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PubMed1965

Specific agglutination of tanned red cells coated with a globulin fraction of an antithyroid serum by saline extracts of thyroid glands.

Experiments are described in which tanned red cells coated with a globulin fraction of human serum with a high titre of antibody to human thyroglobulin were agglutinated by saline extracts of human thyroid gland and thyroglobulin but not by other tissue extracts. It is suggested that the linkage is due to a specific antigen antibody reaction between cell-bound antithyroid antibody and thyroglobulin in solution.

Autoantibodies↗
PubMed1996

Quantitation of five forms of high molecular weight angiotensinogen from human placenta.

In addition to the well characterized predominant form of plasma angiotensinogen, which will be termed low molecular weight angiotensinogen (LMrA), significant quantities of a high molecular weight angiotensinogen (HMrA) occur in the human pregnant state. HMrA is the predominant form of angiotensinogen in the placenta and amniotic fluid. The ratio of HMrA/LMrA is elevated in approximately half of the women who develop pregnancy induced hypertension (PIH). This report documents a simple two step methodology for the separation and quantitation of different forms of HMrA. The two steps are gel filtration and ion exchange chromatography. The application of this methodology to amniotic fluid and plasma from normotensive pregnant women and extracts of amnion, chorion, and placental tissue has shown five distinct forms in the tissue extracts and amniotic fluid, but only three significant forms in plasma. The elution position of all forms of HMrA are highly reproducible and are the same for each tissue or fluid studied, thus lending support to the concept that the three forms seen in plasma of normotensive pregnant women are the same as three of the forms of HMrA seen in extracts of placental tissue.

Angiotensinogen↗
PubMed1981

Tissue metabolism of estrogens in the female rhesus monkey.

The overall MCRs and [rho]BB values (fraction of infused precursor measured in blood as product) and individual tissue extractions and conversions were measured in the follicular and luteal phases of normal cycling female rhesus monkeys using constant infusions of [3H]estradiol ([3H]E2) and [14C]estrone ([14C]E1). During the infusions, blood samples were obtained from the femoral artery and veins draining the splanchnic tissue, kidney, head, arm, and uterus. The overall mean (+/- SE) MCR for E2 (214 +/- 17 liters/day) was significantly less than the MCR for E1 (295 +/- 13 liters/day). There were no differences in the MCR measured in the follicular or luteal phases of the cycle. The [rho]BB values were greater for the fraction of infused E1 measured in blood as product E2 [rho]E1, E2, BB; (0.25 +/- 0.02) than for [rho] E1, E2, BB (0.11 +/- 0.01). Neither value was affected by the time of the cycle. The extractions (that fraction of steroid measured in arterial blood entering a tissue which is metabolized and not measured as that steroid in venous blood draining the tissue) across the splanchnic tissues were the largest of the tissue extractions measured (0.63 +/- 0.05 for E2 and 0.73 +/- 0.10 for estrone). The arm, uterus, kidney, and head had lower extractions, and the extraction of E2 was always lower than that of E1, probably due to the specific globulin binding of E2. Interconversion of the estrogens occurred across each tissue bed but reflected, in general, only a small portion of the total extraction, especially for the splanchnic tissue. There was no apparent difference in any of the transtissue conversions measured in the follicular as compared to the luteal phase. The administration of pharmacological amounts of dexamethasone to three monkeys resulted in a marked increase in the MCR of estradiol and a slight decrease in the MCR of estrone. Individual tissue extractions and transtissue conversions showed no consistent alteration after dexamethasone.

Animals↗
PubMed1984

Characterization of plasminogen activators from normal human breast and colon and from breast and colon carcinomas.

