The molecular function of kallikrein‐related peptidase 14 demonstrates a key modulatory role in advanced prostate cancer
Kallikrein‐related peptidase 14 (KLK14) is one of the several secreted KLK serine proteases involved in prostate cancer (PCa) pathogenesis. While relatively understudied, recent reports have identified KLK14 as overexpressed during PCa development. However, the modulation of KLK14 expression during...
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| Published in | Molecular oncology Vol. 14; no. 1; pp. 105 - 128 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
John Wiley & Sons, Inc
01.01.2020
John Wiley and Sons Inc Wiley |
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| Abstract | Kallikrein‐related peptidase 14 (KLK14) is one of the several secreted KLK serine proteases involved in prostate cancer (PCa) pathogenesis. While relatively understudied, recent reports have identified KLK14 as overexpressed during PCa development. However, the modulation of KLK14 expression during PCa progression and the molecular and biological functions of this protease in the prostate tumor microenvironment remain unknown. To determine the modulation of KLK14 expression during PCa progression, we analyzed the expression levels of KLK14 in patient samples using publicly available databases and immunohistochemistry. In order to delineate the molecular mechanisms involving KLK14 in PCa progression, we integrated proteomic, transcriptomic, and in vitro assays with the goal to identify substrates, related‐signaling pathways, and functional roles of this protease. We showed that KLK14 expression is elevated in advanced PCa, and particularly in metastasis. Additionally, KLK14 levels were found to be decreased in PCa tissues from patients responsive to neoadjuvant therapy compared to untreated patients. Furthermore, we also identified that KLK14 expression reoccurred in patients who developed castrate‐resistant PCa. The combination of proteomic and transcriptomic analysis as well as functional assays revealed several new KLK14 substrates (agrin, desmoglein 2, vitronectin, laminins) and KLK14‐regulated genes (Interleukin 32, midkine, SRY‐Box 9), particularly an involvement of the mitogen‐activated protein kinase 1 and interleukin 1 receptor pathways, and an involvement of KLK14 in the regulation of cellular migration, supporting its involvement in aggressive features of PCa progression. In conclusion, our work showed that KLK14 expression is associated with the development of aggressive PCa suggesting that targeting this protease could offer a novel route to limit the progression of prostate tumors. Additional work is necessary to determine the benefits and implications of targeting/cotargeting KLK14 in PCa as well as to determine the potential use of KLK14 expression as a predictor of PCa aggressiveness or response to treatment.
Kallikrein‐related peptidase 14 (KLK14) is a secreted serine protease belonging to the kallikrein‐related‐peptidase family. We identified that KLK14 is overexpressed in advanced prostate cancer and acts on various substrates involved in adhesion, migration, and invasion of cancer cells, thus modulating genes and signaling pathways essential for prostate cancer progression. These results suggest that KLK14 is a potential target to control aggressiveness of prostate tumors. |
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| AbstractList | Kallikrein‐related peptidase 14 (KLK14) is one of the several secreted KLK serine proteases involved in prostate cancer (PCa) pathogenesis. While relatively understudied, recent reports have identified KLK14 as overexpressed during PCa development. However, the modulation of KLK14 expression during PCa progression and the molecular and biological functions of this protease in the prostate tumor microenvironment remain unknown. To determine the modulation of KLK14 expression during PCa progression, we analyzed the expression levels of KLK14 in patient samples using publicly available databases and immunohistochemistry. In order to delineate the molecular mechanisms involving KLK14 in PCa progression, we integrated proteomic, transcriptomic, and
in vitro
