Decorin, biglycan and their endocytosis receptor in rat renal cortex

Schaefer, Liliana; Hausser, Heinz; Altenburger, Martin; Ugorcakova, Jana; August, Christian; Fisher, Larry W.; Schaefer, Roland M.; Kresse, Hans

doi:10.1046/j.1523-1755.1998.00149.x

Cited by 60 publications

(83 citation statements)

References 36 publications

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“…In contrast, biglycan, with side chains of similar composition compared to those of decorin, is restricted to the perineural lamellae. This is in agreement with the fact that it has been localized in intracellular and pericellular compartments (Bianco et al 1990;Schaefer et al 1998). Biglycan has also been localized in connective tissue (Huang et al 1999).…”

Section: Discussionsupporting

confidence: 89%

Lectin and Proteoglycan Histochemistry of Feline Pacinian Corpuscles

Sames

Halata

Jojovic

et al. 2001

J Histochem Cytochem.

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S U M M A R YWe studied carbohydrate residues of glycoproteins and proteoglycans (PGs) in peritoneal Pacinian corpuscles of five adult cats. Terminal monosaccharides of glycoproteins and related polysaccharides were identified by lectin histochemistry and the PGs and glycosaminoglycans (GAGs) by specific antibodies. The most intensive lectin staining reactions indicated an abundance of glycoconjugates with terminal mannose (Man) or sialic acid residues, but no complex-type oligosaccharides were detected within the corpuscles. Terminal fucose (Fuc) and galactose (Gal) residues typical for O -linked mucin-type glycoproteins generally associated with high water binding capacity were also absent. Antibodies against unsulfated chondroitin (C-0-S), chondroitin-4-sulfate (C-4-S), and decorin showed positive reactions in the interfibrillar spaces between the lamellae, around collagen fibers, and around the lamellae of the perineural capsule, especially in the outer parts known to contain Type II collagen. Biglycan showed a preference for the innermost part of the perineural capsule (intermediate layer), known to contain Type V collagen. Collagen V and biglycan are both linked to growth processes. Hyaluronic acid (HA), chondroitin-6-sulfate (C-6-S) chains, and a chondroitin sulfate proteoglycan (CSPG) were colocalized in the terminal glia. The study of carbohydrates with high water binding capacity may contribute to our understanding of the high viscoelasticity of Pacinian corpuscles.

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Section: Discussionsupporting

confidence: 89%

Lectin and Proteoglycan Histochemistry of Feline Pacinian Corpuscles

Sames

Halata

Jojovic

et al. 2001

J Histochem Cytochem.

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“…In contrast, the normal glomerulus contains only trace amounts of decorin synthesized by mesangial cells. [11][12][13][14][15] In the absence of collagen type I, a well known binding partner, decorin is not retained at the site of formation but is removed by diffusing into the circulation or alternatively by endocytosis. 12,13,16 Decorin accumulates in areas of tubulointerstitial fibrosis in several experimental and human nephropathies and may be a good predictor of progression in chronic kidney disease.…”

Section: Decorinmentioning

confidence: 99%

“…[11][12][13][14][15] In the absence of collagen type I, a well known binding partner, decorin is not retained at the site of formation but is removed by diffusing into the circulation or alternatively by endocytosis. 12,13,16 Decorin accumulates in areas of tubulointerstitial fibrosis in several experimental and human nephropathies and may be a good predictor of progression in chronic kidney disease. 13,[17][18][19][20] Recent progress in SLRP research indicates the amount of decorin in tissue sections does not necessarily reflect its biologic effect because it represents mainly that which has been sequestered in the ECM and therefore may not be available to neutralize TGF-␤ or act as a ligand to various receptors (Figure 1).…”

Section: Decorinmentioning

confidence: 99%

“…16,38,51,53 The bulk of newly synthesized biglycan escapes from the kidney through plasma and presumably also after proteolytic fragmentation of the pro-tein core in the urine or it becomes sequestered in the kidney by binding to various other ECM components. 12,13,16 In fibrotic conditions, the increasing deposition of potential binding partners (collagen types I or VI) 54,55 and reduced proteolytic degradation results in progressive renal accumulation of biglycan within the fibrotic scar. 16 Biglycan is required for stable ECM formation by regulating collagen and elastic fibrils.…”

Section: Biglycan and Renal Fibrosismentioning

confidence: 99%

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Small Leucine-Rich Proteoglycans in Kidney Disease

Schaefer¹

2011

Journal of the American Society of Nephrology

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103

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“…The expression of TLR ligands was studied by using rabbit anti-mouse polyclonal antibodies against fibrinogen (Glostrup, Denmark), GRP-94 (Santa Cruz, CA, USA) and HMGB1 (BD Pharmingen), and goat anti-mouse antibodies against HSP-60 and HSP-70 (Santa Cruz). Bgn was stained using MAY-01, a chicken anti-rat Bgn antiserum, as described previously (Schaefer et al, 1998).…”

Section: Immunohistochemistrymentioning

confidence: 99%

Recipient Toll-like receptors contribute to chronic graft dysfunction by both MyD88- and TRIF-dependent signaling

Wang

Schmaderer

Kiss

et al. 2010

Disease Models &Amp; Mechanisms

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SUMMARY Toll-like receptors (TLRs) recognize specific molecular patterns derived from microbial components (exogenous ligands) or stressed cells (endogenous ligands). Stimulation of these receptors leads to a pronounced inflammatory response in a variety of acute animal models. Chronic allograft dysfunction (CAD) was regarded as a candidate disease to test whether TLRs influence chronic fibrosing inflammation. Potential endogenous renal TLR ligands, specifically for TLR2 and TLR4, have now been detected by a significant upregulation of glucose regulated protein (GRP)-94, fibrinogen, heat shock protein (HSP)-60, HSP-70, biglycan (Bgn) and high-mobility group box chromosomal protein 1 (HMGB1) in the acute and chronic transplant setting. In a genetic approach to define the contribution of TLR2 and TLR4, and their adaptor proteins MyD88 and TRIF [Toll/interleukin (IL)-1 receptor domain-containing adaptor-protein inducing interferon β], to CAD, kidney transplantation of TLR wild-type grafts to recipients who were deficient in TLR2, TLR4, TLR2/4, MyD88 and TRIF was performed. TLR and adaptor protein deficiencies significantly improved the excretory function of chronic kidney grafts by between 65% and 290%, and histopathologic signs of chronic allograft damage were significantly ameliorated. T cells, dendritic cells (DCs) and foremost macrophages were reduced in grafts by up to 4.5-fold. The intragraft concentrations of IL-6, IL-10, monocyte chemotactic protein-1 (MCP-1) and IL-12p70 were significantly lower. TLR-, MyD88- and TRIF-deficient recipients showed a significant reduction in fibrosis. α-smooth muscle actin (α-SMA)-positive cells were decreased by up to ninefold, and collagen I and III were reduced by up to twofold. These findings highlight the functional relevance of TLRs and their two major signaling pathways in graft-infiltrating mononuclear cells in the pathophysiology of CAD. A TLR signaling blockade may be a therapeutic option for the prevention of CAD.

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Decorin, biglycan and their endocytosis receptor in rat renal cortex

Cited by 60 publications

References 36 publications

Lectin and Proteoglycan Histochemistry of Feline Pacinian Corpuscles

Lectin and Proteoglycan Histochemistry of Feline Pacinian Corpuscles

Small Leucine-Rich Proteoglycans in Kidney Disease

Recipient Toll-like receptors contribute to chronic graft dysfunction by both MyD88- and TRIF-dependent signaling

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