Triton X-100 and NaSCN extracts of 18 normal breast and colon tissues and of 20 breast and colon carcinomas were fractionated by SDS-PAGE and plasminogen activators (PA) revealed by a zymographic method. Four different lysis bands, corresponding to MWs of 54,000, 68,000, 95,000 and 110,000 were observed. Using immunoadsorption with specific antisera against urokinase (UK) and tissue PA (t-PA), we found that all normal tissue extracts contained free t-PA (68 kd). Some of these revealed, in addition, a complex (110 kd) of t-PA with a 40-kd component. The latter presumably represents the fast-acting specific inhibitor of t-PA and UK. Most carcinoma extracts contained, in addition to the two t-PA-related lysis bands, the UK-related 54 kd PA, and some a 95 kd complex of UK with the 40 kd component. For each extractant, mean total fibrinolytic activity of normal and tumor tissue was comparable when measured on conventional fibrin plates, but breast and colon carcinomas contained higher concentrations of UK-related PA. PA activity was higher in normal and carcinoma NaSCN extracts than in the corresponding Triton X-100 extracts. In general, Triton X-100 but not NaSCN extracts of malignant tissue contained a high concentration of fibrinolytic inhibitors. Mixing experiments revealed that the inhibitory activity was mainly directed against UK. It was abolished by acidification of the carcinoma extracts. The anti-UK inhibitory activity was absent in extracts of normal breast or colon and appears to be different from the 40 kd fast-acting PA inhibitor. These studies show that malignant transformation of breast and colon is accompanied by important changes of the production of a UK-related PA and of an inhibitory activity directed against UK.

Breast↗
PubMedDate not supplied

Growth stimulating activity of lung extract on lung-colonizing colon 26 clones and its partial characterization.

The effects of lung tissue extract on the cell growth of eight colon 26 tumor clones, four highly and four poorly lung-colonizing clones, were examined in vitro. Addition of lung extract to serum-free medium stimulated the growth of all four of the highly lung-colonizing clones and one of the poorly lung-colonizing clones, but it had minimal effect on the other three poorly lung-colonizing clones. These results indicate that the lung extract contains a growth stimulating activity; it selectively stimulated some of the colon 26 clones including highly lung-colonizing ones. The growth stimulating activity was not dialyzable, was partially destroyed by heating at 56 degrees C or 80 degrees C for 30 min and completely destroyed by trypsin. These results suggest that the activity resides in a protein. Gel filtration chromatography of lung extract on Sephacryl S-200 revealed that the active component was eluted in a molecular weight range of 90,000-120,000.

Animals↗
PubMed1977

Structural similarities between a protein extracted from normal human tissues and a component of amyloid fibrils.

Comparative immunologic and chemical studies of crude or fractionated amyloid fibrils and materials obtained from corresponding normal tissues have been performed. Materials from the amyloidotic and normal tissues were subjected to identical methods of extraction, chemical treatment and protein fractionation. Antigenic similarities between crude amyloid fibrils and corresponding normal tissue extracts were observed, however, a considerably larger concentration of the latter antigens was needed to obtain immunologic reactivity in double diffusion in gel. Striking similarities were observed when the amino acid composition of a high molecular weight subcomponent of amyloid fibrils was compared with that of normal tissue extracts. Crude, intact amyloid fibrils were highly effective in absorbing Congo-red while the ability to absorb Congo-red was by far less if the high molecular weight subcomponent of amyloid fibrils as well as the corresponding normal tissue extracts were used. The high molecular weight subcomponent of amyloid, which seems to be an integral part of the amyloid fibrils, most probably is a protein derived from normal tissue.

Adult↗
PubMed1992

Characterization of parathyroid hormone-related protein in the human term placenta.

To characterize parathyroid hormone-related protein (PTHrP) in the human placenta, we measured PTHrP-like immunoreactivity (PRP-LI) in the term placenta and studied the elution profiles of placental tissue extracts on Sephadex G-75 chromatography with a specific RIA. We also examined the gene expression of PTHrP mRNA by Northern blot analysis and the localization of PRP-LI in the placenta by immunohistochemistry. The amount of PRP-LI in placental extracts (n = 7) was 20.9 +/- 2.2 pg/g wet tissue (mean +/- SE). Dilution curves of placental tissue ran parallel to those of synthetic PTHrP (1-34) standards. Sephadex G-75 gel chromatography demonstrated two major PRP-LI peaks; the first peak was eluted around the molecular size between 10 kilodaltons (Kda) and 20 Kda and the other around 5 Kda. Northern blot analysis of PTHrP mRNA extracted from placental tissues showed a major hybridization signal around 18S. PTHrP immunohistochemistry showed PRP-LI staining in the cytoplasm of syncytiotrophoblasts and stroma cells (Hofbauer cells) in the term placenta. These results suggest that syncytiotrophoblasts and stroma cells in the term placenta synthesize PTHrP in two major molecular forms, 10 Kda-20 Kda and around 5 Kda.

