological Chemistry | 1994

Distinct roles of the intracellular domains of transforming growth factor-beta type I and type II receptors in signal transduction.

Toshihide Okadome; H Yamashita; Petra Franzen; A Morén; C H Heldin; Kohei Miyazono


Archive | 1993

Activin receptor-like kinases, proteins having serine threonine kinase domains and their use

Kohei Miyazono; Peter Ten Dijke; Petra Franzen; H Yamashita; Carl-Henrik Heldin


Archive | 1993

Aktivin-rezeptor-ähnliche kinasen, proteine mit serin/threonin kinase domänen und deren anwendungen

Kohei Miyazono; Ten Dijke; Petra Franzen; H Yamashita; Carl-Henrik Heldin

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P ten Dijke

Ludwig Institute for Cancer Research

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Petra Franzen

Ludwig Institute for Cancer Research

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T K Sampath

National Institutes of Health

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Toshihide Okadome

Ludwig Institute for Cancer Research

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