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  1. Article ; Online: Exploring the Interplay between Polyphenols and Lysyl Oxidase Enzymes for Maintaining Extracellular Matrix Homeostasis

    Carolina Añazco / Janin Riedelsberger / Lorenzo Vega-Montoto / Armando Rojas

    International Journal of Molecular Sciences, Vol 24, Iss 10985, p

    2023  Volume 10985

    Abstract: Collagen, the most abundant structural protein found in mammals, plays a vital role as a constituent of the extracellular matrix (ECM) that surrounds cells. Collagen fibrils are strengthened through the formation of covalent cross-links, which involve ... ...

    Abstract Collagen, the most abundant structural protein found in mammals, plays a vital role as a constituent of the extracellular matrix (ECM) that surrounds cells. Collagen fibrils are strengthened through the formation of covalent cross-links, which involve complex enzymatic and non-enzymatic reactions. Lysyl oxidase (LOX) is responsible for catalyzing the oxidative deamination of lysine and hydroxylysine residues, resulting in the production of aldehydes, allysine, and hydroxyallysine. These intermediates undergo spontaneous condensation reactions, leading to the formation of immature cross-links, which are the initial step in the development of mature covalent cross-links. Additionally, non-enzymatic glycation contributes to the formation of abnormal cross-linking in collagen fibrils. During glycation, specific lysine and arginine residues in collagen are modified by reducing sugars, leading to the creation of Advanced Glycation End-products (AGEs). These AGEs have been associated with changes in the mechanical properties of collagen fibers. Interestingly, various studies have reported that plant polyphenols possess amine oxidase-like activity and can act as potent inhibitors of protein glycation. This review article focuses on compiling the literature describing polyphenols with amine oxidase-like activity and antiglycation properties. Specifically, we explore the molecular mechanisms by which specific flavonoids impact or protect the normal collagen cross-linking process. Furthermore, we discuss how these dual activities can be harnessed to generate properly cross-linked collagen molecules, thereby promoting the stabilization of highly organized collagen fibrils.
    Keywords collagen cross-linking ; extracellular matrix ; fibrosis ; glycation ; lysyl oxidase ; polyphenols ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 571
    Language English
    Publishing date 2023-07-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Transporter networks can serve plant cells as nutrient sensors and mimic transceptor-like behavior

    Ingo Dreyer / Kunkun Li / Janin Riedelsberger / Rainer Hedrich / Kai R. Konrad / Erwan Michard

    iScience, Vol 25, Iss 4, Pp 104078- (2022)

    2022  

    Abstract: Summary: Sensing of external mineral nutrient concentrations is essential for plants to colonize environments with a large spectrum of nutrient availability. Here, we analyzed transporter networks in computational cell biology simulations to understand ... ...

    Abstract Summary: Sensing of external mineral nutrient concentrations is essential for plants to colonize environments with a large spectrum of nutrient availability. Here, we analyzed transporter networks in computational cell biology simulations to understand better the initial steps of this sensing process. The networks analyzed were capable of translating the information of changing external nutrient concentrations into cytosolic H+ and Ca2+ signals, two of the most ubiquitous cellular second messengers. The concept emerging from the computational simulations was confirmed in wet-lab experiments. We document in guard cells that alterations in the external KCl concentration were translated into cytosolic H+ and Ca2+ transients as predicted. We show that transporter networks do not only serve their primary task of transport, but can also take on the role of a receptor without requiring conformational changes of a transporter protein. Such transceptor-like phenomena may be quite common in plants.
    Keywords Biological sciences ; Mathematical biosciences ; Plant biology ; Plant physiology ; Plant nutrition ; Science ; Q
    Subject code 580
    Language English
    Publishing date 2022-04-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Plant HKT Channels

    Janin Riedelsberger / Julia K. Miller / Braulio Valdebenito-Maturana / Miguel A. Piñeros / Wendy González / Ingo Dreyer

    International Journal of Molecular Sciences, Vol 22, Iss 4, p

    An Updated View on Structure, Function and Gene Regulation

    2021  Volume 1892

    Abstract: HKT channels are a plant protein family involved in sodium (Na + ) and potassium (K + ) uptake and Na + -K + homeostasis. Some HKTs underlie salt tolerance responses in plants, while others provide a mechanism to cope with short-term K + shortage by ... ...

