Abstract
Tissue kallikrein, kallikrein-related peptidases (KLKs), and plasma kallikrein form the largest group of serine proteases in the human genome, sharing many structural and functional characteristics. In this study, we describe the molecular cloning of four novel splice variants of the human KLK11 and KLK12 genes, discovered by combining 3′ rapid amplification of cDNA ends (3′ RACE), next-generation sequencing (NGS) technology, advanced bioinformatic analysis and Sanger sequencing. Expression analysis of these new transcripts in cell lines originating from 17 cancerous and two normal tissues revealed the expression pattern of each transcript. These novel KLK11 and KLK12 splice variants represent new potential cancer biomarkers.
References
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Supplementary Material:
The online version of this article offers supplementary material (https://doi.org/10.1515/hsz-2017-0294).
©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