assays with the goal to identify substrates, related‐signaling pathways, and functional roles of this protease. We showed that KLK14 expression is elevated in advanced PCa, and particularly in metastasis. Additionally, KLK14 levels were found to be decreased in PCa tissues from patients responsive to neoadjuvant therapy compared to untreated patients. Furthermore, we also identified that KLK14 expression reoccurred in patients who developed castrate‐resistant PCa. The combination of proteomic and transcriptomic analysis as well as functional assays revealed several new KLK14 substrates (agrin, desmoglein 2, vitronectin, laminins) and KLK14‐regulated genes (Interleukin 32, midkine, SRY‐Box 9), particularly an involvement of the mitogen‐activated protein kinase 1 and interleukin 1 receptor pathways, and an involvement of KLK14 in the regulation of cellular migration, supporting its involvement in aggressive features of PCa progression. In conclusion, our work showed that KLK14 expression is associated with the development of aggressive PCa suggesting that targeting this protease could offer a novel route to limit the progression of prostate tumors. Additional work is necessary to determine the benefits and implications of targeting/cotargeting KLK14 in PCa as well as to determine the potential use of KLK14 expression as a predictor of PCa aggressiveness or response to treatment. Kallikrein‐related peptidase 14 (KLK14) is one of the several secreted KLK serine proteases involved in prostate cancer (PCa) pathogenesis. While relatively understudied, recent reports have identified KLK14 as overexpressed during PCa development. However, the modulation of KLK14 expression during PCa progression and the molecular and biological functions of this protease in the prostate tumor microenvironment remain unknown. To determine the modulation of KLK14 expression during PCa progression, we analyzed the expression levels of KLK14 in patient samples using publicly available databases and immunohistochemistry. In order to delineate the molecular mechanisms involving KLK14 in PCa progression, we integrated proteomic, transcriptomic, and in vitro assays with the goal to identify substrates, related‐signaling pathways, and functional roles of this protease. We showed that KLK14 expression is elevated in advanced PCa, and particularly in metastasis. Additionally, KLK14 levels were found to be decreased in PCa tissues from patients responsive to neoadjuvant therapy compared to untreated patients. Furthermore, we also identified that KLK14 expression reoccurred in patients who developed castrate‐resistant PCa. The combination of proteomic and transcriptomic analysis as well as functional assays revealed several new KLK14 substrates (agrin, desmoglein 2, vitronectin, laminins) and KLK14‐regulated genes (Interleukin 32, midkine, SRY‐Box 9), particularly an involvement of the mitogen‐activated protein kinase 1 and interleukin 1 receptor pathways, and an involvement of KLK14 in the regulation of cellular migration, supporting its involvement in aggressive features of PCa progression. In conclusion, our work showed that KLK14 expression is associated with the development of aggressive PCa suggesting that targeting this protease could offer a novel route to limit the progression of prostate tumors. Additional work is necessary to determine the benefits and implications of targeting/cotargeting KLK14 in PCa as well as to determine the potential use of KLK14 expression as a predictor of PCa aggressiveness or response to treatment. Kallikrein‐related peptidase 14 (KLK14) is one of the several secreted KLK serine proteases involved in prostate cancer (PCa) pathogenesis. While relatively understudied, recent reports have identified KLK14 as overexpressed during PCa development. However, the modulation of KLK14 expression during PCa progression and the molecular and biological functions of this protease in the prostate tumor microenvironment remain unknown. To determine the modulation of KLK14 expression during PCa progression, we analyzed the expression levels of KLK14 in patient samples using publicly available databases and immunohistochemistry. In order to delineate the molecular mechanisms involving KLK14 in PCa progression, we integrated proteomic, transcriptomic, and in vitro assays with the goal to identify substrates, related‐signaling pathways, and functional roles of this protease. We showed that KLK14 expression is elevated in advanced PCa, and particularly in metastasis. Additionally, KLK14 levels were found to be decreased in PCa tissues from patients responsive to neoadjuvant therapy compared to untreated patients. Furthermore, we also identified that KLK14 expression reoccurred in patients who developed castrate‐resistant PCa. The combination of proteomic and transcriptomic analysis as well as functional assays revealed several new KLK14 substrates (agrin, desmoglein 2, vitronectin, laminins) and KLK14‐regulated genes (Interleukin 32, midkine, SRY‐Box 9), particularly an involvement of the mitogen‐activated protein kinase 1 and interleukin 1 receptor pathways, and an involvement of KLK14 in the regulation of cellular migration, supporting its involvement in aggressive features of PCa progression. In conclusion, our work showed that KLK14 expression is associated with the development of aggressive PCa suggesting that targeting this protease could offer a novel route to limit the progression of prostate tumors. Additional work is necessary to determine the benefits and implications