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PubMed1997

Effects of the hydroxamic acid derivate Ro 31-4724 on the metabolism and morphology of interleukin-1-treated cartilage explants.

Matrix metalloproteinases (MMPs) belong to the key enzymes of the proteolytic destruction of cartilage matrix during chronic rheumatic diseases. Our work focused on the inhibitory potential of the hydroxamate Ro 31-4724 on the activity of MMP-proteoglycanases as well as on the viability, morphology and proteoglycan metabolism of interleukin-1 (IL-1)-treated bovine articular cartilage explants. The in vitro activity of MMP-proteoglycanases as well as the release of proteoglycans from IL-1-treated cartilage explants were significantly and concentration-dependently inhibited by Ro 31-4724 tested at concentrations ranging from 1 nmol/l to 10 mumol/l. Histopathological evaluation of sections from cartilage explants treated with this drug revealed no microscopically discernible alterations, and did not show any cytotoxic effects of Ro 31-4724. In addition, Ro 31-4724 had no effect on the rate of proteoglycan biosynthesis by IL-1-treated cartilage explants and increased the percentage of newly synthesized proteoglycans to form macromolecular aggregates. In conclusion, Ro 31-4724 displayed MMP-proteoglycanase inhibitory activity both in vitro and ex vivo and proved to be not harmful to the morphology, viability and proteoglycan biosynthesis of bovine articular cartilage explants.

Animals↗
PubMed1979

Colorimetric determination of penicillins and related compounds in intravenous solutions by nickel (II)-catalyzed hydroxamic acid formation.

Solutions of ampicillin, carbenicillin, methicillin, oxacillin, penicillin G, and cephalothin in 5% dextrose were analyzed by nickel(II)-catalyzed hydroxylaminolysis. The reactions of these antibiotics were complete within 20 min at room temperature. Under the analytical conditions, molar absorptivities of the ferric-hydroxamate complexes ranged from 830 to 1005 liters/mole/cm. Coefficients of variation for the analysis of these antibiotics in 5% dextrose were typically less than 3% at concentrations of 1 mg/ml. Oxacillin was analyzed by the same method in normal saline and/or lactated Ringer solutions. The method also was applied to the analysis of chloramphenicol in aqueous solutions. Only ampicillin showed a significant decrease in concentration in 48 hr.

Catalysis↗
PubMed1983

Use of pentachlorophenol as long-term inhibitor of sulfation of phenols and hydroxamic acids in the rat in vivo.

Inhibition of sulfation of the phenolic compound harmol (7-hydroxy-1-methyl-9H-pyrido[3,4-b]indole) by pentachlorophenol (PCP) was studied in the Wistar rat: PCP was administered in various ways to find a convenient method for long-term inhibition of sulfation. High doses of PCP or sodium pentachlorophenolate (NaPCP) in the diet (350 ppm) or NaPCP in the drinking water (1.4 mM) of Wistar rats for one week inhibited the sulfation of harmol by 30-45%. The plasma concentration of PCP in rats with NaPCP (1.4 mM) in their drinking water was highest (270 microM) in the period that the animals were kept in the dark and consumed food and water. This is explained by a rapid elimination: the elimination of PCP from plasma, after intravenous administration, showed a biphasic disappearance curve with half-lives of 2.17 and 7.24 hrs, respectively. This is much faster than in Sprague-Dawley rats. A log-linear correlation was found between the plasma concentration of pentachlorophenol and the inhibition of harmol sulfation. Although administration of NaPCP to rats in their drinking water inhibited the sulfation of harmol only by 45%, it inhibited the sulfation of the carcinogenic arylhydroxamic acid N-hydroxy-2-acetylaminofluorene by 70-75%.

Animals↗