    Abstract HKT channels are a plant protein family involved in sodium (Na + ) and potassium (K + ) uptake and Na + -K + homeostasis. Some HKTs underlie salt tolerance responses in plants, while others provide a mechanism to cope with short-term K + shortage by allowing increased Na + uptake under K + starvation conditions. HKT channels present a functionally versatile family divided into two classes, mainly based on a sequence polymorphism found in the sequences underlying the selectivity filter of the first pore loop. Physiologically, most class I members function as sodium uniporters, and class II members as Na + /K + symporters. Nevertheless, even within these two classes, there is a high functional diversity that, to date, cannot be explained at the molecular level. The high complexity is also reflected at the regulatory level. HKT expression is modulated at the level of transcription, translation, and functionality of the protein. Here, we summarize and discuss the structure and conservation of the HKT channel family from algae to angiosperms. We also outline the latest findings on gene expression and the regulation of HKT channels.
    Keywords HKT channels ; sodium transport ; potassium transport ; selectivity filter ; gene regulation ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 333
    Language English
    Publishing date 2021-02-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article: The potassium battery: a mobile energy source for transport processes in plant vascular tissues

    Dreyer, Ingo / Judith Lucia Gomez‐Porras / Janin Riedelsberger

    new phytologist. 2017 Dec., v. 216, no. 4

    2017  

    Abstract: Contents 1049 I. 1049 II. 1050 III. 1050 IV. 1050 V. 1051 VI. 1051 VII. 1052 VIII. 1052 1053 References 1053 SUMMARY: Plant roots absorb potassium ions from the soil and transport them in the xylem via the transpiration stream to the shoots. There, in ... ...

    Abstract Contents 1049 I. 1049 II. 1050 III. 1050 IV. 1050 V. 1051 VI. 1051 VII. 1052 VIII. 1052 1053 References 1053 SUMMARY: Plant roots absorb potassium ions from the soil and transport them in the xylem via the transpiration stream to the shoots. There, in source tissues where sufficient chemical energy (ATP) is available, K⁺ is loaded into the phloem and then transported with the phloem stream to other parts of the plant; in part, transport is also back to the roots. This, at first sight, futile cycling of K⁺ has been uncovered to be part of a sophisticated mechanism that (1) enables the shoot to communicate its nutrient demand to the root, (2) contributes to the K⁺ nutrition of transport phloem tissues and (3) transports energy stored in the K⁺ gradient between phloem cytosol and the apoplast. This potassium battery can be tapped by opening AKT2‐like potassium channels and then enables the ATP‐independent energization of other transport processes, such as the reloading of sucrose. Insights into these mechanisms have only been possible by combining wet‐lab and dry‐lab experiments by means of computational cell biology modeling and simulations.
    Keywords adenosine triphosphate ; apoplast ; batteries ; cations ; cytosol ; energy ; models ; nutrition ; phloem ; potassium ; potassium channels ; roots ; shoots ; soil ; streams ; sucrose ; transpiration ; xylem
    Language English
    Dates of publication 2017-12
    Size p. 1049-1053.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note REVIEW
    ZDB-ID 208885-x
    ISSN 1469-8137 ; 0028-646X
    ISSN (online) 1469-8137
    ISSN 0028-646X
    DOI 10.1111/nph.14667
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: The Surprising Dynamics of Electrochemical Coupling at Membrane Sandwiches in Plants

    Ingo Dreyer / Fernando Vergara-Valladares / Franko Mérida-Quesada / María Eugenia Rubio-Meléndez / Naomí Hernández-Rojas / Janin Riedelsberger / Sadith Zobeida Astola-Mariscal / Charlotte Heitmüller / Mónica Yanez-Chávez / Oscar Arrey-Salas / Alex San Martín-Davison / Carlos Navarro-Retamal / Erwan Michard

    Plants, Vol 12, Iss 1, p

    2023  Volume 204

    Abstract: Transport processes across membranes play central roles in any biological system. They are essential for homeostasis, cell nutrition, and signaling. Fluxes across membranes are governed by fundamental thermodynamic rules and are influenced by electrical ... ...

    Abstract Transport processes across membranes play central roles in any biological system. They are essential for homeostasis, cell nutrition, and signaling. Fluxes across membranes are governed by fundamental thermodynamic rules and are influenced by electrical potentials and concentration gradients. Transmembrane transport processes have been largely studied on single membranes. However, several important cellular or subcellular structures consist of two closely spaced membranes that form a membrane sandwich. Such a dual membrane structure results in remarkable properties for the transport processes that are not present in isolated membranes. At the core of membrane sandwich properties, a small intermembrane volume is responsible for efficient coupling between the transport systems at the two otherwise independent membranes. Here, we present the physicochemical principles of transport coupling at two adjacent membranes and illustrate this concept with three examples. In the supplementary material, we provide animated PowerPoint presentations that visualize the relationships. They could be used for teaching purposes, as has already been completed successfully at the University of Talca.
    Keywords computational cell biology ; modelling ; nutrient transport ; plant biophysics ; mathematical model ; plant–fungus interaction ; Botany ; QK1-989
    Subject code 612
    Language English
    Publishing date 2023-01-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Outward Rectification of Voltage-Gated K+ Channels Evolved at Least Twice in Life History.

