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Elevated Levels of Type II Soluble Tumor Necrosis Factor Receptors in the Bronchoalveolar Lavage Fluids of Patients with Sarcoidosis (1997)

Hino, T. ; Nakamura, H. ; Shibata, Y. ; [et al.]

Springer

Lung 175 (1997), S. 187 -193

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ISSN: 1432-1750

Keywords: Key words: Sarcoidosis—Tumor necrosis factor receptor—Lymphocyte—Bronchoalveolar lavage

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract. Since tumor necrosis factor (TNF) is known to be involved in granuloma formation in sarcoidosis, and soluble TNF receptors (sTNF-Rs) inhibit TNF action in vivo, we evaluated the levels of sTNF-Rs in the bronchoalveolar lavage fluids (BALF) of 31 subjects using an enzyme-linked immunosorbent assay. Our group consisted of 13 patients with sarcoidosis (7 sarcoidosis patients who received no treatment and 6 who received corticosteroid therapy) and 18 control subjects (11 healthy nonsmokers and 7 asymptomatic smokers). Type II (75-kDa), but not type I (55 kDa) sTNF-R in BALF was elevated significantly in patients with sarcoidosis compared with the healthy nonsmokers (type I: 126.7 ± 17.6 pg/ml BALF vs 79.4 ± 16.5 pg/ml BALF, p 〉 0.05; type II: 98.3 ± 27.8 pg/ml BALF vs 26.7 ± 4.9 pg/ml BALF, p 〈 0.05). Although levels of type I sTNF-R in BALF from sarcoidosis patients were not correlated with any cellular profiles of BALF, concentrations of type II correlated significantly with the numbers of lymphocytes in BALF. We concluded that sTNF-R is a normal constituent of the epithelial lining fluids and that levels of type II sTNF-R are elevated significantly in the BALF from individuals with sarcoidosis. This suggests that sTNF-Rs may influence the local bioactivity of TNF and may also contribute to the pathogenesis of sarcoidosis.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/PL00007566

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The in vitro and in vivo behavior of urokinase immobilized onto collagen-synthetic polymer composite material (1981)

Watanabe, S. ; Shimizu, Y. ; Teramatsu, T. ; [et al.]

Hoboken, NJ : Wiley-Blackwell

Journal of Biomedical Materials Research 15 (1981), S. 553-563

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ISSN: 0021-9304

Keywords: Chemistry ; Polymer and Materials Science

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine , Technology

Notes: With a view to developing biomaterials for semipermanent substitution, we have studied a composite material constituted with collagen and a synthetic polymer which possesses high tissue compatibility. This collagen - synthetic polymer composite was applied as a support for immobilization of enzymes for the purpose of providing a material surface with biological function. The enzymes, urokinase and trypsin, were successfully bound to the collagen membrane layer which had been activated by acyl azide formation of its carboxyl groups. The enzyme-bearing composite material showed excellent catalytic activity toward a protein substrate as well as a low-molecular-weight synthetic substrate. The immobilized urokinase was characterized enzymatically and compared with native urokinase. The apparent affinity of immobilized urokinase for the substrate was slightly decreased, but its intrinsic kinetic properties were not significantly affected. No decrease in its esterase activity was observed both on repeated use and on long-term storage, and its fibrinolytic activity was stable on heat or disinfection treatment. When this urokinase-bearing composite material was applied into rabbit blood vessels, its in vivo fibrinolytic activity was maintained. Thus, enzyme - collagen - synthetic polymer composites may find wide application for biomaterials and artificial organs as functional biomaterials.

Additional Material: 7 Ill.