Adult↗
PubMed1982

Distribution of 13N following intravenous injection of [13N]ammonia in the rat.

Ammonia labeled with cyclotron-produced 13N was injected intravenously in rats and the content of 13N in 14 major organs and tissues was determined at eight intervals ranging from 0.2 to 50 min after injection. The distribution of 13N at 12 s was employed to estimate the unidirectional tissue extraction for ammonia. The estimated fractional extraction for most of the tissues studied ranged from 70 to 100%. The 12-s 13N concentrations in a number of tissues (with lungs and brain the principal exceptions) were found to be quite similar to those reported for 42K+ and 86Rb+ in the rat, suggesting a similar mechanism to transcapillary extraction. Most of the injected dose was initially extracted by the musculature, lungs, and kidneys. The lungs and kidneys released the bulk of their extracted ammonia-derived nitrogen within 10 min of injection. The gut, heart, and spleen also recirculated extracted nitrogen, but on a much smaller scale than the lungs and kidneys. The recirculated label was accumulated mainly by muscle, liver, and skin. The results suggest that the lungs and kidneys are important sources of systemically recirculated ammonia metabolites in the rat.

Ammonia↗
PubMed1982

Tetrodotoxin-sensitive protein in the extracts from excitable tissues.

The sodium permeability of liposomes preincubated with the soluble fraction of brain and heart muscle homogenates was increased veratrine. The veratrine increment was decreased by tetrodotoxin. The effect was specific for the extracts from excitable tissues. Bovine serum and soluble fraction of liver homogenate induced neither veratrine- nor tetrodotoxin-sensitivity of the liposomes. Treatment of the excitable tissue extracts by pronase and heat denaturation caused their complete inactivation. Tetrodotoxin-sensitive factor could be fractionated by ammonium sulfate precipitation and by DEAE-Servacel chromatography. On a column of Sephadex G-200 it was eluted with the void volume. It is suggested that the tetrodotoxin-sensitive factor is a protein which could be a soluble precursor of the voltage-dependent sodium channels.

Animals↗
PubMed1995

Analysis of tilmicosin in swine liver extracts by liquid chromatography/atmospheric pressure chemical ionization mass spectrometry.

Tilmicosin is a semisynthetic macrolide antibiotic used in the treatment of respiratory disease in cattle and swine. The technique of liquid chromatography/atmospheric pressure chemical ionization mass spectrometry (LC/APCI-MS) was employed in an on-line capacity for the analysis of tilmicosin in extracts from spiked swine liver. Increasing the potential in the cone/skimmer region of the ion source resulted in an increased abundance of unique structurally indicating fragment ions of tilmicosin. Three ions, [M+H]+ and two diagnostic fragment ions were chosen for confirmation of the presence of tilmicosin in swine liver tissue extracts using the mass spectrometer in selected-ion monitoring mode. The ion abundance ratios arising from any given combination of ions in data acquired from extracts of swine liver tissue spiked with tilmicosin at 5 and 10 ppm were within +/- 10% of the corresponding mean standard abundance ratio, and duplicate sample analyses exhibited < 10% relative standard deviation. These results suggest the potential for the application of LC/APCI-MS as a confirmatory technique for tilmicosin in swine liver.

Animals↗
PubMed1986

ATP- and coenzyme A-dependent fatty acid incorporation into proteins of cell-free extracts from mouse tissues.

The incorporation of tritiated fatty acids into proteins has been studied in cell-free extracts from mouse tissues. Incubation of heart extracts with [3H]tetradecanoic or [3H]palmitic acid in the presence of ATP and CoA resulted in the time-dependent and selective labeling of proteins (Mr = 60,000, 47,000, 42,000, 31,000, 16,000, and 13,000) which could be detected after sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Two polypeptides (Mr = 47,000 and 42,000) reached a maximum in fatty acid incorporation very rapidly and were mainly localized in the membrane subcellular fractions of the extract. These proteins underwent transient labeling with [3H] tetradecanoyl-CoA, the maximum incorporation being obtained within 1 min. The fatty acid-labeled proteins from tissue extracts had the same properties as other proteins known to be acylated in intact cells, i.e. the acyl moiety was resistant to delipidation with organic solvents but could be hydrolyzed by treatment with neutral hydroxylamine. Screening of different tissues showed that extracts from liver and kidney also catalyze the ATP- and CoA-dependent formation of a similar group of fatty acid-acylated proteins. The results provide evidence for a group of proteins in mammalian tissues which selectively incorporate fatty acids in vitro and should be of value for further studies on the biosynthesis of acylated proteins.