of targeting/cotargeting KLK14 in PCa as well as to determine the potential use of KLK14 expression as a predictor of PCa aggressiveness or response to treatment. Kallikrein‐related peptidase 14 (KLK14) is one of the several secreted KLK serine proteases involved in prostate cancer (PCa) pathogenesis. While relatively understudied, recent reports have identified KLK14 as overexpressed during PCa development. However, the modulation of KLK14 expression during PCa progression and the molecular and biological functions of this protease in the prostate tumor microenvironment remain unknown. To determine the modulation of KLK14 expression during PCa progression, we analyzed the expression levels of KLK14 in patient samples using publicly available databases and immunohistochemistry. In order to delineate the molecular mechanisms involving KLK14 in PCa progression, we integrated proteomic, transcriptomic, and in vitro assays with the goal to identify substrates, related‐signaling pathways, and functional roles of this protease. We showed that KLK14 expression is elevated in advanced PCa, and particularly in metastasis. Additionally, KLK14 levels were found to be decreased in PCa tissues from patients responsive to neoadjuvant therapy compared to untreated patients. Furthermore, we also identified that KLK14 expression reoccurred in patients who developed castrate‐resistant PCa. The combination of proteomic and transcriptomic analysis as well as functional assays revealed several new KLK14 substrates (agrin, desmoglein 2, vitronectin, laminins) and KLK14‐regulated genes (Interleukin 32, midkine, SRY‐Box 9), particularly an involvement of the mitogen‐activated protein kinase 1 and interleukin 1 receptor pathways, and an involvement of KLK14 in the regulation of cellular migration, supporting its involvement in aggressive features of PCa progression. In conclusion, our work showed that KLK14 expression is associated with the development of aggressive PCa suggesting that targeting this protease could offer a novel route to limit the progression of prostate tumors. Additional work is necessary to determine the benefits and implications of targeting/cotargeting KLK14 in PCa as well as to determine the potential use of KLK14 expression as a predictor of PCa aggressiveness or response to treatment. Kallikrein‐related peptidase 14 (KLK14) is a secreted serine protease belonging to the kallikrein‐related‐peptidase family. We identified that KLK14 is overexpressed in advanced prostate cancer and acts on various substrates involved in adhesion, migration, and invasion of cancer cells, thus modulating genes and signaling pathways essential for prostate cancer progression. These results suggest that KLK14 is a potential target to control aggressiveness of prostate tumors. Kallikrein‐related peptidase 14 (KLK14) is one of the several secreted KLK serine proteases involved in prostate cancer (PCa) pathogenesis. While relatively understudied, recent reports have identified KLK14 as overexpressed during PCa development. However, the modulation of KLK14 expression during PCa progression and the molecular and biological functions of this protease in the prostate tumor microenvironment remain unknown. To determine the modulation of KLK14 expression during PCa progression, we analyzed the expression levels of KLK14 in patient samples using publicly available databases and immunohistochemistry. In order to delineate the molecular mechanisms involving KLK14 in PCa progression, we integrated proteomic, transcriptomic, and in vitro assays with the goal to identify substrates, related‐signaling pathways, and functional roles of this protease. We showed that KLK14 expression is elevated in advanced PCa, and particularly in metastasis. Additionally, KLK14 levels were found to be decreased in PCa tissues from patients responsive to neoadjuvant therapy compared to untreated patients. Furthermore, we also identified that KLK14 expression reoccurred in patients who developed castrate‐resistant PCa. The combination of proteomic and transcriptomic analysis as well as functional assays revealed several new KLK14 substrates (agrin, desmoglein 2, vitronectin, laminins) and KLK14‐regulated genes (Interleukin 32, midkine, SRY‐Box 9), particularly an involvement of the mitogen‐activated protein kinase 1 and interleukin 1 receptor pathways, and an involvement of KLK14 in the regulation of cellular migration, supporting its involvement in aggressive features of PCa progression. In conclusion, our work showed that KLK14 expression is associated with the development of aggressive PCa suggesting that targeting this protease could offer a novel route to limit the progression of prostate tumors. Additional work is necessary to determine the benefits and implications of targeting/cotargeting KLK14 in PCa as well as to determine the potential use of KLK14 expression as a predictor of PCa aggressiveness or response to treatment. Kallikrein‐related peptidase 14 (KLK14) is a secreted serine protease belonging to the kallikrein‐related‐peptidase family. We identified that KLK14 is overexpressed in advanced prostate cancer and acts on various substrates involved in adhesion, migration, and invasion of cancer cells, thus modulating genes and signaling pathways essential for prostate cancer progression. These results suggest that KLK14 is a potential target to control aggressiveness of prostate tumors. |
