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Annexins in Cell Biology, Biotechnology and Medicine
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Annexins in Cell Biology, Biotechnology and Medicine

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: closed (30 September 2020) | Viewed by 9768

Special Issue Editors

Prof. Dr. Slawomir Pikula

E-Mail Website
Guest Editor
Laboratory of Biochemistry of Lipids, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Str., 02-093 Warsaw, Poland
Interests: calcium homeostasis and transport; roles of annexins in the mineralization processes
Special Issues, Collections and Topics in MDPI journals
Dr. Joanna Bandorowicz-Pikula

E-Mail Website
Guest Editor
Laboratory of Cellular Metabolism, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Str., 02-093 Warsaw, Poland
Interests: Annexins; Endothelial dysfunction; Cholesterol metabolism; Rare diseases

Special Issue Information

Dear Colleagues,

The Special Issue of International Journal of Molecular Sciences is dedicated to annexins, a ubiquitous family of homologous, multifunctional calcium and membrane binding proteins. The first annexin identified more than 40 years ago by the group of Professor Harvey B. Pollard as synexin (annexin A7) from adrenal medulla, stimulating calcium-dependent aggregation of isolated chromaffin granules, turned out to be a member of the large family of proteins widely expressed in Eukaryotes but also found in Prokaryotes.

Accumulating evidence for the last four decades strongly suggests that annexins are implicated in the calcium-controlled regulation of a broad range of membrane events, including vesicular transport, changes of membrane structure, lateral organization of membrane constituents, signal transduction pathways, virus infection, and many more, both in norm and pathology. In addition, many annexin-related diseases, called annexinopathies, have been identified and described, such as cancer and autoimmune disorders, revealing a pivotal role of certain annexins in such processes as calcium and cholesterol homeostasis, inflammatory and immunological responses, fetal development, bacterial invasion, biomineralization, and so on. Moreover, further advances in the field of annexins point to their potential role as important therapeutic targets for many diseases. Thus, an understanding of annexin functions at molecular, cellular, and organismal levels is crucial for uncovering molecular mechanisms of vital cellular processes in the fields of biotechnology and medicine.

In summary, this Special Issue, “Annexins”, welcomes contributions in all areas of recent and current research associated with physiological and pathological functions of the calcium and membrane binding proteins, annexins.

Prof. Dr. Slawomir Pikula
Dr. Joanna Bandorowicz-Pikula
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • annexins
  • membrane traffic
  • cholesterol metabolism
  • membrane microdomains
  • biomineralization
  • markers of diseases
  • annexinopathies

Published Papers (2 papers)

