Defects in the Transport Mechanism of Membrane Proteins and Related Diseases
A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Cellular Biochemistry".
Deadline for manuscript submissions: 31 July 2024 | Viewed by 4154
Special Issue Editor
Interests: structure/function relationship; transport mechanism; mitochondrial transport proteins; mitochondrial carrier diseases; mitochondrial carrier identification; design, synthesis and biological evaluation of new drugs against neurodegenerative diseases
Special Issue Information
Dear Colleagues,
Membrane transport proteins play crucial roles across biological membranes and participate in cell physiology; metabolism and signaling; maintaining cellular homeostasis; and permitting the translocation of many classes of metabolites (i.e. sugar, amino acids, lipids, vitamins, inorganic ions and others). These proteins are essential for cellular functions ensuring cell survival in response to frequent stimuli of intracellular or environmental stress. Indeed, the transport mechanism exerted by membrane transport proteins, generating concentration gradients via active transport mechanisms, passive diffusion and ion channels, contributes to the regulation of biochemical pathways through correct cellular concentrations of substrates and products. Therefore, genetic mutations or the impairment of these transport systems could result in defects on transport mechanism with changes in the expression, activity and structure of proteins, which are manifested in different groups of neurodegenerative and metabolic diseases.
Hence, the purpose of this Special Issue “Defects in the Transport Mechanism of Membrane Proteins and Related Diseases" is to integrate current knowledge regarding physiological functions and the mechanisms of transport of a wide group of membrane transport proteins underlying their involvements in the initiation and progression of many diseases. Research papers and review manuscripts depicting a special focus on membrane transporters are cordially invited. Short communications will also be taken into consideration.
Dr. Daniela Valeria Miniero
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.
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Keywords
- function, structure and folding of membrane transport proteins
- pathological mutations
- mechanism of transport
- neurological and metabolic disease
- transport of nanoparticles
- organelle membranes
- cellular function and signaling
- bioenergetics
- neuroinflammation
- nanoformulations for drug targets
Planned Papers
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: Theoretical and experimental insights into the Inhibition of Purified Rat Brain 2-Oxoglutarate Carrier by Hemin
Authors: Daniela Valeria Miniero
Affiliation: University of Bari - Department of Biosciences, Biotechnologies and Biopharmaceutics Via Orabona 4 Bari-Italy
Abstract: A new kinetic analysis of the transport assays of the purified Rat Brain 2-Oxoglutarate carrier was performed starting from the results showing a competitive inhibitory behaviour of hemin, a phys-iological porphirine derivative, on the 2-oxoglutarate/malate antiport, catalyzed by the mito-chondrial 2-oxoglutarate carrier, isolated from rat brain mitochondria and reconstituted in an active form into proteoliposomes. In the light of the new elaboration of the kinetic equation, the data clearly support the hypothesis that hemin shows a partially competitive inhibition, instead of a pure competitive inhibition, with the formation of a ternary complex consisting of “he-min-carrier-substrate”. A possible interpretation of the provided kinetic analysis was also supported by computational studies, allowing to propose a regulation binding region located on OGC mito-chondrial matrix loops, where hemin can establish interactions with residues involved in the sub-strate recognition and/or conformational changes responsible for the translocation of mitochondrial carrier substrates. Such regulation site is placed about 10 Å from the binding site and enables the simultaneous binding of hemin and 2-oxoglutarate or malate within the carrier. Overall, the ex-perimental and computational analysis helped to shed light on the possible structure of the proposed “hemin-carrier-substrate complex”.
Title: To be confirmed
Authors: Nancy J. Philp
Affiliation: Department of Pharmacology and Experimental Therapeutics, Sydney Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, United States