| Audience | Academic |
| Author | Srinivasan, Srilakshmi Rockstroh, Anja Williams, Elizabeth D. Lovell, Scott Panchadsaram, Janaththani Harris, Jonathan Tate, Edward W. Nelson, Colleen Lehman, Melanie L. Bock, Nathalie Gleave, Martin Fazli, Ladan Kryza, Thomas Lesner, Adam Hooper, John D. Clements, Judith A. Snell, Cameron E. Silva, Lakmali Munasinghage Batra, Jyotsna |
| AuthorAffiliation | 3 Translational Research Institute Woolloongabba Australia 1 Australian Prostate Cancer Research Centre‐Queensland (APCRC‐Q) Institute of Health & Biomedical Innovation Queensland University of Technology Woolloongabba Australia 7 Faculty of Chemistry University of Gdansk Poland 8 Mater Health Services South Brisbane Australia 2 School of Biomedical Sciences Faculty of Health Queensland University of Technology Woolloongabba Australia 6 Vancouver Prostate Centre Department of Urologic Sciences University of British Columbia Canada 5 Department of Chemistry Imperial College London UK 4 Mater Research Institute – The University of Queensland Brisbane Australia |
| AuthorAffiliation_xml | – name: 6 Vancouver Prostate Centre Department of Urologic Sciences University of British Columbia Canada – name: 3 Translational Research Institute Woolloongabba Australia – name: 2 School of Biomedical Sciences Faculty of Health Queensland University of Technology Woolloongabba Australia – name: 7 Faculty of Chemistry University of Gdansk Poland – name: 4 Mater Research Institute – The University of Queensland Brisbane Australia – name: 8 Mater Health Services South Brisbane Australia – name: 5 Department of Chemistry Imperial College London UK – name: 1 Australian Prostate Cancer Research Centre‐Queensland (APCRC‐Q) Institute of Health & Biomedical Innovation Queensland University of Technology Woolloongabba Australia |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31630475$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1515/cclm-2019-0123 10.1084/jem.20131797 10.1002/pros.22978 10.1016/j.ccr.2010.05.026 10.1155/2012/169170 10.1097/CCO.0000000000000520 10.1371/journal.pgen.1005389 10.1074/jbc.M608348200 10.1016/j.amjms.2017.04.019 10.1515/hsz-2016-0163 10.1016/j.biochi.2010.06.022 10.1002/pros.22607 10.1160/TH12-07-0518 10.1515/BC.2007.124 10.1093/bioinformatics/btt703 10.1007/s00432-018-2623-7 10.1515/hsz-2018-0451 10.1038/nrc2228 10.1038/s41598-017-15415-4 10.1159/000132565 10.18632/oncotarget.11790 10.1210/er.2009-0034 10.1038/onc.2015.127 10.1006/geno.2000.6490 10.1155/2011/249290 10.3390/cancers9060067 10.1038/ng.629 10.1074/mcp.RA118.001304 10.1038/ncomms7184 10.1016/S1476-5586(04)80047-2 10.1038/nprot.2011.382 10.1038/s41416-018-0260-1 10.1038/s41413-019-0049-8 10.18632/oncotarget.3743 10.1038/s41598-017-11914-6 10.1002/pros.10263 10.1515/bc-2011-250 10.3109/10408363.2016.1154643 10.1002/pros.22670 10.1074/jbc.M115.679084 10.1074/jbc.M705190200 10.1038/nature11125 10.1016/j.cell.2009.02.034 10.3389/fendo.2018.00483 10.1073/pnas.1318548111 10.1515/bc-2011-231 10.1093/annonc/mdy082 10.1038/bjc.2011.163 10.1186/s12885-017-3617-6 10.1016/j.jid.2016.09.017 10.1016/j.biochi.2015.09.002 10.1515/hsz-2011-0268 10.2108/zsj.24.774 10.1186/1755-8794-1-6 10.1016/j.ccell.2017.09.003 10.1242/dmm.033100 10.1016/j.biomaterials.2018.10.014 10.1371/journal.pone.0098786 10.1186/1471-2407-7-64 10.1158/1940-6207.CAPR-12-0293-T |
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| Copyright | 2019 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. COPYRIGHT 2020 John Wiley & Sons, Inc. 2020. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. |
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| Keywords | protease protease-substrate prostate cancer metastasis kallikrein-related peptidase castrate-resistant prostate cancer |
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| License | Attribution 2019 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
