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      Unveiling Plant-Based Pectins: Exploring the Interplay of Direct Effects, Fermentation, and Technological Applications in Clinical Research with a Focus on the Chemical Structure

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      Plants
      MDPI AG

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          Abstract

          Pectin, a plant-derived polysaccharide, possesses immense technological and biological application value. Several variables influence pectin’s physicochemical aspects, resulting in different fermentations, interactions with receptors, and other functional properties. Some of those variables are molecular weight, degree of methylation and blockiness, and monosaccharide composition. Cancer cell cytotoxicity, important fermentation-related byproducts, immunomodulation, and technological application were found in cell culture, animal models, and preclinical and clinical assessments. One of the greater extents of recent pectin technological usage involves nanoencapsulation methods for many different compounds, ranging from chemotherapy and immunotherapy to natural extracts from fruits and other sources. Structural modification (modified pectin) is also utilized to enhance the use of dietary fiber. Although pectin is already recognized as a component of significant importance, there is still a need for a comprehensive review that delves into its intricate relationships with biological effects, which depend on the source and structure of pectin. This review covers all levels of clinical research, including cell culture, animal studies, and clinical trials, to understand how the plant source and pectin structures influence the biological effects in humans and some technological applications of pectin regarding human health.

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          Toll-like Receptors and the Control of Immunity

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            Carbohydrate quality and human health: a series of systematic reviews and meta-analyses

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              Toll-like receptors activation, signaling, and targeting: an overview

              Toll-like receptors (TLRs) are an important family of receptors that constitute the first line of defense system against microbes. They can recognize both invading pathogens and endogenous danger molecules released from dying cells and damaged tissues and play a key role in linking innate and adaptive immunity. TLRs are widely distributed in both immune and other body cells. The expressions and locations of TLRs are regulated in response to specific molecules derived from pathogens or damaged host cells. The binding of ligands to TLR activates specific intracellular signaling cascades that initiate host defense reactions. Such binding is ligand-dependent and cell type-dependent and leads to production of pro-inflammatory cytokines and type 1 interferon. TLR-dependent signaling pathways are tightly increased during innate immune responses by a variety of negative regulators. Overactivation of TLRs can ultimately lead to disruption of immune homeostasis and thus increase the risk for inflammatory diseases and autoimmune disorders. Antagonists/inhibitors targeting the TLR signaling pathways have emerged as novel therapeutics to treat these diseases. The present review summarizes the structure, characterizations, and signaling of TLRs and their regulators, as well as describes the implication of TLRs in many diseases with a brief idea about the inhibitors that target TLR signaling pathways. We conclude that TLRs are the main elements of our immune system, and they should be maintained functioning to keep the integrity of innate immunity. Targeting of TLR signaling represents a new challenge for treatment of many diseases.
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                Author and article information

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                Journal
                PLANCD
                Plants
                Plants
                MDPI AG
                2223-7747
                July 2023
                July 24 2023
                : 12
                : 14
                : 2750
                Article
                10.3390/plants12142750
                3a3ae063-48f0-4a05-82d3-e452cabe862a
                © 2023

                https://creativecommons.org/licenses/by/4.0/

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