Adenosine Triphosphate↗
PubMed1994

Effect of pyridine and its methylated derivatives on storage by rat pineal nerves of monoaminergic neurotransmitter.

In previous work of our laboratory, it was demonstrated that collidine (2-4-6-trimethylpyridine) applied briefly to fresh tissues extracted noradrenaline or closely related compound/s of neuronal origin. This effect gave rise to the abolition of osmiophilia and chromaffin reaction of electron-dense cores of monoaminergic synaptic vesicles and to the extraction of radioactive compounds in tissues that had previously taken up tritiated noradrenaline. In this work, the role of the pyridine ring and its progressive methylation on the monoamine releasing effect was investigated. For this purpose, the effect of pyridine, two picolines (2 and 4 monomethylpyridines) and a lutidine (2-6-dimethylpyridine) was compared to the effect of collidine. It was found that pyridine has a much smaller effect than collidine on the histochemical reactivity of monoaminergic synaptic vesicles and on the extraction of tritiated compounds and that its extent was dependent upon the number of methyl groups incorporated in the pyridine ring.

Animals↗
PubMed1990

31P NMR of phospholipid glycerol phosphodiester residues.

Saponification of extracted tissue phospholipids yields a set of isolated glycerol 3-phosphoryl phospholipid polar headgroups from which semi-quantitative 31P NMR spectra can be obtained. The resonance signals from these molecules, which frequently have been reported as uncharacterized phosphate signals observed in perchloric acid extracts of tissue, can be used as an aid in the characterization of isolated phospholipids and of tissue phospholipid 31P NMR profiles. 31P NMR chemical-shift values of the resonances at pH 7 in water and relative to 85% phosphoric acid are: glycerol 3-phosphocholine (-0.13 delta), glycerol 3-phosphoethanolamine (0.42 delta), glycerol 3-phospho(monomethyl)ethanolamine (0.29 delta), glycerol 3-phospho(dimethyl)ethanolamine (0.16 delta), glycerol 3-phosphoserine (0.14 delta), glycerol 3-phosphoinositol (-0.07 delta), glycerol 3-phosphoglycerol (0.92 delta), bis(glycerol 3-phospho)glycerol (0.79 delta), serine ethanolamine phosphodiester (-0.46 delta), glycerol 3-phosphate (0.60 delta; 4.29 delta at pH 10) glycerol 2-phosphate (0.15 delta; 3.92 delta at pH 10). In addition, analysis of extracted cancer tissue phospholipid samples yielded a new and uncharacterized polar headgroup fragment with a chemical-shift value of 0.29 delta that is independent of sample pH.

Animals↗
PubMed1965

ORGAN SPECIFICITY AND LACTATE-DEHYDROGENASE ACTIVITY. DIFFERENTIAL INHIBITION BY UREA AND RELATED COMPOUNDS.

1. The effect of urea on the lactate-dehydrogenase activities of human-heart and -liver tissue extracts and on crystalline ox-heart and rabbit-muscle enzyme have been determined. Similar studies on electrophoretically separated isoenzyme fractions have shown an inverse relationship between sensitivity to urea inhibition and electrophoretic mobility. 2. With pyruvate as substrate a sharp change in the nature of the inhibition of tissue lactate dehydrogenase with increasing concentrations of urea occurs at 1 m or 4 m with the electrophoretically slow and fast isoenzymes respectively. 3. At concentrations of urea less than 1 m, inhibition of the purified enzymes is competitive with respect to pyruvate and 2-oxobutyrate. 4. Similar studies have been carried out with methylurea and hydantoic acid, both of which are more potent inhibitors than urea.

Animals↗
PubMed1988

Oxidation of indole-3-acetic acid to oxindole-3-acetic acid by an enzyme preparation from Zea mays.