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| References | 2017; 7 2012; 2012 2012; 487 2010; 18 2019; 57 2015; 75 2019; 190–191 2004; 6 2019; 18 2008; 1 2017; 354 2013; 6 2017; 9 2016; 35 2014; 211 2003; 56 2018; 9 2015; 290 2008; 29 2017; 32 2016; 397 2007; 7 2014; 9 2007; 24 2019; 7 2018; 144 2018; 29 2010; 31 2015; 6 2013; 109 2019; 31 2007; 282 2015; 11 2007b; 282 2016; 53 2016; 122 2014; 111 2011; 6 2017; 137 2009; 136 2012; 393 2011; 104 2011; 2011 2007a; 388 2016; 7 2010; 42 2017; 17 2018; 119 2013; 73 2019 2010; 92 2018; 12 2014; 30 2018; 11 2003; 63 2001; 73 e_1_2_10_23_1 e_1_2_10_46_1 e_1_2_10_21_1 e_1_2_10_44_1 e_1_2_10_42_1 e_1_2_10_40_1 e_1_2_10_2_1 e_1_2_10_4_1 e_1_2_10_18_1 e_1_2_10_53_1 e_1_2_10_6_1 e_1_2_10_16_1 e_1_2_10_39_1 e_1_2_10_55_1 e_1_2_10_8_1 e_1_2_10_14_1 e_1_2_10_37_1 e_1_2_10_57_1 e_1_2_10_58_1 e_1_2_10_13_1 e_1_2_10_34_1 e_1_2_10_11_1 e_1_2_10_32_1 e_1_2_10_30_1 e_1_2_10_51_1 e_1_2_10_61_1 Innocenti M (e_1_2_10_27_1) 2018; 12 e_1_2_10_29_1 e_1_2_10_25_1 e_1_2_10_48_1 e_1_2_10_24_1 e_1_2_10_45_1 e_1_2_10_22_1 e_1_2_10_43_1 Zhang XA (e_1_2_10_63_1) 2003; 63 e_1_2_10_20_1 e_1_2_10_41_1 e_1_2_10_52_1 e_1_2_10_3_1 e_1_2_10_19_1 e_1_2_10_54_1 e_1_2_10_5_1 e_1_2_10_17_1 e_1_2_10_38_1 e_1_2_10_56_1 e_1_2_10_7_1 e_1_2_10_15_1 e_1_2_10_36_1 e_1_2_10_12_1 e_1_2_10_35_1 e_1_2_10_9_1 e_1_2_10_59_1 e_1_2_10_10_1 e_1_2_10_33_1 e_1_2_10_31_1 e_1_2_10_50_1 e_1_2_10_60_1 e_1_2_10_62_1 e_1_2_10_28_1 e_1_2_10_49_1 e_1_2_10_26_1 e_1_2_10_47_1 |
| References_xml | – volume: 397 start-page: 1299 year: 2016 end-page: 1305 article-title: evidence that KLK14 regulates the components of the HGF/Met axis, pro‐HGF and HGF‐activator inhibitor 1A and 1B publication-title: Biol Chem – volume: 6 start-page: 6184 year: 2015 article-title: An oncogenic role of Agrin in regulating focal adhesion integrity in hepatocellular carcinoma publication-title: Nat Commun – volume: 24 start-page: 774 year: 2007 end-page: 780 article-title: Expression and enzymatic characterization of recombinant human kallikrein 14 publication-title: Zoolog Sci – volume: 9 start-page: 67 year: 2017 article-title: Androgen receptor‐dependent and ‐independent mechanisms involved in prostate cancer therapy resistance publication-title: Cancers (Basel) – volume: 136 start-page: 1161 year: 2009 end-page: 1171 article-title: Coincident pre‐ and postsynaptic activation induces dendritic filopodia via neurotrypsin‐dependent agrin cleavage publication-title: Cell – volume: 75 start-page: 957 year: 2015 end-page: 968 article-title: Over‐expression of lipocalin 2 promotes cell migration and invasion through activating ERK signaling to increase SLUG expression in prostate cancer publication-title: Prostate – volume: 7 start-page: 64309 year: 2016 end-page: 64317 article-title: Lipocalin 2 over‐expression facilitates progress of castration‐resistant prostate cancer via improving androgen receptor transcriptional activity publication-title: Oncotarget – volume: 9 year: 2014 article-title: Characterization of desmoglein expression in the normal prostatic gland. Desmoglein 2 is an independent prognostic factor for aggressive prostate cancer publication-title: PLoS ONE – volume: 53 start-page: 277 year: 2016 end-page: 291 article-title: Kallikrein‐related peptidases (KLKs) and the hallmarks of cancer publication-title: Crit Rev Clin Lab Sci – volume: 282 start-page: 31852 year: 2007 end-page: 31864 article-title: Activation profiles and regulatory cascades of the human kallikrein‐related peptidases publication-title: J Biol Chem – volume: 29 start-page: 1 year: 2008 end-page: 8 article-title: High expression of KLK14 in prostatic adenocarcinoma is associated with elevated risk of prostate‐specific antigen relapse publication-title: Tumour Biol – volume: 393 start-page: 413 year: 2012 end-page: 420 article-title: Kallikrein‐related peptidase signaling in colon carcinoma cells: targeting proteinase‐activated receptors publication-title: Biol Chem – volume: 6 start-page: 495 year: 2013 end-page: 505 article-title: Curcumin‐targeting pericellular serine protease matriptase role in suppression of prostate cancer cell invasion, tumor growth, and metastasis publication-title: Cancer Prev Res (Phila) – volume: 18 start-page: 818 year: 2019 end-page: 836 article-title: Integration of two in‐depth quantitative proteomics approaches determines the kallikrein‐related peptidase 7 (KLK7) degradome in ovarian cancer cell secretome publication-title: Mol Cell Proteomics – volume: 63 start-page: 2665 year: 2003 end-page: 2674 article-title: EWI2/PGRL associates with the metastasis suppressor KAI1/CD82 and inhibits the migration of prostate cancer cells publication-title: Cancer Res – volume: 56 start-page: 287 year: 2003 end-page: 292 article-title: Differential expression of the human kallikrein gene 14 (KLK14) in normal and cancerous prostatic tissues publication-title: Prostate – volume: 42 start-page: 676 year: 2010 end-page: 683 article-title: Matriptase initiates activation of epidermal pro‐kallikrein and disease onset in a mouse model of Netherton syndrome publication-title: Nat Genet – volume: 190–191 start-page: 63 year: 2019 end-page: 75 article-title: A 3D tumor microenvironment regulates cell proliferation, peritoneal growth and