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The Use of Reverse Phase Protein Arrays RPPA to Explore Protein Expression Variation within Individual Renal Cell Cancers
Published on: January 22, 2013
Bio-informatics analysis of renal carcinoma gene matrix metalloproteinase-7
1Department of Medical Oncology, The First Affiliated Hospital of Zhengzhou University, and Henan Cancer Hospital, Affiliated to Zhengzhou University, Zhengzhou, Henan, China.
Background:
Renal cancer is one of the common malignant tumors of the urinary system, seriously threatening human being's health. The current discoveries, however, are far enough for efficient and secure treatment of renal cancer.
Aims:
The aim was to explore the mechanism of matrix metalloproteinase-7 (MMP-7) protein in renal carcinoma cell metastasis by bioinformatics analysis.
Materials And Methods:
Bioinformatics methods were used to analyze the composition of amino acids, as well as transmembrane structure, coiled coils, subcellular localization, signal peptide, functions and structures at all levels.
Results And Conclusions:
It showed that the gene MMP-7 totally had 1131 bp. A peptide chain containing 267 amino acids was encoded in the coding region. Based on random coil, α helix, and further super-helix, it had formed a stable neutral hydrophilic protein. The subcellular location analysis indicated that the protein was located outside the cell. The mature peptide started from the 18th amino acid, and its front-end was the sequence of the signal peptide, belonging to the secreted protein. Analysis of the functional domain showed that this protein had two functional domains, the PG binding domain, and the zinc finger binding domain. Moreover, the protein, which was cross-linked with it, was also one related to cancer cell proliferation and metastasis. To sum up, MMP-7 is a stable neutral hydrophilic secreted protein, and it may play a vital role in the invasion and metastasis of cancer cells.
Insights
Matrix metalloproteinase-7 (MMP-7) is a secreted protein that may drive renal carcinoma cell metastasis. Bioinformatics analysis revealed its structure and functional domains, suggesting a vital role in cancer progression.
Area of Science:
- Oncology
- Molecular Biology
- Bioinformatics
Background:
- Renal cancer poses a significant threat to human health.
- Current treatments for renal cancer are insufficient for effective and secure management.
Purpose of the Study:
- To investigate the role of matrix metalloproteinase-7 (MMP-7) in renal carcinoma cell metastasis using bioinformatics.
- To elucidate the molecular mechanisms underlying MMP-7's involvement in cancer progression.
Main Methods:
- Bioinformatics analysis was employed to study MMP-7.
- Analysis included amino acid composition, protein structure (transmembrane, coiled coils), subcellular localization, signal peptide identification, and functional domains.
Main Results:
- The MMP-7 gene is 1131 bp, encoding a 267-amino acid peptide.
- MMP-7 forms a stable, neutral, hydrophilic secreted protein located extracellularly.
- Functional domains identified include PG binding and zinc finger binding domains, linked to cancer cell proliferation and metastasis.
Conclusions:
- MMP-7 is characterized as a stable, neutral, hydrophilic secreted protein.
- MMP-7 likely plays a critical role in the invasion and metastasis of renal cancer cells.
- Further research into MMP-7 could lead to novel therapeutic strategies for renal cancer.
