| Title: | Cathepsin H indirectly regulates morphogenetic protein-4 (BMP-4) in various human cell lines |
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| Authors: | ID Rojnik, Matija (Author)
ID Jevnikar, Zala (Author)
ID Mirković, Bojana (Author)
ID Janeš, Damjan (Author)
ID Zidar, Nace (Author)
ID Kikelj, Danijel (Author)
ID Kos, Janko (Author) |
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| Files: |  URL - Source URL, visit http://versita.metapress.com/content/p203104l6755v4x4/
 PDF - Presentation file, download (722,81 KB)
MD5: 645C9D7F13AE114496E9897DD30D5B5E
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| Language: | English |
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| Typology: | 1.01 - Original Scientific Article |
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| Organization: |  OI - Institute of Oncology
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| Abstract: | Background. Cathepsin H is a cysteine protease considered to play a major role in tumor progression, however, its precise function in tumorigenesis is unclear. Cathepsin H was recently proposed to be involved in processing of bone morphogenetic protein 4 (BMP-4) in mice. In order to clarify whether cathepsin H also regulates BMP-4 in humans, its impact on BMP-4 expression, processing and degradation was investigated in prostate cancer (PC-3), osteosarcoma (HOS) and pro-monocytic (U937) human cell lines. Materials and methods. BMP-4 expression was founded to be regulated by cathepsin H using PCR array technology and confirmed by real time PCR. Immunoassays including Western blot and confocal microscopy were used to evaluate the influence of cathepsin H on BMP-4 processing. Results. In contrast to HOS, the expression of BMP-4 mRNA in U937 and PC3 cells was significantly decreased by cathepsin H. The different regulation of BMP-4 synthesis could be associated with the absence of the mature 28 kDa cathepsin H form in HOS cells, where only the intermediate 30 kDa form was observed. No co-localization of BMP-4 and cathepsin H was observed in human cell lines and the multistep processing of BMP-4 was not altered in the presence of specific cathepsin H inhibitor. Isolated cathepsin H does not cleave mature recombinant BMP-4, neither with its amino- nor its endopeptidase activity. Conclusions. Our results exclude direct proteolytic processing of BMP-4 by cathepsin H, however, they provide support for its involvement in the regulation of BMP-4 expression. |
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| Publication status: | Published |
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| Publication version: | Version of Record |
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| Publication date: | 01.01.2011 |
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| Publisher: | Association of Radiology and Oncology |
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| Year of publishing: | 2011 |
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| Number of pages: | str. 259-266, II |
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| Numbering: | Vol. 45, no. 4 |
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| Source: | Ljubljana |
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| PID: | 20.500.12556/DiRROS-18457  |
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| UDC: | 577 |
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| ISSN on article: | 1318-2099 |
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| DOI: | 10.2478/v10019-011-0034-3 |
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| COBISS.SI-ID: | 3157361 |
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| Copyright: | by Authors |
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| Note: | Soavtorji: Zala Jevnikar, Bojana Mirković, Damjan Janeš, Nace Zidar, Danijel Kikelj, Janko Kos;
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| Publication date in DiRROS: | 18.03.2024 |
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| Views: | 1168 |
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| Downloads: | 759 |
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