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Pancreatic Neoplasms: HELP
Articles by Oakley C. Olson
Based on 2 articles published since 2010
(Why 2 articles?)
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Between 2010 and 2020, Oakley C. Olson wrote the following 2 articles about Pancreatic Neoplasms.
 
+ Citations + Abstracts
1 Article Inflammatory Monocytes Promote Perineural Invasion via CCL2-Mediated Recruitment and Cathepsin B Expression. 2017

Bakst, Richard L / Xiong, Huizhong / Chen, Chun-Hao / Deborde, Sylvie / Lyubchik, Anna / Zhou, Yi / He, Shizhi / McNamara, William / Lee, Sei-Young / Olson, Oakley C / Leiner, Ingrid M / Marcadis, Andrea R / Keith, James W / Al-Ahmadie, Hikmat A / Katabi, Nora / Gil, Ziv / Vakiani, Efsevia / Joyce, Johanna A / Pamer, Eric / Wong, Richard J. ·Department of Radiation Oncology, Mount Sinai School of Medicine, New York, New York. · Immunology Program, Memorial Sloan-Kettering Cancer Center, New York, New York. · Department of Surgery, Memorial Sloan-Kettering Cancer Center, New York, New York. · Cancer Biology and Genetics Program, Memorial Sloan Kettering Cancer Center, New York, New York. · Department of Pathology, Memorial Sloan Kettering Cancer Center, New York, New York. · Department of Otolaryngology, Rambam Healthcare Campus, The Technion-Israel Institute of Technology, Haifa, Israel. · Ludwig Institute for Cancer Research, University of Lausanne, Lausanne, Switzerland. · Department of Surgery, Memorial Sloan-Kettering Cancer Center, New York, New York. wongr@mskcc.org. ·Cancer Res · Pubmed #28951461.

ABSTRACT: Perineural invasion (PNI) is an ominous event strongly linked to poor clinical outcome. Cells residing within peripheral nerves collaborate with cancer cells to enable PNI, but the contributing conditions within the tumor microenvironment are not well understood. Here, we show that CCR2-expressing inflammatory monocytes (IM) are preferentially recruited to sites of PNI, where they differentiate into macrophages and potentiate nerve invasion through a cathepsin B-mediated process. A series of adoptive transfer experiments with genetically engineered donors and recipients demonstrated that IM recruitment to nerves was driven by CCL2 released from Schwann cells at the site of PNI, but not CCL7, an alternate ligand for CCR2. Interruption of either CCL2-CCR2 signaling or cathepsin B function significantly impaired PNI

2 Article TAILS N-Terminomics and Proteomics Show Protein Degradation Dominates over Proteolytic Processing by Cathepsins in Pancreatic Tumors. 2016

Prudova, Anna / Gocheva, Vasilena / Auf dem Keller, Ulrich / Eckhard, Ulrich / Olson, Oakley C / Akkari, Leila / Butler, Georgina S / Fortelny, Nikolaus / Lange, Philipp F / Mark, Jennifer C / Joyce, Johanna A / Overall, Christopher M. ·Centre for Blood Research, Life Sciences Institute and Faculty of Dentistry, Department of Oral Biological and Medical Sciences, University of British Columbia, Vancouver, BC V6T 1Z3, Canada. · Cancer Biology and Genetics Program, Memorial Sloan Kettering Cancer Center, New York City, NY 10021, USA. · Ludwig Institute for Cancer Research, 1066 Lausanne, Switzerland; Department of Oncology, University of Lausanne, 1066 Lausanne, Switzerland. · Cancer Biology and Genetics Program, Memorial Sloan Kettering Cancer Center, New York City, NY 10021, USA; Ludwig Institute for Cancer Research, 1066 Lausanne, Switzerland; Department of Oncology, University of Lausanne, 1066 Lausanne, Switzerland. Electronic address: johanna@joycelab.org. · Centre for Blood Research, Life Sciences Institute and Faculty of Dentistry, Department of Oral Biological and Medical Sciences, University of British Columbia, Vancouver, BC V6T 1Z3, Canada. Electronic address: chris.overall@ubc.ca. ·Cell Rep · Pubmed #27477282.

ABSTRACT: Deregulated cathepsin proteolysis occurs across numerous cancers, but in vivo substrates mediating tumorigenesis remain ill-defined. Applying 8-plex iTRAQ terminal amine isotopic labeling of substrates (TAILS), a systems-level N-terminome degradomics approach, we identified cathepsin B, H, L, S, and Z in vivo substrates and cleavage sites with the use of six different cathepsin knockout genotypes in the Rip1-Tag2 mouse model of pancreatic neuroendocrine tumorigenesis. Among 1,935 proteins and 1,114 N termini identified by TAILS, stable proteolytic products were identified in wild-type tumors compared with one or more different cathepsin knockouts (17%-44% of 139 cleavages). This suggests a lack of compensation at the substrate level by other cathepsins. The majority of neo-N termini (56%-83%) for all cathepsins was consistent with protein degradation. We validated substrates, including the glycolytic enzyme pyruvate kinase M2 associated with the Warburg effect, the ER chaperone GRP78, and the oncoprotein prothymosin-alpha. Thus, the identification of cathepsin substrates in tumorigenesis improves the understanding of cathepsin functions in normal physiology and cancer.