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Transforming Growth Factor-β: A Cytokine Paradigm
Published in Thomas F. Kresina, Immune Modulating Agents, 2020
Michelle R. Frazier-Jessen, Nancy McCartney-Francis, Sharon M. Wahl
While treatment with neutralizing antibodies to TGF-β might be one effective method for improving kidney fibrosis in these instances, it is likely not cost-effective and may lead to other side effects. Therefore, treatment with TGF-β antagonists or even antisense therapy might prove more efficacious. Isaka and colleagues have recently demonstrated an alternative form of drug delivery in an animal model of chronic renal glomerulosclerosis [43]. In this approach, rat muscle cells were transfected with a vector containing the gene for human decorin, a proteoglycan that is associated with the extracellular matrix and is able to bind and neutralize TGF-β via its core protein. In rats receiving muscle-based gene therapy, accumulation of pathological matrix is not observed, proteinuria (a measure of kidney function) is significantly reduced, and glomerular TGF-β1 expression is also substantially reduced.
Metabolic Therapies for Muscle Injury
Published in Kohlstadt Ingrid, Cintron Kenneth, Metabolic Therapies in Orthopedics, Second Edition, 2018
Ana V. Cintrón, Kenneth Cintron
The use of an anti-fibrotic agent in combination with PRP has significantly improved healing when compared to PRP alone. Losartan, an angiotensin II receptor antagonist, blocks the effect of TGF-β1 and reduces fibrosis, improving the effectiveness of the PRP on muscle healing, an effect which is suspected to be mediated through the increase of angiogenesis [83]. Decorin, a growth factor antagonist for tumor growth which has an antifibrotic, anti-inflammatory and anticancer effect, has also been found to neutralize the negative effect of TGF-β1 when combined with PRP [82].
Cell and Extracellular Matrix Interactions in a Dynamic Biomechanical Environment:
Published in Michel R. Labrosse, Cardiovascular Mechanics, 2018
The proteoglycan biglycan, which has been found to bind elastin (Reinboth et al. 2002), is present in the ventricularis (Latif et al. 2005a, Stephens et al. 2008), where it may contribute to elastogenesis. Elastin retains its elastic properties only when hydrated and becomes brittle when dry (Lillie and Gosline 2002), so the presence of proteoglycans and GAGs in the elastin-rich ventricularis is likely important in maintaining the layer’s mechanical properties. Decorin, which plays a role in collagen fibrillogenesis (Danielson et al. 1997), has been found in the collagen-rich fibrosa (Latif et al. 2005a, Stephens et al. 2008).
Insight into the role of myokines and myogenic regulatory factors under hypobaric hypoxia induced skeletal muscle loss
Published in Biomarkers, 2022
Sukanya Srivastava, Richa Rathor, Som Nath Singh, Geetha Suryakumar
In the present study, our observations indicate enhanced levels of decorin along with irisin, IL-6 and IL-15 on 1 dHH and 3 dHH exposure when compared with the normoxic control rats; however, the levels were found to be non-significant with prolonged HH exposure in relation to control. In vitro and in vivo studies have demonstrated that enhanced decorin levels regulate myofiber proliferation and differentiation that strengthens muscle growth (Kishioka et al. 2008, El Shafey et al. 2016). Carbó et al. (2000) reported IL-15 as anti-inflammatory cytokine, ameliorating skeletal muscle wasting via suppressing protein degradation pathway. Recently, Liu et al. (2022) described the negative regulation of FNDC5/irisin by HIF-1α during hypoxia induces muscle atrophy. Further, irisin attenuated denervation-induced atrophy via inducing skeletal muscle protein synthesis and improving skeletal muscle injury. Consequently, suggesting a pivot role of irisin in various cellular as well as metabolic responses. Another study by Serrano et al. (2008) demonstrated the anti-inflammatory effect of IL-6 as a critical regulator of satellite cells and induces skeletal muscle hypertrophy. Our results indicate an adaptive response of the skeletal muscles during the initial days of HH exposure by the levels of various myokines evaluated in the study.
Granzyme B as a therapeutic target: an update in 2022
Published in Expert Opinion on Therapeutic Targets, 2022
Alexandre Aubert, Michael Lane, Karen Jung, David J. Granville
Lastly, GzmB is also indirectly involved in PI-dependent collagen disorganization and fibrosis induction through the cleavage of decorin [25,46], a small 100 kDa proteoglycan of the ECM that possesses two major functions. First, decorin has important structural properties within the dermis, as it promotes collagen fibrillogenesis through assembly and direct binding of collagen I [54]. Decorin is also a potent endogenous inhibitor of TGF-β1, a major pro-fibrotic cytokine that can promote fibroblast activation and matrix deposition [55,56]. Almost completely absent from human PI, decorin levels are significantly reduced in PI from AKO-HFD compared to DKO-HFD mice [46]. GzmB-dependent degradation of decorin leads to (i) reduction of fibrillar collagen content and organization, (ii) increased TGF-β1 bioavailability, and (iii) subsequent activation of dermal fibroblasts in aged human and mice skin during the wound healing process following PI (Figure 1).
Effect of decorin protein administration on rat sciatic nerve injury: an experimental study
Published in Neurological Research, 2022
Alper Geyik, Basar Koc, Serap Cilaker Micili, Müge Kiray, Haluk Vayvada, Selin Guler
Decorin (DCN) is a member of a small leucine-rich proteoglycan family that encompasses 18 members [6]. Fibroblasts and endothelial cells secrete DCN in the matrix. DCN is a natural ligand for TGF-β receptors in particular [7]. DCN suppresses fibrosis formation in various tissues via blockage of TGF-β1 signaling and improves the healing of injured tissue [8]. Besides the regulation of cell proliferation, migration, and differentiation, it is also involved in regulating the inflammation process that occurs after injury. Recombinant DCN has been shown to reduce central nervous system scarring and extracellular matrix protein deposition after laceration, although it is not clear to what extent it penetrates the blood–brain barrier [9]. However, no previous study model on the peripheral nerves has been found in the literature.