Two Distinct Populations of Tumor Necrosis Factor-Stimulated Gene-6 Protein in the Extracellular Matrix of Expanded Mouse Cumulus Cell–Oocyte Complexes

Mukhopadhyay, Durba; Hascall, Vincent C.; Day, Anthony J.; Salustri, Antonietta; Fülöp, Csaba

doi:10.1006/abbi.2001.2552

Cited by 120 publications

(145 citation statements)

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“…3 Previous studies have shown that high glucose treatment of mesangial cell cultures induced monocyte adhesion (7), and our studies now show that about 75% of the glucose-induced adhesion of monocytes is actually mediated by hyaluronan structures. The organization of these unique structures must involve hyaluronan-binding proteins (hyaladherins), such as versican and the protein product of the TNF-␣-stimulated gene 6, as well as the serum-protein complex, inter-␣-trypsin inhibitor (25). No doubt, the different organizations of hyaluronan with cell surface and ECM hyaladherins define different functions of cells in normal and pathogenic processes.…”

Section: Discussionmentioning

confidence: 99%

“…Immunohistochemistry-Thin sections of paraffin-embedded kidneys and methanol-fixed RMC cultures on coverslips were stained for hyaluronan with a hyaluronan-binding protein (HABP) (Seikagaku America), for nuclei with 4Ј,6-diamidino-2-phenylindole (DAPI), and in the sections, for monocytes/macrophages with anti-rat ED1 antibody, as described previously (5,12,25,26). Samples were treated with HABP at a 1:100 dilution and with anti-rat ED1 antibody at a 1:75 dilution, washed and treated with fluorescein isothiocyanate-streptavidin at 1:500 dilution and/or with anti-mouse IgG TRITC antibody at 1:200 dilution.…”

Section: Establishment Of Rmc Cultures and Induction Of Diabetes In Rmentioning

confidence: 99%

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Hyaluronan Structures Synthesized by Rat Mesangial Cells in Response to Hyperglycemia Induce Monocyte Adhesion

Ai-min

Hascall

2004

Journal of Biological Chemistry

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128

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Mesangial expansion, the principal glomerular lesion in diabetic nephropathy, is preceded by a phenotypic activation and transient proliferation of the glomerular mesangial cells and by a prominent glomerular infiltration of monocytes and macrophages. Because this infiltration seems to play a key role in the subsequent mesangial matrix expansion, we tested the response of cultures of rat mesangial cells (RMCs) for monocyte adhesion in response to hyperglycemia. Increasing the medium glucose concentration from 5.6 mM (normal) to 25.6 mM (hyperglycemic) significantly increased hyaluronan in the cell matrix, with a concurrent 3-to 4-fold increase in adhesion of U937 monocytic leukemic cells to cultures of near confluent RMCs. These responses were attributed directly to the high glucose concentration and not to increased extracellular osmolality. The monocytes primarily bind directly to hyaluronan-based structures in vitro. Abnormal deposits of hyaluronan were found in glomeruli of kidney sections from diabetic rats 1 week after streptozotocin treatment, often with closely associated monocytes/macrophages, suggesting that similar structures are relevant in vivo. The monocyte adhesion response to high glucose concentration required growth stimulation of RMCs by serum and activation of protein kinase C, and was inhibited by prior passage of the RMCs in the presence of heparin. These results suggest that the response may be cell growth state and protein kinase C-dependent. When incubated with the viral mimetic, poly I:C, in the presence of normal glucose, heparin-passaged RMCs still increased cell-associated hyaluronan and exhibited hyaluronan-mediated adhesion of monocytes, indicating that the two stimuli, high glucose and viral mimetic, induce the production of the hyaluronan structures that promote monocyte adhesion by distinctly different intracellular signaling mechanisms.Mesangial expansion, the principal glomerular lesion in diabetic nephropathy, reduces the area for filtration and leads eventually to sclerosis and renal failure (1, 2). However, the expansion of the mesangial extracellular matrix (ECM) 1 and the sclerosis that characterize diabetic nephropathy are preceded by a phenotypic activation and transient proliferation of the glomerular mesangial cells. This is followed by a prominent glomerular infiltration of monocytes and macrophages (3-5) that seems to play a key role in the subsequent mesangial matrix expansion, hypercellularity, and onset of proteinuria (6, 7). Nevertheless, the molecular mechanisms underlying glomerular infiltration by monocytes and macrophages are still unclear.The interaction of monocytes with mesangial cells in culture has been studied previously using U937 cells, a monocytic leukemic cell line that is a widely accepted model for monocyte adhesion (7,8), and mesangial cell cultures incubated in media with high glucose concentrations bind more U937 cells (7). Generally, the interactions between monocytes and resident cells involve: (i) monocyte cell surface proteins, including C...

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Section: Discussionmentioning

confidence: 99%

Section: Establishment Of Rmc Cultures and Induction Of Diabetes In Rmentioning

confidence: 99%

Hyaluronan Structures Synthesized by Rat Mesangial Cells in Response to Hyperglycemia Induce Monocyte Adhesion

Ai-min

Hascall

2004

Journal of Biological Chemistry

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128

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“…In vivo expression of TSG-6/Tnfip6 has been associated with inflammatory arthritis (3,5), but the protein is produced in a variety of cells exposed to proinflammatory stimuli in vitro (2,28,29), and also in a physiologic process such as matrix formation around the cumulus cell-oocyte complex (30). In fact, the relationship between impaired cumulus cell-oocyte matrix assembly and female sterility in Tnfip6-knockout mice reveals an essential role for this protein in the formation of crosslinked HA fibers around the oocyte that is necessary for the expansion of cumulus matrix and subsequent oocyte fertilization (15).…”

