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Special Issue Editors

Prof. Dr. Hassan Y. Naim

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Guest Editor

Department of Biochemistry, University of Veterinary Medicine Hannover, Bünteweg 17, 30559 Hannover, Germany
Interests: protein trafficking; protein glycosylation; lipid rafts; gastrointestinal disorders; molecular basis of carbohydrate malabsorption; lysosomal storage diseases

Prof. Dr. Bernd Lepenies

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Guest Editor

Center for Emerging Infections and Zoonoses, Institute for Immunology & Research, University of Veterinary Medicine Hannover, Bünteweg 17, 30559 Hannover, Germany
Interests: infection immunology; innate immunity; glycobiology; C-type lectin receptors; vaccination; adjuvants; targeted antigen delivery
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Glycosylation is an essential, crucial, and critical posttranslational modification in the life cycle of membrane and secretory proteins and membrane lipids. It affects an array of cellular processes, including the folding, trafficking, and sorting of proteins. It influences the binding affinities in protein–protein interactions, regulates protein function, increases protein stability, and protects against proteolytic degradation. Glycans serve as structural components of cell membranes and contribute to cell–cell interactions as well as host–pathogen interactions; they also play a role also in the immune response.

The modulation of glycosylation helps to elucidate the implication of glycoproteins in a variety of cellular mechanisms in health and disease. Considering this, glycosylation modulators can be utilized in biomedical research and as therapeutic tools in clinical medicine.

The scope of this Special Issue is to describe the latest advances in the biosynthesis and processing of glycans, glycoconjugates, and glycoproteins and their implication in the abovementioned crucial roles in (patho)physiology.

Contributions exploring the following topics are particularly encouraged:

Protein folding;
Membrane trafficking;
Protein sorting and polarity;
Protein–protein interactions;
Enzyme functions;
Cell–cell communication;
Host–pathogen interaction;
Immune response;
Novel therapeutic approaches.

This Special Issue particularly welcomes original research articles and brief communications.

Up-to-date reviews on the described topics will be also considered.

We look forward to reading your contributions.

Prof. Dr. Hassan Y. Naim
Prof. Dr. Bernd Lepenies
Guest Editors

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. Biomolecules 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 2700 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.

Keywords

protein folding
membrane trafficking
protein sorting and polarity
protein–protein interactions
host–pathogen interaction
immune response
novel therapeutic approaches

Published Papers (2 papers)

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Research

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29 pages, 6471 KiB

Open AccessArticle

Glycation Interferes with the Activity of the Bi-Functional UDP-N-Acetylglucosamine 2-Epimerase/N-Acetyl-mannosamine Kinase (GNE)

by Vanessa Hagenhaus, Jacob L. Gorenflos López, Rebecca Rosenstengel, Carolin Neu, Christian P. R. Hackenberger, Arif Celik, Klara Weinert, Mai-Binh Nguyen, Kaya Bork, Rüdiger Horstkorte and Astrid Gesper

Biomolecules 2023, 13(3), 422; https://doi.org/10.3390/biom13030422 - 23 Feb 2023

Cited by 1 | Viewed by 2151

Abstract

Mutations in the gene coding for the bi-functional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE), the key enzyme of the sialic acid biosynthesis, are responsible for autosomal-recessive GNE myopathy (GNEM). GNEM is an adult-onset disease with a yet unknown exact pathophysiology. Since the protein appears to work adequately for a certain period of time even though the mutation is already present, other effects appear to influence the onset and progression of the disease. In this study, we want to investigate whether the late onset of GNEM is based on an age-related effect, e.g., the accumulation of post-translational modifications (PTMs). Furthermore, we also want to investigate what effect on the enzyme activity such an accumulation would have. We will particularly focus on glycation, which is a PTM through non-enzymatic reactions between the carbonyl groups (e.g., of methylglyoxal (MGO) or glyoxal (GO)) with amino groups of proteins or other biomolecules. It is already known that the levels of both MGO and GO increase with age. For our investigations, we express each domain of the GNE separately, treat them with one of the glycation agents, and determine their activity. We demonstrate that the enzymatic activity of the N-acetylmannosamine kinase (GNE-kinase domain) decreases dramatically after glycation with MGO or GO—with a remaining activity of 13% ± 5% (5 mM MGO) and 22% ± 4% (5 mM GO). Whereas the activity of the UDP-N-acetylglucosamine 2-epimerase (GNE-epimerase domain) is only slightly reduced after glycation—with a remaining activity of 60% ± 8% (5 mM MGO) and 63% ± 5% (5 mM GO). Full article

(This article belongs to the Special Issue Glycoconjugates in Health, Disease, and Therapy—an Update)

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Review

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12 pages, 782 KiB

Open AccessReview

Protein Targeting to Glycogen (PTG): A Promising Player in Glucose and Lipid Metabolism

by Xia Deng, Chenxi Wang, Yue Xia and Guoyue Yuan

Biomolecules 2022, 12(12), 1755; https://doi.org/10.3390/biom12121755 - 26 Nov 2022

Cited by 2 | Viewed by 2012

Abstract

Protein phosphorylation and dephosphorylation are widely considered to be the key regulatory factors of cell function, and are often referred to as “molecular switches” in the regulation of cell metabolic processes. A large number of studies have shown that the phosphorylation/dephosphorylation of related signal molecules plays a key role in the regulation of liver glucose and lipid metabolism. As a new therapeutic strategy for metabolic diseases, the potential of using inhibitor-based therapies to fight diabetes has gained scientific momentum. PTG, a protein phosphatase, also known as glycogen targeting protein, is a member of the protein phosphatase 1 (PP1) family. It can play a role by catalyzing the dephosphorylation of phosphorylated protein molecules, especially regulating many aspects of glucose and lipid metabolism. In this review, we briefly summarize the role of PTG in glucose and lipid metabolism, and update its role in metabolic regulation, with special attention to glucose homeostasis and lipid metabolism. Full article

(This article belongs to the Special Issue Glycoconjugates in Health, Disease, and Therapy—an Update)

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