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Research

16 pages, 4331 KiB  
Article
Localization of Annexin A6 in Matrix Vesicles During Physiological Mineralization
by Ekeveliny Amabile Veschi, Maytê Bolean, Agnieszka Strzelecka-Kiliszek, Joanna Bandorowicz-Pikula, Slawomir Pikula, Thierry Granjon, Saida Mebarek, David Magne, Ana Paula Ramos, Nicola Rosato, José Luis Millán, Rene Buchet, Massimo Bottini and Pietro Ciancaglini
Int. J. Mol. Sci. 2020, 21(4), 1367; https://doi.org/10.3390/ijms21041367 - 18 Feb 2020
Cited by 19 | Viewed by 3216
Abstract
Annexin A6 (AnxA6) is the largest member of the annexin family of proteins present in matrix vesicles (MVs). MVs are a special class of extracellular vesicles that serve as a nucleation site during cartilage, bone, and mantle dentin mineralization. In this study, we [...] Read more.
Annexin A6 (AnxA6) is the largest member of the annexin family of proteins present in matrix vesicles (MVs). MVs are a special class of extracellular vesicles that serve as a nucleation site during cartilage, bone, and mantle dentin mineralization. In this study, we assessed the localization of AnxA6 in the MV membrane bilayer using native MVs and MV biomimetics. Biochemical analyses revealed that AnxA6 in MVs can be divided into three distinct groups. The first group corresponds to Ca2+-bound AnxA6 interacting with the inner leaflet of the MV membrane. The second group corresponds to AnxA6 localized on the surface of the outer leaflet. The third group corresponds to AnxA6 inserted in the membrane’s hydrophobic bilayer and co-localized with cholesterol (Chol). Using monolayers and proteoliposomes composed of either dipalmitoylphosphatidylcholine (DPPC) to mimic the outer leaflet of the MV membrane bilayer or a 9:1 DPPC:dipalmitoylphosphatidylserine (DPPS) mixture to mimic the inner leaflet, with and without Ca2+, we confirmed that, in agreement with the biochemical data, AnxA6 interacted differently with the MV membrane. Thermodynamic analyses based on the measurement of surface pressure exclusion (πexc), enthalpy (ΔH), and phase transition cooperativity (Δt1/2) showed that AnxA6 interacted with DPPC and 9:1 DPPC:DPPS systems and that this interaction increased in the presence of Chol. The selective recruitment of AnxA6 by Chol was observed in MVs as probed by the addition of methyl-β-cyclodextrin (MβCD). AnxA6-lipid interaction was also Ca2+-dependent, as evidenced by the increase in πexc in negatively charged 9:1 DPPC:DPPS monolayers and the decrease in ΔH in 9:1 DPPC:DPPS proteoliposomes caused by the addition of AnxA6 in the presence of Ca2+ compared to DPPC zwitterionic bilayers. The interaction of AnxA6 with DPPC and 9:1 DPPC:DPPS systems was distinct even in the absence of Ca2+ as observed by the larger change in Δt1/2 in 9:1 DPPC:DPPS vesicles as compared to DPPC vesicles. Protrusions on the surface of DPPC proteoliposomes observed by atomic force microscopy suggested that oligomeric AnxA6 interacted with the vesicle membrane. Further work is needed to delineate possible functions of AnxA6 at its different localizations and ways of interaction with lipids. Full article
(This article belongs to the Special Issue Annexins in Cell Biology, Biotechnology and Medicine)
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11 pages, 2158 KiB  
Article
Triple-Negative Breast Cancer with High Levels of Annexin A1 Expression Is Associated with Mast Cell Infiltration, Inflammation, and Angiogenesis
by Maiko Okano, Masanori Oshi, Ali Linsk Butash, Eriko Katsuta, Kazunoshin Tachibana, Katsuharu Saito, Hirokazu Okayama, Xuan Peng, Li Yan, Koji Kono, Toru Ohtake and Kazuaki Takabe
Int. J. Mol. Sci. 2019, 20(17), 4197; https://doi.org/10.3390/ijms20174197 - 27 Aug 2019
Cited by 75 | Viewed by 6137
Abstract
Annexin A1 (ANXA1) is a phospholipid-linked protein involved in inflammation, immune response, and mast cell reactivity. Recently, we reported that ANXA1 is associated with aggressive features of triple-negative breast cancer (TNBC); however, its clinical relevance remains controversial. We hypothesized that human TNBC with [...] Read more.
Annexin A1 (ANXA1) is a phospholipid-linked protein involved in inflammation, immune response, and mast cell reactivity. Recently, we reported that ANXA1 is associated with aggressive features of triple-negative breast cancer (TNBC); however, its clinical relevance remains controversial. We hypothesized that human TNBC with high expression of ANXA1 mRNA is associated with pro-cancerous immune cell infiltration, including mast cells, and with an aggressive phenotype. Clinical and RNA-seq data were obtained from The Cancer Genome Atlas (TCGA, n = 1079) and Molecular Taxonomy of Breast Cancer International Consortium (METABRIC) (n = 1904). TNBC patients had significantly higher levels of ANXA1 expression compared to the other subtypes in both TCGA and METABRIC cohorts (p < 0.001). ANXA1 protein expression was assessed by immunohistochemistry in Japanese TNBC patient cohort (n = 48), where 17 cases (35.4%) had positive ANXA1 staining, and their overall survival was significantly shorter compared with negative staining group (p = 0.008). The CIBERSORT algorithm was used to calculate immune cell infiltrations. ANXA1 high tumors were associated with activated mast cells and M2 macrophages (p > 0.01), but did not show any association with tumor heterogeneity nor cytolytic activity. High expression of ANXA1 group enriched inflammation, epithelial-to-mesenchymal transition (EMT), and angiogenesis-related genes in a gene set enrichment assay in both cohorts. To our knowledge, this is the first study to demonstrate that ANXA1 is associated with infiltration of mast cells and inflammation that is associated with the aggressive phenotype of TNBC, such as EMT and angiogenesis. Full article
(This article belongs to the Special Issue Annexins in Cell Biology, Biotechnology and Medicine)
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