Pharmaceutical compositions containing the enzyme cyprosin, an aspartic peptidase from cynara cardunculus and its inclusion in antitumour formulations

A composition and technology of cardoon, applied in the field of recombinant cyprosin and pharmaceutical preparations, can solve the problem of no direct relationship report between peptidase and PCD

Inactive Publication Date: 2010-09-29
ECBIO INVESTIGACAO E DESENVOLVIMENTO EM BIOTECHA SA
View PDF1 Cites 2 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0018] Compared with the existing knowledge in animal model PCD, there is no report on the direct relationship between peptidase and PCD in plant cells

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Pharmaceutical compositions containing the enzyme cyprosin, an aspartic peptidase from cynara cardunculus and its inclusion in antitumour formulations
  • Pharmaceutical compositions containing the enzyme cyprosin, an aspartic peptidase from cynara cardunculus and its inclusion in antitumour formulations
  • Pharmaceutical compositions containing the enzyme cyprosin, an aspartic peptidase from cynara cardunculus and its inclusion in antitumour formulations

Examples

Experimental program
Comparison scheme
Effect test

Embodiment I

[0049] Antitumor activity of natural cyprosin preparations comprising two structural chains: N-terminal chain (composed of N-terminal propeptide and mature N-terminal) and C-terminal chain (mature peptide C-terminal) , which is isolated and purified from dried cardoon flowers.

[0050] The cyprosin preparation was obtained from dried cardoon flowers as previously described by Brodelius et al., 1995 . The antitumor activity of the enzyme preparation was evaluated with 4 kinds of human tumor cell lines and 2 kinds of non-tumor cell lines. The 4 kinds of human tumor cell lines were: epithelial cell lines derived from colon cancer (HCT116, ATCC CCL-247), Epithelial cell line from fibrosarcoma (HT1080, ATCCCCL-121), rhabdomyosarcoma (TE671, ATCC CCL-136), and adenocarcinoma (Hela, ATCC CCL-2TM) ; The 2 non-neoplastic cell lines: one consisting of human intestinal (epithelial) cells (FHs74Int, ATCC CCL-241) and the other consisting of Vero cells (Vero, ATCC CRL-1587).

[0051] The...

Embodiment II

[0096] Antitumor activity of recombinant cyprosin preparations comprising two structural chains: the N-terminal chain (composed of the N-terminal propeptide and the mature N-terminal) and the C-terminal chain (composed of the mature C-terminal peptide ) was isolated and purified from the culture medium of Saccharomyces cerevisiae strain transformed with CYPRO11.

[0097] The cyprosin preparation was obtained from the culture supernatant of a Saccharomyces cerevisiae strain (BJ1991 ) transformed with the CYPRO11 gene encoding cyprosin as described above (Pais et al., 2000). The antitumor activity of the enzyme preparation was determined on a human tumor epithelial cell line derived from colon cancer (HCT116, ATCCCCL-247) and a non-tumor cell line composed of human intestinal epithelial cells (FHs74Int, ATCC CCL-241).

[0098] The tumor cell line HCT116 was inoculated on basal medium DMEM (Cambrex) supplemented with fetal bovine serum (FBS-Gibco). The final concentrations of gl...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

No PUM Login to view more

Abstract

The object of the present invention is the use of a preparation containing a phytepsin, more specifically a cyprosin, containing the heterodimer, its N-terminal pro-peptide, the mature N-terminal peptide, and mature C-terminal peptide, as well as other precursor species, processing products, and aggregate species, either isolated or in any combinations of the former, native, extracted and partially purified from flowers of Cynara cardunculus, or recombinant, extracted from the supernatant from a culture of Saccharomyces cereviseae genetically modified for the heterologous production of cyprosin, for therapeutic applications more precisely for its use as an antitumor agent.

Description

technical field [0001] The present invention aims at the development of pharmaceutical preparations containing phytepsin preparations, more specifically cyprosin preparations, which are characterized as aspartic proteases native to cardoon flowers (accession number UniProtKB / TrEMBL: Q39476). [0002] The present invention aims at preparing said cyprosin, said cyprosin contains: [0003] heterodimer, [0004] cyprosin pre-propeptide (pre-propeptide), and / or [0005] cyprosin propeptides containing N-terminal and / or leaf / chain / N-terminal mature subunits, and / or [0006] cyprosin propeptide containing C-terminal and / or PSI domain specific to plant phytepsin and / or leaf / polypeptide chain / N-terminal mature subunit, and / or [0007] an isolated polypeptide comprising a PSI domain, or [0008] any other secondary products resulting from processing or degradation of the original prepropeptide and other precursor species, processed products and aggregate species, [0009] The above...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
Patent Type & Authority Applications(China)
IPC IPC(8): A61K38/48A61K36/28A61P35/00
CPCA61K36/28A61K38/488A61P1/00A61P1/14A61P31/14A61P35/00A61P9/00A61P9/12Y02A50/30
Inventor M·S·索瑞斯派斯P·N·德索萨萨姆派奥R·I·甘查斯索瑞斯M·C·巴普蒂斯塔库尔霍J·M·斯尔瓦桑托斯P·E·达克鲁兹H·J·索瑞斯达克鲁兹
Owner ECBIO INVESTIGACAO E DESENVOLVIMENTO EM BIOTECHA SA
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap