Abstract
We compared signalling pathways such as calcium transients, MAPK activation, β-arrestin interactions and receptor internalization triggered by kallikrein-related peptidases (KLKs) 8 and 14 in human and rat proteinase-activated receptor (PAR)2-expressing human embryonic kidney (HEK) and Kirsten transformed rat kidney (KNRK) cells. Further, we analysed processing by KLK8 vs. KLK14 of synthetic human and rat PAR2-derived sequences representing the cleavage-activation domain of PAR2. Our data show that like KLK14, KLK8 can unmask a PAR2 receptor-activating sequence from a peptide precursor. However, whilst KLK8, like KLK14, can signal in rat-PAR2-expressing KNRK cells, this enzyme cannot signal via human PAR2 in HEK or KNRK cells, but rather, disarms HEK PAR1. Thus, KLK8 and KLK14 can signal differentially via the PARs to affect tissue function.
©2012 by Walter de Gruyter Berlin Boston
Articles in the same Issue
- Guest Editorial
- Highlight: The 4th International Symposium on Kallikreins and Kallikrein-Related Peptidases
- Kallikrein-related peptidases in prostate, breast, and ovarian cancers: from pathobiology to clinical relevance
- Epigenetic regulation of kallikrein-related peptidases: there is a whole new world out there
- Non-combinatorial library screening reveals subsite cooperativity and identifies new high-efficiency substrates for kallikrein-related peptidase 14
- One round of SELEX for the generation of DNA aptamers directed against KLK6
- Kallikrein 6 is a novel molecular trigger of reactive astrogliosis
- Characterization of SPINK9, a KLK5-specific inhibitor expressed in palmo-plantar epidermis
- The miRNA-kallikrein axis of interaction: a new dimension in the pathogenesis of prostate cancer
- Stromal cell-associated expression of kallikrein-related peptidase 6 (KLK6) indicates poor prognosis of ovarian cancer patients
- The kallikrein 14 gene is down-regulated by androgen receptor signalling and harbours genetic variation that is associated with prostate tumour aggressiveness
- Kallikrein-related peptidase signaling in colon carcinoma cells: targeting proteinase-activated receptors
- Proteinase-activated receptors (PARs): differential signalling by kallikrein-related peptidases KLK8 and KLK14
- Masthead
- Masthead
Articles in the same Issue
- Guest Editorial
- Highlight: The 4th International Symposium on Kallikreins and Kallikrein-Related Peptidases
- Kallikrein-related peptidases in prostate, breast, and ovarian cancers: from pathobiology to clinical relevance
- Epigenetic regulation of kallikrein-related peptidases: there is a whole new world out there
- Non-combinatorial library screening reveals subsite cooperativity and identifies new high-efficiency substrates for kallikrein-related peptidase 14
- One round of SELEX for the generation of DNA aptamers directed against KLK6
- Kallikrein 6 is a novel molecular trigger of reactive astrogliosis
- Characterization of SPINK9, a KLK5-specific inhibitor expressed in palmo-plantar epidermis
- The miRNA-kallikrein axis of interaction: a new dimension in the pathogenesis of prostate cancer
- Stromal cell-associated expression of kallikrein-related peptidase 6 (KLK6) indicates poor prognosis of ovarian cancer patients
- The kallikrein 14 gene is down-regulated by androgen receptor signalling and harbours genetic variation that is associated with prostate tumour aggressiveness
- Kallikrein-related peptidase signaling in colon carcinoma cells: targeting proteinase-activated receptors
- Proteinase-activated receptors (PARs): differential signalling by kallikrein-related peptidases KLK8 and KLK14
- Masthead
- Masthead