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001-es BibID:BIBFORM015936
Első szerző:Fülöp Csaba
Cím:Impaired cumulus mucification and female sterility in tumor necrosis factor-induced protein-6 deficient mice / Csaba Fülöp, Sándor Szántó, Durba Mukhopadhyay, Tamás Bárdos, Rajesh V. Kamath, Marylin S. Rugg, Anthony J. Day, Antonietta Salustri, Vincent C. Hascall, Tibor T. Glant, Katalin Mikecz
Dátum:2003
ISSN:0950-1991 (Print)
Megjegyzések:Mucification of the cumulus layer around the oocyte is an obligatory process for female fertility. Tumor necrosis factor-induced protein-6 (TNFIP6 or TSG6) has been shown to be specifically expressed during this process. We have generated TNFIP6-deficient mice and tested the ability of their cumulus cells to undergo mucification. Cumulus cell-oocyte complexes fail to expand in TNFIP6-deficient female mice because of the inability of the cumulus cells to assemble their hyaluronan-rich extracellular matrix. The impaired cumulus matrix formation is due to the lack of covalent complexes between hyaluronan and the heavy chains of the inter-alpha-trypsin inhibitor family. As a consequence, TNFIP6-deficient females are sterile. Cultured TNFIP6-deficient cumulus cell-oocyte complexes also fail to expand when stimulated with dibutyryl cyclic AMP or epidermal growth factor. Recombinant TNFIP6 is able to catalyze the covalent transfer of heavy chains to hyaluronan in a cell-free system, restore the expansion of Tnfip6-null cumulus cell-oocyte complexes in vitro, and rescue the fertility in Tnfip6-null females. These results provide clear evidence that TNFIP6 is a key catalyst in the formation of the cumulus extracellular matrix and indispensable for female fertility.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animals
Cell Adhesion Molecules/genetics/*metabolism
Extracellular Matrix/*metabolism
Female
Genotype
Humans
Hyaluronic Acid/chemistry/*metabolism
*Infertility, Female
Male
Mice
Mice, Knockout
Oocytes/cytology/*physiology
Ovary/anatomy & histology/pathology
Recombinant Proteins/genetics/metabolism
Megjelenés:Development. - 130 : 10 (2003), p. 2253-2261. -
További szerzők:Szántó Sándor (1968-) (belgyógyász, reumatológus) Mukhopadhyay, Durba Bárdos Tamás Kamath, Rajesh V. Rugg, Marylin S. Day, Anthony J. Salustri, Antonietta Hascall, Vincent C. Glant Tibor T. Mikecz Katalin
Internet cím:elektronikus változat
DOI
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2.

001-es BibID:BIBFORM039164
Első szerző:Glant Tibor T.
Cím:Cartilage-specific constitutive expression of TSG-6 protein (product of tumor necrosis factor alpha-stimulated gene 6) provides a chondroprotective, but not antiinflammatory, effect in antigen-induced arthritis / Glant, T. T., Kamath, R. V., Bardos, T., Gal, I., Szanto, S., Murad, Y. M., Sandy, J. D., Mort, J. S., Roughley, P. J., Mikecz, K.
Dátum:2002
ISSN:0004-3591
Megjegyzések:To study the chondroprotective effect of constitutively expressed TSG-6 protein (tumor necrosis factor alpha-induced protein 6; Tnfip6) in cartilage, using antigen-induced arthritis (AIA) in mice. METHODS: Transgenic mice constitutively expressing TSG-6 protein in cartilage were generated. Cartilage-specific constitutive expression of TSG-6 protein was confirmed by in situ hybridization, Western blot analysis, and immunohistochemistry. Control and transgenic mice were immunized with methylated bovine serum albumin (mBSA), and arthritis was induced by the intraarticular injection of mBSA. Mice were monitored up to day 35 after the challenge, and knee joint sections were examined for loss of cartilage proteoglycan (aggrecan) using Safranin O staining and antibodies to neoepitopes generated by various metalloproteinases (MPs). The loss of aggrecan in Safranin O-stained sections was quantified by morphometric methods. RESULTS: Tsg6/tnfip6 transgenic mice constitutively expressed tsg6/tnfip6 messenger RNA and corresponding TSG-6 protein in cartilage from embryonic life through adulthood, without any phenotypic abnormalities. These mice were used for AIA studies. Intraarticular injection of mBSA uniformly induced severe inflammation both in control (wild-type and an irrelevant transgenic line) mice and in tsg6/tnfip6 transgenic mice. In contrast to the mBSA-injected knee joints of control animals that were heavily damaged from day 5, the cartilage of transgenic mice that constitutively expressed TSG-6 protein remained intact for at least 1 week, and this was followed by a relatively reduced loss of aggrecan. Concomitant with the loss of aggrecan, MP-generated neoepitopes accumulated in unprotected joints. By day 35, the proteoglycan content returned to nearly normal levels in tsg6/tnfip6 transgenic mice, whereas it remained low in MP-damaged knee cartilage of control mice. CONCLUSION: TSG-6 protein is known to form a complex with inter-alpha-inhibitor (IalphaI), a potent serine protease inhibitor, which may be immobilized via the hyaluronan (HA)-binding domain of TSG-6 protein in the HA-rich extracellular matrix of cartilage. Thus, the local accumulation of TSG-6 protein and TSG-6 protein-bound IalphaI in tsg6/tnfip6 transgenic mice may inhibit serine proteases and subsequent activation of MPs. It is suggested that this mechanism might protect cartilage from extensive degradation even in the presence of acute inflammation.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Arthritis And Rheumatism. - 46 : 8 (2002), p. 2207-2218. -
További szerzők:Kamath, Rajesh V. Bárdos Tamás Gál István (1957-) (belgyógyász) Szántó Sándor (1968-) (belgyógyász, reumatológus) Murad, Yanal M. Sandy, John D. Mort, John S. Roughley, Peter J. Mikecz Katalin
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