Kallikrein-related peptidase 7 overexpression in melanoma cells modulates cell adhesion leading to a malignant phenotype
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Meriem Haddada
Abstract
We recently reported that human melanoma cells, but not benign melanocytes, aberrantly express kallikrein-related peptidase 7 (KLK7). Here, we show a KLK7 overexpression-mediated decrease of cell adhesion to extracellular matrix binding proteins, associated with downregulation of α5/β1/αv/β3 integrin expression. We also report an up-regulation of MCAM/CD146 and an increase in spheroid formation of these cells. Our results demonstrate that aberrant KLK7 expression leads to a switch to a more malignant phenotype suggesting a potential role of KLK7 in melanoma invasion. Thus, KLK7 may represent a biomarker for melanoma progression and may be a potential therapeutic target for melanoma.
Acknowledgments
The authors thank IUH Technological Platform for their help. This work was supported by the Institut National de la Santé et de la Recherche Médicale (INSERM) and a mobility grant by the Centre de Coopération Universitaire Franco-Bavarois (V.M. and D.D.).
Conflicts of interest statement: None to declare.
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Supplementary Material:
The online version of this article offers supplementary material (https://doi.org/10.1515/hsz-2017-0339).
©2018 Walter de Gruyter GmbH, Berlin/Boston
Articles in the same Issue
- 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
Articles in the same Issue
- 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