    Janin Riedelsberger / Ingo Dreyer / Wendy Gonzalez

    PLoS ONE, Vol 10, Iss 9, p e

    2015  Volume 0137600

    Abstract: Voltage-gated potassium (K+) channels are present in all living systems. Despite high structural similarities in the transmembrane domains (TMD), this K+ channel type segregates into at least two main functional categories-hyperpolarization-activated, ... ...

    Abstract Voltage-gated potassium (K+) channels are present in all living systems. Despite high structural similarities in the transmembrane domains (TMD), this K+ channel type segregates into at least two main functional categories-hyperpolarization-activated, inward-rectifying (Kin) and depolarization-activated, outward-rectifying (Kout) channels. Voltage-gated K+ channels sense the membrane voltage via a voltage-sensing domain that is connected to the conduction pathway of the channel. It has been shown that the voltage-sensing mechanism is the same in Kin and Kout channels, but its performance results in opposite pore conformations. It is not known how the different coupling of voltage-sensor and pore is implemented. Here, we studied sequence and structural data of voltage-gated K+ channels from animals and plants with emphasis on the property of opposite rectification. We identified structural hotspots that alone allow already the distinction between Kin and Kout channels. Among them is a loop between TMD S5 and the pore that is very short in animal Kout, longer in plant and animal Kin and the longest in plant Kout channels. In combination with further structural and phylogenetic analyses this finding suggests that outward-rectification evolved twice and independently in the animal and plant kingdom.
    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2015-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article: Voltage-Sensor Transitions of the Inward-Rectifying K⁺ Channel KAT1 Indicate a Latching Mechanism Biased by Hydration within the Voltage Sensor

    Lefoulon, Cécile / Annegret Honsbein / Christopher Grefen / Ingo Dreyer / Janin Riedelsberger / Michael R. Blatt / Paul Vijay Gutla / Rucha Karnik / Tomás Poblete / Wendy Gonzalez

    Plant physiology. 2014 Oct., v. 166, no. 2

    2014  

    Abstract: Manipulating the electrostatic charge network that stabilizes the voltage sensor of the KAT1 K ⁺ channel displaces channel gating across more than 140 mV within the physiological voltage range . ... The Kv-like (potassium voltage-dependent) K ⁺ ... ...

    Abstract Manipulating the electrostatic charge network that stabilizes the voltage sensor of the KAT1 K ⁺ channel displaces channel gating across more than 140 mV within the physiological voltage range .

    The Kv-like (potassium voltage-dependent) K ⁺ channels at the plasma membrane, including the inward-rectifying KAT1 K ⁺ channel of Arabidopsis ( Arabidopsis thaliana ), are important targets for manipulating K ⁺ homeostasis in plants. Gating modification, especially, has been identified as a promising means by which to engineer plants with improved characteristics in mineral and water use. Understanding plant K ⁺ channel gating poses several challenges, despite many similarities to that of mammalian Kv and Shaker channel models. We have used site-directed mutagenesis to explore residues that are thought to form two electrostatic countercharge centers on either side of a conserved phenylalanine (Phe) residue within the S2 and S3 α-helices of the voltage sensor domain (VSD) of Kv channels. Consistent with molecular dynamic simulations of KAT1, we show that the voltage dependence of the channel gate is highly sensitive to manipulations affecting these residues. Mutations of the central Phe residue favored the closed KAT1 channel, whereas mutations affecting the countercharge centers favored the open channel. Modeling of the macroscopic current kinetics also highlighted a substantial difference between the two sets of mutations. We interpret these findings in the context of the effects on hydration of amino acid residues within the VSD and with an inherent bias of the VSD, when hydrated around a central Phe residue, to the closed state of the channel.
    Keywords electrostatic interactions ; potassium ; potassium channels
    Language English
    Dates of publication 2014-10
    Size p. 960-975.
    Publishing place American Society of Plant Biologists
    Document type Article
    ZDB-ID 208914-2
    ISSN 1532-2548 ; 0032-0889
    ISSN (online) 1532-2548
    ISSN 0032-0889
    DOI 10.1104/pp.114.244319
    Database NAL-Catalogue (AGRICOLA)

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