The Internal Region Leucine-rich Repeat 6 of Decorin Interacts with Low Density Lipoprotein Receptor-related Protein-1, Modulates Transforming Growth Factor (TGF)-β-dependent Signaling, and Inhibits TGF-β-dependent Fibrotic Response in Skeletal Muscles

Cabello-Verrugio, Claudio; Santander, Cristián; Cofre, Catalina; Acuña, María José; Melo, Francisco S.; Brandan, Enrique

doi:10.1074/jbc.m111.312488

Cited by 60 publications

(42 citation statements)

References 67 publications

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“…In addition, decorin is also involved in various pathological processes, such as wound healing, fibrosis, inflammation and tumor invasion, in which remodeling of connective tissues occur [13], [28]–[33]. The multifunctional role of decorin is due to its capacity to modulate the activity and/or stability of a wide variety of proteins, such as cytokines, growth factors, cell surface receptors and structural matrix proteins via direct binding to these proteins.…”

Section: Discussionmentioning

confidence: 99%

“…The multifunctional role of decorin is due to its capacity to modulate the activity and/or stability of a wide variety of proteins, such as cytokines, growth factors, cell surface receptors and structural matrix proteins via direct binding to these proteins. Impairment of decorin binding to its partners due to aberrant decorin degradation is linked to fibrotic wound healing [28]. Recent data suggest that granzyme B, a serine protease produced mainly by cytotoxic lymphocytes is capable of cleaving decorin [34], [35].…”

Section: Discussionmentioning

confidence: 99%

“…The temporal and spatial expressions of these two proteases are likely different in a given inflammatory response, as neutrophils are much more abundant than cytotoxic lymphocytes in peripheral blood, and neutrophils influx into inflammatory lesions normally occurs prior to lymphocytes. Further characterization of decorin-degrading proteases would enhance our understanding of decorin biology and its involvement in diseases [13], [28]–[33].…”

Section: Discussionmentioning

confidence: 99%

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Solar Ultraviolet Irradiation Induces Decorin Degradation in Human Skin Likely via Neutrophil Elastase

Xia

Liu

et al. 2013

PLoS ONE

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Exposure of human skin to solar ultraviolet (UV) irradiation induces matrix metalloproteinase-1 (MMP-1) activity, which degrades type I collagen fibrils. Type I collagen is the most abundant protein in skin and constitutes the majority of skin connective tissue (dermis). Degradation of collagen fibrils impairs the structure and function of skin that characterize skin aging. Decorin is the predominant proteoglycan in human dermis. In model systems, decorin binds to and protects type I collagen fibrils from proteolytic degradation by enzymes such as MMP-1. Little is known regarding alterations of decorin in response to UV irradiation. We found that solar-simulated UV irradiation of human skin in vivo stimulated substantial decorin degradation, with kinetics similar to infiltration of polymorphonuclear (PMN) cells. Proteases that were released from isolated PMN cells degraded decorin in vitro. A highly selective inhibitor of neutrophil elastase blocked decorin breakdown by proteases released from PMN cells. Furthermore, purified neutrophil elastase cleaved decorin in vitro and generated fragments with similar molecular weights as those resulting from protease activity released from PMN cells, and as observed in UV-irradiated human skin. Cleavage of decorin by neutrophil elastase significantly augmented fragmentation of type I collagen fibrils by MMP-1. Taken together, these data indicate that PMN cell proteases, especially neutrophil elastase, degrade decorin, and this degradation renders collagen fibrils more susceptible to MMP-1 cleavage. These data identify decorin degradation and neutrophil elastase as potential therapeutic targets for mitigating sun exposure-induced collagen fibril degradation in human skin.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Solar Ultraviolet Irradiation Induces Decorin Degradation in Human Skin Likely via Neutrophil Elastase

Xia

Liu

et al. 2013

PLoS ONE

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“…[122][123][124] As a result of their diverse protein cores and GAG side chains, SLRPs interact with various cytokines, growth factors, cell surface receptors, as well as other matrix proteins. Indeed, they can bind different types of collagens, 125 TLRs, 123 epidermal growth factor receptors and insulin growth factor receptors, 126 low-density lipoprotein receptors, 127 and TGF-β. 128 These interactions illustrate the involvement of SLRPs in a wide range of cellular functions and pathophysiologic responses, including collagen fibril assembly, 125 inflammation, 123 cell proliferation, 126 atherosclerosis, 127 and fibrosis, 128 hence emphasizing their potential role in cardiac matrix biology.…”

Section: Small Leucine-rich Proteoglycansmentioning

confidence: 99%

Myocardial Extracellular Matrix

Rienks

Papageorgiou

Frangogiannis

et al. 2014

Circulation Research

313

170

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Abstract:The cardiac extracellular matrix (ECM) is a complex architectural network consisting of structural and nonstructural proteins, creating strength and plasticity. The nonstructural compartment of the ECM houses a variety of proteins, which are vital for ECM plasticity, and can be divided into 3 major groups: glycoproteins, proteoglycans, and glycosaminoglycans. The common denominator for these groups is glycosylation, which refers to the decoration of proteins or lipids with sugars. This review will discuss the fundamental role of the matrix in cardiac development, homeostasis, and remodeling, from a glycobiology point of view. Glycoproteins (eg, thrombospondins, secreted protein acidic and rich in cysteine, tenascins), proteoglycans (eg, versican, syndecans, biglycan), and glycosaminoglycans (eg, hyaluronan, heparan sulfate) are upregulated on cardiac injury and regulate key processes in the remodeling myocardium such as inflammation, fibrosis, and angiogenesis. Albeit some parallels can be made regarding the processes these proteins are involved in, their specific functions are extremely diverse. In fact, under varying conditions, individual proteins can even have opposing functions, making spatiotemporal contribution of these proteins in the rearrangement of multifaceted ECM very hard to grasp. Alterations of protein characteristics by the addition of sugars may explain the immense, yet tightly regulated, variability of the remodeling cardiac matrix. Understanding the role of glycosylation in altering the ultimate function of glycoproteins, proteoglycans, and glycosaminoglycans in the myocardium may lead to the development of new biochemical structures or compounds with great therapeutic potential for patients with heart disease. (Circ Res. 2014;114:872-888.)

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“…(i) It can bind to TLR2 and TLR4 followed by inducing NF-B signaling (20). (ii) It is capable of sequestering TGF-␤ under fibrotic conditions (21,22). It enhances the IFN-␥-induced expression of inducible NO synthase, TNF-␣, IL-1␤, and IL-6 (23).…”

mentioning

confidence: 99%