Special Issue "Lectins: From Basic Science to Application for Glycobiology, Cell Biology, and Medicine"
Deadline for manuscript submissions: 28 February 2018
Dr. Hiroaki Tateno
Department of Life Science and Biotechnology, National Institute of Advanced Industrial Science and Technology (AIST), Central 2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, Japan
Website | E-Mail
Interests: lectins; glycans, stem cells; regenerative medicine; drug discovery; diagnosis; exosome; cancer stem cells
It is our great pleasure to inform you that a Special Issue on “Lectins: From Basic Science to Application for Glycobiology, Cell Biology, and Medicine” will be published in the journal Molecules. Lectins are carbohydrate-binding proteins, which recognize the specific carbohydrate structures expressed on cells and mediate various physiological and pathological phenomenon through cell-cell and host-pathogen communications. Lectins are useful as research tools for glycomic analysis, and cell identification/separation. They were also demonstrated to be applied as cargo to deliver drugs inside cells, such as stem cells and tumor cells.
In this Special Issue, we focused on lectins from basics to applications for glycobiology, cell biology, and medicine.
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 papers will be 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. Molecules is an international peer-reviewed open access monthly journal published by MDPI.
Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). 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.
- cell recognition
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title: Galectin-1 in cardiovascular disease: from bench to bedside
Authors: Ignacio Seropian, Antonio Abbate
Abstract: Galectin-1 (Gal-1) is a prototype beta-galacotoside binding lectin widely expressed. Gal-1 inhibits acute and chronic inflammation, promoting tumor growth and autoimmune diseases. Recent evidence suggests a relevant role of Gal-1 in cardiovascular physiology and disease. Here we review the role of Gal-1 in acute myocardial infarction and heart failure, Chagas’ disease, pulmonary hypertension and stroke. Gal-1 treatment is a promising target for acute myocardial infarction and stroke, while Gal-1 inhibition may improve pulmonary hypertension.
Article: A lectin inhibits antigen-antibody reaction: Rapid detection of glycan-Isoforms In body fluid and tissues
Article type: Review
Authors: Yasuhiro Hashimoto, Hiromi Ito and Kyoka Hoshi
Abstract: Antibodies are useful tools to detect antigens including glycoproteins. However, they usually recognize a protein portion but not a glycan portion.
Therefore, quantification of each glycoforms of glycoproteins requires time- and labor- consuming processes such as lectin affinity column chromatography coupled with ELISA.
We found that a lectin inhibits antigen-antibody reaction, leading to glycoform-specific assay for glycoproteins (lectin inhibition).
The lectin inhibition assay was applicable to quantification of glycoforms in tissue extracts by ELISA or an automated latex-agglutination immunoassay (auto-analyzer method).
The lectin inhibition also visualizes localization of glycoforms on tissue sections
Title: The double face of mucin-type O-glycans in infection and immunity
Author: Franz-Georg Hanisch
Abstract: Epithelial human blood group antigens (HBGAs) on O-linked mucin-type glycans play roles in pathogen binding and the initiation of infection, while the same or similar structures on soluble secretory mucins exert protective functions. These double-faced features of O-glycans in infection and innate immunity are reviewed based on two instructive examples of bacterial and viral pathogens.
Helicobacter pylori represents one of the major causes for the development of gastric cancer and despite successive eradication in industrialized countries the parasite can be found at frequencies up to 50% of the population. H. pylori co-localizes with the mucin MUC5AC in the surface epithelium of the stomach, but not with MUC6, which is co-secreted with TFF2 by deep gastric glands. Both components of the glandular secretome and are concertedly up-regulated on infection. HBGAs form the basis of both, microbial interaction with the protecting mucin layer via Lewis-type glycans and infection by bacterial adhesion to the epithelium with induction of inflammation. On the other hand, organ-characteristic a-GlcNAc-capped glycans on MUC6 were described as natural antibiotics as they interfere with the formation of a-glucosyl cholesterol, a major cell wall component of H. pylori. Interestingly, gastric glycoforms of TFF2 are active as a calcium-independent, pH-resistant lectin, which binds with high specificity to these antibiotic glycans and could control bacterial growth as a probiotic. Also human noroviruses of the GII genogroup interact via their major capsid protein VP1 with HBGAs. However, certain noroviruses are known to bind poorly to HBGAs, yet still cause infections; some noroviruses interact with numerous HBGA types, but are non-prevalent; and other noroviruses appear to have acquired a taste for HBGAs and seem to be increasing in prevalence. HBGAs and related structures on human milk oligosaccharides (HMOs) can be found as soluble antigens in humans, and may exert protective functions by binding to the P2 domain pocket on the capsid. We discuss blood group H/Lewis-b, polyvalent fucose-dendrimers, and fucoidan-derived oligofucoses as highly effective interactors for noroviruses GII.4 and GII.17 as the most prevalent strains.
Title: Sialic acid-binding lectin from bullfrog eggs exhibits anti-tumor effect against breast cancer cells including triple-negative phenotype cells
Authors: Takeo Tatsuta1, Shoko Sato2, Toshiyuki Sato3, Shigeki Sugawara1, Tsuneyoshi Suzuki2, Akiyoshi Hara3, Masahiro Hosono1
1 Division of Cell Recognition Study, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, Aobaku, Sendai, Japan
2 Department of Pharmaceutical Sciences, Tohoku Medical and Pharmaceutical University, Aobaku, Sendai, Japan
3 Department of Clinical Pharmacotherapeutics, Tohoku Medical and Pharmaceutical University, Aobaku, Sendai, Japan
Abstract: Sialic acid-binding lectin from Rana catesbeiana eggs (cSBL) is a multifunctional protein that has lectin and ribonuclease activity. In this study, anti-tumor activities of cSBL were accessed using a panel of breast cancer cell lines. cSBL suppressed the cell growth of all cancer cell lines tested in here at the concentration that does not affect the viability of normal cells. The growth suppressive effect was attributed to the cancer-selective induction of apoptosis. We assessed the expression of several key molecules associated with breast cancer phenotype after cSBL treatment by western blotting. cSBL decreased the expression level of estrogen receptor (ER) while it increased the phosphorylation level of p38 MAPK. cSBL also suppresses the expression of progesterone receptor (PG) and human epidermal growth factor receptor type 2 (HER2/ErbB2). Furthermore, it was revealed that cSBL decreases epidermal growth factor receptor (EGFR/ErbB1) in triple negative breast cancer cells. These results indicate that cSBL induces apoptosis with decreasing ErbB family proteins and may have great potential for breast cancer chemotherapy particularly in triple-negative phenotype cells.