expression patterns publication-title: Biomaterials – volume: 487 start-page: 239 year: 2012 end-page: 243 article-title: The mutational landscape of lethal castration‐resistant prostate cancer publication-title: Nature – volume: 6 start-page: 1578 year: 2011 end-page: 1611 article-title: Identifying and quantifying proteolytic events and the natural N terminome by terminal amine isotopic labeling of substrates publication-title: Nat Protoc – volume: 6 start-page: 13088 year: 2015 end-page: 13104 article-title: Identification of novel genes that regulate androgen receptor signaling and growth of androgen‐deprived prostate cancer cells publication-title: Oncotarget – volume: 7 start-page: 15101 year: 2017 article-title: The kunitz domain i of hepatocyte growth factor activator inhibitor‐2 inhibits matriptase activity and invasive ability of human prostate cancer cells publication-title: Sci Rep – volume: 29 start-page: 1292 year: 2018 end-page: 1303 article-title: MSR1 repeats modulate gene expression and affect risk of breast and prostate cancer publication-title: Ann Oncol – volume: 11 year: 2015 article-title: KLK5 inactivation reverses cutaneous hallmarks of netherton syndrome publication-title: PLOS Genet – volume: 35 start-page: 549 year: 2016 end-page: 557 article-title: Induction of the intestinal stem cell signature gene SMOC‐2 is required for L1‐mediated colon cancer progression publication-title: Oncogene – volume: 388 start-page: 1215 year: 2007a end-page: 1225 article-title: Defining the extended substrate specificity of kallikrein 1‐related peptidases publication-title: Biol Chem – volume: 32 start-page: 474 year: 2017 end-page: 489 article-title: Androgen receptor pathway‐independent prostate cancer is sustained through FGF signaling publication-title: Cancer Cell – volume: 7 start-page: 13 year: 2019 article-title: Engineering osteoblastic metastases to delineate the adaptive response of androgen‐deprived prostate cancer in the bone metastatic microenvironment publication-title: Bone Research – volume: 282 start-page: 2405 year: 2007b end-page: 2422 article-title: Expression and functional characterization of the cancer‐related serine protease, human tissue kallikrein 14 publication-title: J Biol Chem – volume: 111 start-page: 2518 year: 2014 end-page: 2523 article-title: Design of ultrasensitive probes for human neutrophil elastase through hybrid combinatorial substrate library profiling publication-title: Proc Natl Acad Sci USA – volume: 73 start-page: 657 year: 2013 end-page: 667 article-title: Midkine is associated with neuroendocrine differentiation in castration‐resistant prostate cancer publication-title: Prostate – volume: 144 start-page: 1109 year: 2018 end-page: 1118 article-title: Advanced high‐grade serous ovarian cancer: inverse association of KLK13 and KLK14 mRNA levels in tumor tissue and patients' prognosis publication-title: J Cancer Res Clin Oncol – volume: 30 start-page: 523 year: 2014 end-page: 530 article-title: Causal analysis approaches in ingenuity pathway analysis publication-title: Bioinformatics – volume: 2012 year: 2012 article-title: MAP kinases and prostate cancer publication-title: J Signal Transduct – volume: 92 start-page: 1546 year: 2010 end-page: 1567 article-title: Natural and synthetic inhibitors of kallikrein‐related peptidases (KLKs) publication-title: Biochimie – volume: 31 start-page: 407 year: 2010 end-page: 446 article-title: Kallikreins on steroids: structure, function, and hormonal regulation of prostate‐specific antigen and the extended kallikrein locus publication-title: Endocr Rev – volume: 17 start-page: 651 year: 2017 article-title: The outcome of prostate cancer patients treated with curative intent strongly depends on survival after metastatic progression publication-title: BMC Cancer – volume: 104 start-page: 1920 year: 2011 end-page: 1928 article-title: Upregulation of MAPK pathway is associated with survival in castrate‐resistant prostate cancer publication-title: Br J Cancer – volume: 290 start-page: 26103 year: 2015 end-page: 26113 article-title: Syndecan‐1 and syndecan‐4 capture epidermal growth factor receptor family members and the alpha3beta1 integrin via binding sites in their ectodomains: novel synstatins prevent kinase capture and inhibit alpha6beta4‐integrin‐dependent epithelial cell motILITY publication-title: J Biol Chem – volume: 7 start-page: 64 year: 2007 article-title: Gene expression profiles of prostate cancer reveal involvement of multiple molecular pathways in the metastatic process publication-title: BMC Cancer – volume: 393 start-page: 331 year: 2012 end-page: 341 article-title: Non‐combinatorial library screening reveals subsite cooperativity and identifies new high‐efficiency substrates for kallikrein‐related peptidase 14 publication-title: Biol Chem – volume: 18 start-page: 11 year: 2010 end-page: 