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PubMed1997

The concentration of u-PA and PAI-1 antigen in tissue extracts of nasopharyngeal carcinoma.

We measured the antigen levels of urokinase-type plasminogen activator (u-PA) and plasminogen activator inhibitor-1 (PAI-1) in tissue extracts from nasopharyngeal carcinomas. An increase in u-PA antigen was observed with the advanced stages of disease. However, the levels of PAI-1 antigen decreased with each advanced stage. These results suggest that local administration of antiplasminic agents may be effective in suppressing tumor invasion.

Adult↗
PubMed1985

Cultivation of free-living stages of Trichostrongylus colubriformis in media without bacteria, animal tissue extract, or serum.

Trichostrongylus colubriformis was cultured from hatched first-stage to third-stage larvae in bacteria-free media in the absence of animal tissue extract or serum. This was achieved for the first time with a nematode, parasitic in vertebrates, whose rhabditiform larvae are food-dependent. The best media contained enzymatic hydrolysed casein (amino nitrogen:total nitrogen ratio 0.39), yeast extract, phosphatidylcholine from soybean, and a number of chemically defined ingredients, which include a salt solution, a sterol, and an iron porphyrin. The yield of third-stage larvae obtained was up to 17% of all the living larval stages present after incubation. When casein hydrolysate with AN:TN ratio of 0.39 was replaced by casein hydrolysate with AN:TN ratio of 0.53, little or no development to third-stage larvae occurred. Development to infective larvae was shown to be possible in media with soy peptone instead of casein hydrolysate, although to a very limited extent. It is proposed that the free-living stages of the parasite require peptides, whose molecular weights all lie within a narrow range.

Animals↗
PubMed1987

Abnormal n-nonacosane storage in humans: detection by gas chromatography/mass spectrometry of tissue extracts.

We report a case of n-nonacosane storage disease, which went undiagnosed until the death of a 55-year-old farmer. Clinical, histological, and biochemical features are discussed. n-Nonacosane storage was identified by gas chromatographic-mass spectrometric analysis of different tissue extracts, n-nonacosane concentration reaching 1.2 mg g-1 of lung tissue and 0.32 mg g-1 of liver tissue. It was possible to rule out a work-induced intoxication, and n-nonacosane storage appeared to be accounted for by a lifelong, heavy consumption of unpeeled apples and Brussels sprouts.

Alkanes↗
PubMed1987

Levels of glycerate 2,3-P2, 2,3-bisphosphoglycerate synthase and 2,3-bisphosphoglycerate phosphatase activities in rat tissues. A method to quantify blood contamination of tissue extracts.

The levels of glycerate 2,3-P2 and of 2,3-bisphosphoglycerate synthase and 2,3-bisphosphoglycerate phosphatase activities have been determined in isolated rat hepatocytes and adipocytes and in perfused rat tissues to discard blood contamination. The values obtained are much lower than those previously reported, ranging 0.50-40 nmol/g tissue. No relationship appears to exist between glycerate 2,3-P2 concentration and the levels of the enzymatic activities involved in glycerate 2,3-P2 metabolism. Assay of glycerate 2,3-P2 in tissue extracts constitute a very useful way to quantify blood contamination.

2,3-Diphosphoglycerate↗
PubMed1995

Detection and quantitation of phosphorus metabolites in crude tissue extracts by 1H and 31P NMR: use of gradient assisted 1H-31P HMQC experiments, with selective pulses, for the assignment of less abundant metabolites.

