Abstract
The dysregulation of the serine-protease family kallikreins (KLKs), comprising 15 genes, has been reportedly associated with cancer. Their expression in several tissues and physiological fluids makes them potential candidates as biomarkers and therapeutic targets. There are several databases available to mine gene expression in cancer, which often include clinical and pathological data. However, these platforms present some limitations when comparing a specific set of genes and can generate considerable unwanted data. Here, several datasets that showed significant differential expression (p<0.01) in cancer vs. normal (n=118), metastasis vs. primary (n=15) and association with cancer survival (n=21) have been compiled in a user-friendly format from two open and/or publicly available databases Oncomine and OncoLnc for the 15 KLKs. The data have been included in a free web application tool: the KLK-CANMAP https://cancerbioinformatics.shinyapps.io/klk-canmap/. This tool integrates, analyses and visualises data and it was developed with the R Shiny framework. Using KLK-CANMAP box-plots, heatmaps and Kaplan-Meier graphs can be generated for the KLKs of interest. We believe this new cancer KLK focused web tool will benefit the KLK community by narrowing the data visualisation to only the genes of interest.
Acknowledgements
We thank Ms. Sarah Schubert for helping extracting the data from the open Oncomine and free OncoLnc databases. We also thank the support of our funding organisations the Cancer Council Queensland, the National Health and Medical Research Council Career Development Fellowship (Dr. Jyotsna Batra) and the Prostate Cancer Foundation of Australia through the Movember Foundation.
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Supplementary Material
The online version of this article offers supplementary material (https://doi.org/10.1515/hsz-2017-0322).
©2018 Walter de Gruyter GmbH, Berlin/Boston
Artikel in diesem Heft
- Frontmatter
- Highlight: The 7th International Symposium on Kallikreins and Kallikrein-Related Peptidases
- Obituary
- Manfred Schmitt (1947–2018)
- Functional interrelationships between the kallikrein-related peptidases family and the classical kinin system in the human neutrophil
- Overview of tissue kallikrein and kallikrein-related peptidases in breast cancer
- Kallikrein-related peptidases in lung diseases
- The miRNA-kallikrein interaction: a mosaic of epigenetic regulation in cancer
- Mining human cancer datasets for kallikrein expression in cancer: the ‘KLK-CANMAP’ Shiny web tool
- Specificity profiling of human trypsin-isoenzymes
- Activation and activity of glycosylated KLKs 3, 4 and 11
- Microenvironment proteinases, proteinase-activated receptor regulation, cancer and inflammation
- Kallikrein-related peptidase 6 orchestrates astrocyte form and function through proteinase activated receptor-dependent mechanisms
- Kallikrein-related peptidase 5 and seasonal influenza viruses, limitations of the experimental models for activating proteases
- Novel splice variants of the human kallikrein-related peptidases 11 (KLK11) and 12 (KLK12), unraveled by next-generation sequencing technology
- Insights into the activity control of the kallikrein-related peptidase 6: small-molecule modulators and allosterism
- Kallikrein-related peptidase 14 is the second KLK protease targeted by the serpin vaspin
- Profiling system for skin kallikrein proteolysis applied in gene-deficient mouse models
- Evidence that cell surface localization of serine protease activity facilitates cleavage of the protease activated receptor CDCP1
- Kallikrein-related peptidase 7 overexpression in melanoma cells modulates cell adhesion leading to a malignant phenotype
- KLK5, a novel potential suppressor of vaginal carcinogenesis
Artikel in diesem Heft
- Frontmatter
- Highlight: The 7th International Symposium on Kallikreins and Kallikrein-Related Peptidases
- Obituary
- Manfred Schmitt (1947–2018)
- Functional interrelationships between the kallikrein-related peptidases family and the classical kinin system in the human neutrophil
- Overview of tissue kallikrein and kallikrein-related peptidases in breast cancer
- Kallikrein-related peptidases in lung diseases
- The miRNA-kallikrein interaction: a mosaic of epigenetic regulation in cancer
- Mining human cancer datasets for kallikrein expression in cancer: the ‘KLK-CANMAP’ Shiny web tool
- Specificity profiling of human trypsin-isoenzymes
- Activation and activity of glycosylated KLKs 3, 4 and 11
- Microenvironment proteinases, proteinase-activated receptor regulation, cancer and inflammation
- Kallikrein-related peptidase 6 orchestrates astrocyte form and function through proteinase activated receptor-dependent mechanisms
- Kallikrein-related peptidase 5 and seasonal influenza viruses, limitations of the experimental models for activating proteases
- Novel splice variants of the human kallikrein-related peptidases 11 (KLK11) and 12 (KLK12), unraveled by next-generation sequencing technology
- Insights into the activity control of the kallikrein-related peptidase 6: small-molecule modulators and allosterism
- Kallikrein-related peptidase 14 is the second KLK protease targeted by the serpin vaspin
- Profiling system for skin kallikrein proteolysis applied in gene-deficient mouse models
- Evidence that cell surface localization of serine protease activity facilitates cleavage of the protease activated receptor CDCP1
- Kallikrein-related peptidase 7 overexpression in melanoma cells modulates cell adhesion leading to a malignant phenotype
- KLK5, a novel potential suppressor of vaginal carcinogenesis