22 article-title: Integrative genomic profiling of human prostate cancer publication-title: Cancer Cell – volume: 137 start-page: 430 year: 2017 end-page: 439 article-title: Selective substrates and inhibitors for kallikrein‐related peptidase 7 (KLK7) shed light on KLK proteolytic activity in the stratum corneum publication-title: J Invest Dermatol – volume: 354 start-page: 299 year: 2017 end-page: 309 article-title: Inhibition of midkine suppresses prostate cancer CD133(+) stem cell growth and migration publication-title: Am J Med Sci – volume: 9 start-page: 483 year: 2018 article-title: Heparan sulfate and heparan sulfate proteoglycans in cancer initiation and progression publication-title: Front Endocrinol (Lausanne) – volume: 7 start-page: 11501 year: 2017 article-title: Semaphorin 3 C drives epithelial‐to‐mesenchymal transition, invasiveness, and stem‐like characteristics in prostate cells publication-title: Sci Rep – volume: 31 start-page: 175 year: 2019 end-page: 182 article-title: Targeting the androgen receptor and overcoming resistance in prostate cancer publication-title: Curr Opin Oncol – volume: 11 start-page: dmm033100 year: 2018 article-title: Metastasis in context: modeling the tumor microenvironment with cancer‐on‐a‐chip approaches publication-title: Dis Model Mech – volume: 73 start-page: 117 year: 2001 end-page: 122 article-title: Identification and characterization of KLK14, a novel kallikrein serine protease gene located on human chromosome 19q13.4 and expressed in prostate and skeletal muscle publication-title: Genomics – volume: 1 start-page: 6 year: 2008 article-title: Midkine is a NF‐kappaB‐inducible gene that supports prostate cancer cell survival publication-title: BMC Med Genomics – volume: 122 start-page: 283 year: 2016 end-page: 299 article-title: The kallikrein‐related peptidase family: dysregulation and functions during cancer progression publication-title: Biochimie – volume: 211 start-page: 499 year: 2014 end-page: 513 article-title: Transgenic kallikrein 5 mice reproduce major cutaneous and systemic hallmarks of Netherton syndrome publication-title: J Exp Med – volume: 2011 start-page: 249290 year: 2011 article-title: Metastasis update: human prostate carcinoma invasion via tubulogenesis publication-title: Prostate Cancer – volume: 7 start-page: 800 year: 2007 end-page: 808 article-title: Emerging roles of proteases in tumour suppression publication-title: Nat Rev Cancer – volume: 6 start-page: 1 year: 2004 end-page: 6 article-title: ONCOMINE: a cancer microarray database and integrated data‐mining platform publication-title: Neoplasia – year: 2019 article-title: The multifaceted roles of tumor‐associated proteases and harnessing their activity for prodrug activation publication-title: Biol Chem – volume: 12 start-page: 401 year: 2018 end-page: 416 article-title: New insights into the formation and the function of lamellipodia and ruffles in mesenchymal cell migration publication-title: Cell Adh Migr – volume: 119 start-page: 1 year: 2018 end-page: 9 article-title: Kallikrein‐related peptidases 4, 5, 6 and 7 regulate tumour‐associated factors in serous ovarian cancer publication-title: Br J Cancer – volume: 73 start-page: 1281 year: 2013 end-page: 1290 article-title: Knockdown of lipocalin‐2 suppresses the growth and invasion of prostate cancer cells publication-title: Prostate – volume: 109 start-page: 716 year: 2013 end-page: 725 article-title: Parallel overexpression and clinical significance of kallikrein‐related peptidases 7 and 14 (KLK7KLK14) in colon cancer publication-title: Thromb Haemost – volume: 393 start-page: 403 year: 2012 end-page: 412 article-title: The kallikrein 14 gene is down‐regulated by androgen receptor signalling and harbours genetic variation that is associated with prostate tumour aggressiveness publication-title: Biol Chem – volume: 57 start-page: 1737 year: 2019 end-page: 1743 article-title: Screening of chemical libraries in pursuit of kallikrein‐5 specific inhibitors for the treatment of inflammatory dermatoses publication-title: Clin Chem Lab Med – ident: e_1_2_10_16_1 doi: 10.1515/cclm-2019-0123 – ident: e_1_2_10_22_1 doi: 10.1084/jem.20131797 – ident: e_1_2_10_17_1 doi: 10.1002/pros.22978 – ident: e_1_2_10_54_1 doi: 10.1016/j.ccr.2010.05.026 – ident: e_1_2_10_48_1 doi: 10.1155/2012/169170 – ident: e_1_2_10_19_1 doi: 10.1097/CCO.0000000000000520 – ident: e_1_2_10_23_1 doi: 10.1371/journal.pgen.1005389 – ident: e_1_2_10_6_1 doi: 10.1074/jbc.M608348200 – ident: e_1_2_10_20_1 doi: 10.1016/j.amjms.2017.04.019 – ident: e_1_2_10_46_1 doi: 10.1515/hsz-2016-0163 – ident: e_1_2_10_24_1 doi: 10.1016/j.biochi.2010.06.022 – ident: e_1_2_10_42_1 doi: 10.1002/pros.22607 – ident: e_1_2_10_15_1 doi: 10.1160/TH12-07-0518 – ident: e_1_2_10_5_1 doi: 10.1515/BC.2007.124 – ident: e_1_2_10_30_1 doi: 10.1093/bioinformatics/btt703 – ident: e_1_2_10_14_1 