The analysis of crude tissue extracts by NMR has proven to be of use in the study of metabolism due to the non-destructive and non-selective character of the technique. Lists of 1H and 31P NMR assignments of phosphorus metabolites in water solution at specified pH and ionic composition are of large general value but their usefulness may be limited when analysing complex mixtures of metabolites at low concentrations. In this work we report on the use of gradient-assisted proton detected multiple quantum 1H and 31P coherence experiments with selective pulses for the rapid and unambiguous assignments of some crowded regions in 1H and 31P spectra of crude extracts from rat liver. The amplitudes of the gradient episodes were calibrated to optimize the coherence transfer pathway between proton and phosphorus, and the delay for the evolution of the long-range coupling was calculated from values of 3JPH and 4JPH ranging from 1.4 to 7.5 Hz. Moreover, a selective 90 degrees Gaussian pulse on the 31P channel was introduced to increase the resolution in the F1-domain and make the method even faster. The procedure was then applied to unambiguously assign the ID 31P and 1H spectra of perchloric acid extracts of rat livers that had been stimulated with phenylephrine, dBcAMP and glucagon and thus detect changes in the concentration of less abundant metabolites such as phosphoenolpyruvate, UDP-glucose and AMP. The fact that the quantification of these metabolites by either 31P and 1H methods lead to different results is discussed, and the use of 1H NMR spectroscopy for the quantification of phosphorus metabolites whose signal are too weak or poorly resolved in a 31P spectrum is proposed.

Adenosine Monophosphate↗
PubMed1995

Urokinase receptor in breast cancer tissue extracts. Enzyme-linked immunosorbent assay with a combination of mono- and polyclonal antibodies.

Urokinase plasminogen activator (uPA) is a proteolytic enzyme involved in degradation of the extracellular matrix during cancer invasion. The levels of uPA and its inhibitor PAI-1 in tumor extracts have previously been demonstrated to be of prognostic value in breast cancer as well as other types of cancer. We have previously characterized a specific cell surface receptor for uPA (uPAR) which strongly enhances the catalytic activity of uPA and is expressed during mammary cancer invasion. In order to quantitate uPAR in breast cancer tissue, we have now developed a sensitive enzyme-linked immunosorbent assay (ELISA), with polyclonal catching antibodies and three monoclonal detecting antibodies. The detection limit of the assay is approximately 0.16 fmol of uPAR in a volume of 100 microliters (1.6 pM). There is a linear relationship between signal and uPAR concentration up to at least 6.6 fmol per 100 microliters (66 pM). Both free uPAR and uPAR in complex with uPA is detected. The recovery of an internal uPAR standard in breast cancer tissue extracts is above 87%. The intra-assay and inter-assay variation coefficients are 7% and 13%. In order to find a suitable buffer for extraction of various components of the uPA-system from breast cancer tissue, we tested buffers which previously have been used for optimal extraction of estrogen receptor (A), uPA (B), and uPAR (C). Buffer A and B extracted approximately 30% and 50%, respectively, of the amount of uPAR extracted with buffer C.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1987

Characterization of autoantigens relevant to autoimmune ophthalmitis and thyroiditis in mice immunized with the syngeneic tissue extracts and Klebsiella O3 lipopolysaccharide.

The histological localization and biochemical properties of the autoantigens relevant to experimental autoimmune ophthalmitis and thyroiditis were studied using sera from mice hyperimmunized with the corresponding tissue extract of syngeneic mice and Klebsiella O3 lipopolysaccharide (KO3 LPS) as a potent adjuvant. Specific antigens were detected in the lens of the eyeball by immunofluorescence test with sera from mice in which ophthalmitis had been induced and the antigens were lenticular proteins with molecular weights (MW) of 15,000 (15K) to 25K, and 45K. The lenticular proteins with MW of 15K to 25K correspond to the subunits of crystalline. These findings clearly demonstrated that our experimental model for autoimmune ophthalmitis was classified as the lens-induced uveitis. The colloids of the thyroid follicles and the follicular cells were markedly stained by sera from mice in which thyroiditis had been induced. One of the autoantigens detected in the thyroid gland was biochemically consistent with a thyroglobulin subunit. It was also shown that these autoantigens detected in the present study were organ-specific but not species-specific. The nature of autoantigens in the eye and the thyroid gland is discussed.

Animals↗