Protein Kinase D1, Reduced in Human Pancreatic Tumors, Increases Secretion of Small Extracellular Vesicles From Cancer Cells That Promote Metastasis to Lung in Mice.


Journal

Gastroenterology
ISSN: 1528-0012
Titre abrégé: Gastroenterology
Pays: United States
ID NLM: 0374630

Informations de publication

Date de publication:
09 2020
Historique:
received: 26 08 2019
revised: 21 04 2020
accepted: 13 05 2020
pubmed: 25 5 2020
medline: 16 4 2021
entrez: 25 5 2020
Statut: ppublish

Résumé

Pancreatic tumor cells release small extracellular vesicles (sEVs, exosomes) that contain lipids and proteins, RNA, and DNA molecules that might promote formation of metastases. It is not clear what cargo these vesicles contain and how they are released. Protein kinase D1 (PRKD1) inhibits cell motility and is believed to be dysregulated in pancreatic ductal adenocarcinomas. We investigated whether it regulates production of sEVs in pancreatic cancer cells and their ability to form premetastatic niches for pancreatic cancer cells in mice. We analyzed data from UALCAN and human pancreatic tissue microarrays to compare levels of PRKD1 between tumor and nontumor tissues. We studied mice with pancreas-specific disruption of Prkd1 (PRKD1 Levels of PRKD1 were reduced in human pancreatic ductal adenocarcinoma tissues compared with nontumor tissues. PRKD1 Human pancreatic ductal adenocarcinoma has reduced levels of PRKD1 compared with nontumor pancreatic tissues. Loss of PRKD1 results in reduced phosphorylation of cortactin in pancreatic cancer cell lines, resulting in increased in F-actin at the plasma membrane and increased release of sEVs, with altered content. These sEVs promote metastasis of xenograft and pancreatic tumors to lung in mice.

Sections du résumé

BACKGROUND & AIMS
Pancreatic tumor cells release small extracellular vesicles (sEVs, exosomes) that contain lipids and proteins, RNA, and DNA molecules that might promote formation of metastases. It is not clear what cargo these vesicles contain and how they are released. Protein kinase D1 (PRKD1) inhibits cell motility and is believed to be dysregulated in pancreatic ductal adenocarcinomas. We investigated whether it regulates production of sEVs in pancreatic cancer cells and their ability to form premetastatic niches for pancreatic cancer cells in mice.
METHODS
We analyzed data from UALCAN and human pancreatic tissue microarrays to compare levels of PRKD1 between tumor and nontumor tissues. We studied mice with pancreas-specific disruption of Prkd1 (PRKD1
RESULTS
Levels of PRKD1 were reduced in human pancreatic ductal adenocarcinoma tissues compared with nontumor tissues. PRKD1
CONCLUSIONS
Human pancreatic ductal adenocarcinoma has reduced levels of PRKD1 compared with nontumor pancreatic tissues. Loss of PRKD1 results in reduced phosphorylation of cortactin in pancreatic cancer cell lines, resulting in increased in F-actin at the plasma membrane and increased release of sEVs, with altered content. These sEVs promote metastasis of xenograft and pancreatic tumors to lung in mice.

Identifiants

pubmed: 32446697
pii: S0016-5085(20)34705-3
doi: 10.1053/j.gastro.2020.05.052
pii:
doi:

Substances chimiques

protein kinase D EC 2.7.10.-
Protein Kinase C EC 2.7.11.13

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1019-1035.e22

Informations de copyright

Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.

Auteurs

Milena Armacki (M)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

Sandra Polaschek (S)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

Mareike Waldenmaier (M)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

Mareen Morawe (M)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

Claudia Ruhland (C)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

Rebecca Schmid (R)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

André Lechel (A)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

Umesh Tharehalli (U)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

Christoph Steup (C)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

Yasin Bektas (Y)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

Hongxia Li (H)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany.

Johann M Kraus (JM)

Institute of Medical Systems Biology, Ulm University, Ulm, Germany.

Hans A Kestler (HA)

Institute of Medical Systems Biology, Ulm University, Ulm, Germany.

Stephan Kruger (S)

Department of Medicine III, University Hospital, Ludwig Maximilian University of Munich, Munich, Germany.

Steffen Ormanns (S)

Institute of Pathology, Faculty of Medicine, Ludwig Maximilian University of Munich, Munich, Germany.

Paul Walther (P)

Central Facility for Electron Microscopy, University of Ulm, Ulm, Germany.

Tim Eiseler (T)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany. Electronic address: thomas.seufferlein@uniklinik-ulm.de.

Thomas Seufferlein (T)

Department of Internal Medicine I, University Hospital Ulm, Ulm, Germany. Electronic address: thomas.seufferlein@uniklinik-ulm.de.

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Classifications MeSH