doi: 10.1007/s00432-018-2623-7 – ident: e_1_2_10_56_1 doi: 10.1515/hsz-2018-0451 – ident: e_1_2_10_35_1 doi: 10.1038/nrc2228 – ident: e_1_2_10_59_1 doi: 10.1038/s41598-017-15415-4 – ident: e_1_2_10_44_1 doi: 10.1159/000132565 – ident: e_1_2_10_18_1 doi: 10.18632/oncotarget.11790 – ident: e_1_2_10_32_1 doi: 10.1210/er.2009-0034 – ident: e_1_2_10_51_1 doi: 10.1038/onc.2015.127 – ident: e_1_2_10_26_1 doi: 10.1006/geno.2000.6490 – ident: e_1_2_10_41_1 doi: 10.1155/2011/249290 – volume: 12 start-page: 401 year: 2018 ident: e_1_2_10_27_1 article-title: New insights into the formation and the function of lamellipodia and ruffles in mesenchymal cell migration publication-title: Cell Adh Migr contributor: fullname: Innocenti M – ident: e_1_2_10_11_1 doi: 10.3390/cancers9060067 – ident: e_1_2_10_50_1 doi: 10.1038/ng.629 – ident: e_1_2_10_39_1 doi: 10.1074/mcp.RA118.001304 – ident: e_1_2_10_7_1 doi: 10.1038/ncomms7184 – ident: e_1_2_10_47_1 doi: 10.1016/S1476-5586(04)80047-2 – ident: e_1_2_10_29_1 doi: 10.1038/nprot.2011.382 – ident: e_1_2_10_58_1 doi: 10.1038/s41416-018-0260-1 – ident: e_1_2_10_4_1 doi: 10.1038/s41413-019-0049-8 – ident: e_1_2_10_33_1 doi: 10.18632/oncotarget.3743 – ident: e_1_2_10_53_1 doi: 10.1038/s41598-017-11914-6 – ident: e_1_2_10_62_1 doi: 10.1002/pros.10263 – ident: e_1_2_10_13_1 doi: 10.1515/bc-2011-250 – ident: e_1_2_10_21_1 doi: 10.3109/10408363.2016.1154643 – ident: e_1_2_10_55_1 doi: 10.1002/pros.22670 – ident: e_1_2_10_57_1 doi: 10.1074/jbc.M115.679084 – ident: e_1_2_10_60_1 doi: 10.1074/jbc.M705190200 – ident: e_1_2_10_25_1 doi: 10.1038/nature11125 – volume: 63 start-page: 2665 year: 2003 ident: e_1_2_10_63_1 article-title: EWI2/PGRL associates with the metastasis suppressor KAI1/CD82 and inhibits the migration of prostate cancer cells publication-title: Cancer Res contributor: fullname: Zhang XA – ident: e_1_2_10_37_1 doi: 10.1016/j.cell.2009.02.034 – ident: e_1_2_10_40_1 doi: 10.3389/fendo.2018.00483 – ident: e_1_2_10_28_1 doi: 10.1073/pnas.1318548111 – ident: e_1_2_10_10_1 doi: 10.1515/bc-2011-231 – ident: e_1_2_10_49_1 doi: 10.1093/annonc/mdy082 – ident: e_1_2_10_38_1 doi: 10.1038/bjc.2011.163 – ident: e_1_2_10_43_1 doi: 10.1186/s12885-017-3617-6 – ident: e_1_2_10_12_1 doi: 10.1016/j.jid.2016.09.017 – ident: e_1_2_10_31_1 doi: 10.1016/j.biochi.2015.09.002 – ident: e_1_2_10_36_1 doi: 10.1515/hsz-2011-0268 – ident: e_1_2_10_45_1 doi: 10.2108/zsj.24.774 – ident: e_1_2_10_61_1 doi: 10.1186/1755-8794-1-6 – ident: e_1_2_10_3_1 doi: 10.1016/j.ccell.2017.09.003 – ident: e_1_2_10_52_1 doi: 10.1242/dmm.033100 – ident: e_1_2_10_34_1 doi: 10.1016/j.biomaterials.2018.10.014 – ident: e_1_2_10_2_1 doi: 10.1371/journal.pone.0098786 – ident: e_1_2_10_8_1 doi: 10.1186/1471-2407-7-64 – ident: e_1_2_10_9_1 doi: 10.1158/1940-6207.CAPR-12-0293-T |
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| Snippet | Kallikrein‐related peptidase 14 (KLK14) is one of the several secreted KLK serine proteases involved in prostate cancer (PCa) pathogenesis. While relatively... Kallikrein-related peptidase 14 (KLK14) is one of the several secreted KLK serine proteases involved in prostate cancer (PCa) pathogenesis. While relatively... |
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| SubjectTerms | Agrin Analysis Androgens Antigens Antimitotic agents Antineoplastic agents Cancer therapies castrate‐resistant prostate cancer Cell Line, Tumor Cell Movement - genetics Cell Proliferation - genetics Chromatography, High Pressure Liquid Databases, Genetic Down-Regulation Ethylenediaminetetraacetic acid Experiments Gene expression Gene Expression Regulation, Neoplastic - genetics Genomes Humans Immunohistochemistry Interleukin 1 Kallikrein Kallikreins - genetics Kallikreins - metabolism kallikrein‐related peptidase Kinases Male Metastases Metastasis Midkine Molecular modelling Neoadjuvant Therapy Neoplasm Metastasis - genetics Patients Peptidase Prostate cancer Prostatic Neoplasms - enzymology Prostatic Neoplasms - genetics Prostatic Neoplasms - metabolism Prostatic Neoplasms - pathology protease protease‐substrate Protein kinase Protein kinases Proteins Proteomics Scientific equipment and supplies industry Serine Signal Transduction - genetics Tandem Mass Spectrometry Transcriptome Tumor Microenvironment - genetics Tumors Up-Regulation Vitronectin |
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| Title | The molecular function of kallikrein‐related peptidase 14 demonstrates a key modulatory role in advanced prostate cancer |
| URI | https://onlinelibrary.wiley.com/doi/abs/10.1002%2F1878-0261.12587 https://www.ncbi.nlm.nih.gov/pubmed/31630475 https://www.proquest.com/docview/2333583339 https://search.proquest.com/docview/2307395483 https://pubmed.ncbi.nlm.nih.gov/PMC6944120 https://doaj.org/article/d544b520f038431180fefe9421c7d971 |
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