Abstract
Human tissue kallikreins (KLKs) are 15 members of the serine protease family and are present in various healthy human tissues including airway tissues. Multiple studies have revealed their crucial role in the pathophysiology of a number of chronic, infectious and tumour lung diseases. KLK1, 3 and 14 are involved in asthma pathogenesis, and KLK1 could be also associated with the exacerbation of this inflammatory disease caused by rhinovirus. KLK5 was demonstrated as an influenza virus activating protease in humans, and KLK1 and 12 could also be involved in the activation and spread of these viruses. KLKs are associated with lung cancer, with up- or downregulation of expression depending on the KLK, cancer subtype, stage of tumour and also the microenvironment. Functional studies showed that KLK12 is a potent pro-angiogenic factor. Moreover, KLK6 promotes malignant-cell proliferation and KLK13 invasiveness. In contrast, KLK8 and KLK10 reduce proliferation and invasion of malignant cells. Considering the involvement of KLKs in various physiological and pathological processes, KLKs appear to be potential biomarkers and therapeutic targets for lung diseases.
Acknowledgements
We particularly thank Laura Smales for editing the English text. Studies conducted by our team were supported by the ‘Ligue Contre le Cancer’ and we especially thank the Departmental committees of Indre et Loire, Morbihan, Maine et Loire, Deux-Sèvres, Indre, and Cher.
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©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