Section: Discussionmentioning

confidence: 99%

Enhanced neutrophil extravasation and rapid progression of proteoglycan‐induced arthritis in TSG‐6–knockout mice

Szántó¹,

Bárdos²,

Gál³

et al. 2004

Arthritis & Rheumatism

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Objective. To gain insight into the mechanisms of the antiinflammatory effect of tumor necrosis factor ␣ (TNF␣)-induced protein 6 (Tnfip6) in arthritis, using Tnfip6-deficient animals.Methods. TNF␣-stimulated gene 6 (TSG-6) coding for Tnfip6 was disrupted. Tnfip6-deficient mice were backcrossed into proteoglycan-induced arthritis (PGIA)-susceptible BALB/c mice, and arthritis was induced by systemic immunization with cartilage proteoglycan (PG). Thioglycollate-induced sterile peritonitis was also assessed, to monitor the early events of neutrophil extravasation in wild-type and Tnfip6-deficient mice in the presence or absence of treatment with recombinant murine Tnfip6.Results. The onset of PGIA was similar, but progression and severity were significantly greater, in Tnfip6-deficient mice compared with wild-type BALB/c mice. However, this was not associated with enhanced T or B cell responses to cartilage PGs, but rather, an early and more extensive infiltration of the synovium with neutrophil leukocytes was the most prominent histopathologic feature of PGIA in Tnfip6-deficient mice. This was accompanied by elevated serum levels of interleukin-6 and amyloid A, and significantly increased activities of the enzymes plasmin, myeloperoxidase, and neutrophil elastase in the inflamed paw joints of Tnfip6-null mice, when compared with that of the wild-type littermates. Loss of control over several components of inflammation resulted in extensive and rapid cartilage degradation, bone erosion, joint ankylosis, and deformities in Tnfip6-null animals. In support of the antiinflammatory effect of Tnfip6 via the inhibition of polymorphonuclear (PMN) cell efflux, neutrophil invasion during thioglycollate-induced peritonitis was 2-fold higher in Tnfip6-deficient animals than in wild-type animals, but was dramatically suppressed by intravenous injection of recombinant murine Tnfip6.Conclusion. Tnfip6 is a multifunctional antiinflammatory protein that is produced at the site of inflammation and can be retained by the hyaluronanrich extracellular matrix. A major effect of Tnfip6 is the inhibition of the extravasation of PMN cells, predominantly neutrophils, into the site of inflammation, most likely via a CD44/hyaluronan/Tnfip6-mediated blocking mechanism.

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“…However, it is yet unclear how the SHAP-HA complex contributes to the stabilization of an HA-rich matrix. Details on its molecular structure, particularly the number of SHAP molecules bound to an HA chain, would help us to understand the molecular interactions in the HA-rich matrix, not only between the SHAP-HA complexes but also between the SHAP-HA complex and other matrix components such as TSG-6 (19). Here for the first time, we have characterized a structural feature of the SHAP-HA complex isolated from pathological synovial fluid, and we provide evidence for the multiple binding of SHAPs to an HA chain.…”

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confidence: 99%

Molecular Heterogeneity of the SHAP-Hyaluronan Complex

Yingsung

Zhuo

Mörgelin

et al. 2003

Journal of Biological Chemistry

101

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We previously found that a covalent complex of SHAPs (serum-derived hyaluronan-associated proteins), the heavy chains of inter-␣-trypsin inhibitor family molecules, with hyaluronan (HA) is accumulated in synovial fluid of patients with rheumatoid arthritis, and the complex is circulated in patient plasma at high concentrations. How the SHAP-HA complex participates in this disease is unknown. To address this question, it is essential to clarify the structural features of this macromolecule. The SHAP-HA complex purified from synovial fluid of the patients by three sequential CsCl isopycnic centrifugations was heterogeneous in density, and the fractions with different densities had distinct SHAPto-HA ratios. Agarose gel electrophoresis and column chromatography revealed that there was no apparent difference in the size distribution of HA to which SHAPs were bound between the fractions with different densities. The SHAP-HA complex in the higher density fraction had fewer SHAP molecules per HA chain. Therefore, the difference between the fractions with different densities was due to a heterogeneous population of the SHAP-HA complex, namely the different number of SHAP molecules bound to an HA chain. Based on the SHAP and HA contents of the purified preparations, we estimated that an HA chain with a molecular weight of 2 ؋ 10 6 has as many as five covalently bound SHAPs, which could give a proteinaceous multivalency to HA. Furthermore, we also found that the SHAP-HA complex tends to form aggregates, judging from the migration and elution profiles in agarose gel electrophoresis and gel filtration, respectively. The multivalent feature of the SHAP-HA complex was also confirmed by the negative staining electron micrographic images of the purified fractions. Taken together, those structural characteristics may underlie the aggregate-forming and extracellular matrix-stabilizing ability of the SHAP-HA complex.

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Two Distinct Populations of Tumor Necrosis Factor-Stimulated Gene-6 Protein in the Extracellular Matrix of Expanded Mouse Cumulus Cell–Oocyte Complexes

Cited by 120 publications

References 37 publications

Hyaluronan Structures Synthesized by Rat Mesangial Cells in Response to Hyperglycemia Induce Monocyte Adhesion

Hyaluronan Structures Synthesized by Rat Mesangial Cells in Response to Hyperglycemia Induce Monocyte Adhesion

Enhanced neutrophil extravasation and rapid progression of proteoglycan‐induced arthritis in TSG‐6–knockout mice

Molecular Heterogeneity of the SHAP-Hyaluronan Complex

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