Cancer Proteomics 2018

A special issue of Proteomes (ISSN 2227-7382).

Deadline for manuscript submissions: closed (31 October 2018) | Viewed by 3432

Special Issue Editor

The Brown Foundation Institute of Molecular Medicine, The University of Texas Health Science Center at Houston, Houston, TX, USA
Interests: proteomics; glycoproteomics; PTM characterization; mass spectrometry; pancreatic cancer
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

 Proteomics offers a wide range of opportunities to investigate malignancy-associated molecular alterations at the functional level and has stimulated great interest in applying the technology to study cancers and associated diseases. Malignancy-associated proteome alterations in a biological system, localized or systemic, related to or discrete from genomic mutations, may reflect the profound changes in cellular functions and biological processes at multiple levels. These steady or perturbation-induced proteome alterations may include changes on protein expressional level, sequence, status of post-translational modifications (PTMs), protein interaction networks, and cellular localization. In the past two decades, enormous efforts have been increasingly applied in cancer proteomics, with research goals ranging from mechanistic study to biomarker development, as well as to clinical applications. A variety of cancer and control samples, including cell lines and derivatives, tumor tissues and isolated cells, plasma/serum and other bodily fluids, have been investigated. These studies have laid important foundations for future cancer proteomics studies. With the recent advances in mass spectrometry technology, bioinformatics and knowledgebase, the depth, breadth and robustness of proteomics have been significantly improved. The emerging fields in PTM analysis, proteogenomics, single cell proteomics and spectral library-based proteomics, such as SWATH, carry great potentials for basic, translational and clinical cancer research. We welcomes submissions of original research or review articles aiming at the broad field of cancer research using proteomics approaches.  Prof. Dr. Sheng Pan

Prof. Dr. Sheng Pan
Guest Editor

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Keywords

  • proteomics
  • cancer
  • mass spectrometry
  • post-translational modifications

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Published Papers (1 paper)

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Research

10 pages, 962 KiB  
Communication
Proteomic Profiling of Primary Human Acute Myeloid Leukemia Cells Does Not Reflect Their Constitutive Release of Soluble Mediators
by Elise Aasebø, Maria Hernandez-Valladares, Frode Selheim, Frode S. Berven, Annette K. Brenner and Øystein Bruserud
Proteomes 2019, 7(1), 1; https://doi.org/10.3390/proteomes7010001 - 20 Dec 2018
Cited by 9 | Viewed by 3004
Abstract
Acute myeloid leukemia (AML) is a heterogeneous disease, and communication between leukemic cells and their neighboring leukemia-supporting normal cells is involved in leukemogenesis. The bone marrow cytokine network is therefore important, and the mediator release profile seems more important than single mediators. It [...] Read more.
Acute myeloid leukemia (AML) is a heterogeneous disease, and communication between leukemic cells and their neighboring leukemia-supporting normal cells is involved in leukemogenesis. The bone marrow cytokine network is therefore important, and the mediator release profile seems more important than single mediators. It is not known whether the characterization of primary AML cell proteomes reflects the heterogeneity of the broad and dynamic constitutive mediator release profile by these cells. To address this, we compared the intracellular levels of 41 proteins in 19 AML patients with the constitutive extracellular release during in vitro culture, including chemokines, growth factors, proteases, and protease regulators. The constitutive release of most mediators showed a wide variation (up to 2000-fold differences) between patients. Detectable intracellular levels were seen for 10 of 41 mediators, but for most of these 10 mediators we could not detect significant correlations between the constitutive release during in vitro culture and their intracellular levels. Intracellular protein levels in primary human AML cells do not reflect the dynamics, capacity, and variation between patients in constitutive mediator release profiles. Measurements of these profiles thus add complementary information to proteomic detection/quantification regarding the heterogeneity of the AML cell contributions to the bone marrow cytokine network. Full article
(This article belongs to the Special Issue Cancer Proteomics 2018)
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