Studies on Thiol Protease Inhibitor Isolated from Human Breast Cancer Tissue

YAMANE, Motoi

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Studies on Thiol Protease Inhibitor Isolated from Human Breast Cancer Tissue

https://hiroshima.repo.nii.ac.jp/records/2013128

名前 / ファイル	ライセンス	アクション
HiroshimaJMedSci_36_39.pdf (3.7 MB)

Item type

デフォルトアイテムタイプ_（フル）(1)

公開日

2023-03-18

タイトル

Studies on Thiol Protease Inhibitor Isolated from Human Breast Cancer Tissue

言語

作成者

YAMANE, Motoi

アクセス権

open access

アクセス権URI

http://purl.org/coar/access_right/c_abf2

主題

主題Scheme

Other

主題

Thiol protease inhibitor

主題

主題Scheme

Other

主題

Human breast cancer

主題

主題Scheme

Other

主題

Human breast cancer cell line

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主題Scheme

NDC

主題

490

内容記述

Protease activity is considered to be involved in malignant tumor growth, invasion and metastasis. Although, protease activity is thought to be controlled by protease inhibitors, there are a few reports concerning the relationship between cancer and protease inhibitor derived from cancer tissue. In the present study, thiol protease inhibitors (TPIs) were isolated from human breast cancer tissue, normal mammary gland tissue and the human breast cancer cell line (YMB-1). Their biochemical properties were investigated, giving the following results. 1) TPIs in human breast cancer extracts were significantly higher than in normal mammary gland extracts. 2) TPI was purified from both human breast cancer and human normal mammary gland extracts by papain-Sepharose affinity chromatography and Sephacryl S-200 gel filtration. Two kinds of TPIs (]ow-molecular weight TPI and high-molecular weight TPI) were purified from both tissues. Their molecular weights were 14,000 and 90,000, respectively as determined by gel filtration. 3) Low-molecular weight (LMW-) TPI had higher specific activity than high-molecular weight (HMW-) TPI. In breast cancer tissue extracts, LMW-TPI was dominant. Contrarily, HMW-TPI was dominant in normal gland tissue extracts. 4) Only HMW-TPI reacted with anti-urinary thiol protease inhibitor (UTPI) rabbit IgG by double immunodiffusion and immunoelectrophoresis. 5) LMW-TPI inhibited papain competitively using S-2302 as substrate. Its Km and Ki were 1.3 x 1Q·3M and 6.1 x 10·8M, respectively. 6) LMW-TPI was found to be stable to heat and pH variation. 7) TPIs were also purified from the human breast cancer cell line (YMB-1). Both TPIs which were extracted from cultured cells and released into the medium, were confirmed to be LMW-TPI. Breast cancer cells may have lower ability to produce HMW-TPI than normal mammary gland cells. The difference of antigenicity to anti-UTPI IgG between HMW-TPI and LMW-TPI may be useful for diagnosis in near future.

言語

内容記述

内容記述タイプ

Other

内容記述

This research was funded in part by Grant-in-Aid for Scientific Research, Project 60480518, of the Japanese Ministry of Education. Some sections of this paper were presented at 14th International Cancer Congress August 21-27, 1986-Budapest, Hungary and 45th annual meeting of Japanese Cancer Association October 21-23, 1986-Sapporo.

出版者

Hiroshima University School of Medicine

言語

eng

資源タイプ

資源タイプ識別子

http://purl.org/coar/resource_type/c_6501

資源タイプ

departmental bulletin paper

出版タイプ

VoR

出版タイプResource

http://purl.org/coar/version/c_970fb48d4fbd8a85

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2025-02-23 06:24:21.518914

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Studies on Thiol Protease Inhibitor Isolated from Human Breast Cancer Tissue

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