Indole-3-acetic acid is oxidized to oxindole-3-acetic acid by Zea mays tissue extracts. Shoot, root, and endosperm tissues have enzyme activities of 1 to 10 picomoles per hour per milligram protein. The enzyme is heat labile, is soluble, and requires oxygen for activity. Cofactors of mixed function oxygenase, peroxidase, and intermolecular dioxygenase are not stimulatory to enzymic activity. A heat-stable, detergent-extractable component from corn enhances enzyme activity 6- to 10-fold. This is the first demonstration of the in vitro enzymic oxidation of indole-3-acetic acid to oxindole-3-acetic acid in higher plants.

Indoleacetic Acids↗
PubMed1998

Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms.

Elastolytic matrix metalloproteinases (MMPs) have been implicated in the pathogenesis of abdominal aortic aneurysms (AAA), a disorder characterized by chronic aortic wall inflammation and destruction of medial elastin. The purpose of this study was to determine if human macrophage elastase (HME; MMP-12) might participate in this disease. By reverse transcription-polymerase chain reaction, HME mRNA was consistently demonstrated in AAA and atherosclerotic occlusive disease (AOD) tissues (six of six), but in only one of six normal aortas. Immunoreactive proteins corresponding to proHME and two products of extracellular processing were present in seven of seven AAA tissue extracts. Total HME recovered from AAA tissue was sevenfold greater than normal aorta (P < 0.001), and the extracted enzyme exhibited activity in vitro. Production of HME was demonstrated in the media of AAA tissues by in situ hybridization and immunohistochemistry, but HME was not detected within the media of normal or AOD specimens. Importantly, immunoreactive HME was specifically localized to residual elastin fragments within the media of AAA tissue, particularly areas adjacent to nondilated normal aorta. In vitro, the fraction of MMP-12 sequestered by insoluble elastin was two- to fivefold greater than other elastases found in AAA tissue. Therefore, HME is prominently expressed by aneurysm-infiltrating macrophages within the degenerating aortic media of AAA, where it is also bound to residual elastic fiber fragments. Because elastin represents a critical component of aortic wall structure and a matrix substrate for metalloelastases, HME may have a direct and singular role in the pathogenesis of aortic aneurysms.

Aortic Aneurysm, Abdominal↗
PubMed1975

Specificity of elevated serum MB creatine phosphokinase activity in the diagnosis of acute myocardial infarction.

Creatine phosphokinase (CPK) isoenzyme determinations are useful in the diagnosis of myocardial infarction. However, until suitably sensitive and precise quantitative procedures became available, the diagnostic specificity of serum CPK isoenzyme elevations could not be thoroughly examined. In this study an assay procedure capable of accurately determining activity of individual CPK isoenzymes even in serum samples with normal total CPK activity was employed to obtain two types of information. First, CPK isoenzyme profiles were examined in extracts of a spectrum of human tissues obtained at operation to determine whether the isoenzyme associated with myocardium is presented in other human tissues in quantities sufficient to produce increased activity in serum. In addition, CPK isoenzymes were analyzed quantitatively in serial serum samples from 50 hospitalized control subjects, 100 patients with acute myocardial infarction, 100 patients undergoing non-cardiac surgery and 50 patients undergoing cardiac catheterization to determine whether insult to tissues other than the heart is associated with increased "myocardial" CPK isoenzyme activity in serum. Results from analyses of tissue extracts indicated that myocardium is the only tissue surveyed containing sufficient MB CPK to account for substantial increases in serum MB activity. Results from analyses of serial serum samples indicated that MB CPK activity levels are consistently elevated after myocardial infarction, averaging 0.089 IU/ml. However, after cardiac cathetrization or noncardiac surgery peak serum MB activity remains low, averaging only 0.004 IU/ml despite marked elevations in total serum CPK activity. Thus, elevated serum MB CPK activity is a highly specific as well as sensitive criterion of myocardial injury.

Acute Disease↗
PubMed1997

Reversible sedimentation and masking of nerve growth factor (NGF) antigen by high molecular weight fractions from rat brain.

Nerve growth factor (NGF) was recently found to be largely associated with sedimentable fractions of adult rat brain and treatments of the fractions by alkaline pH increased the measurable amount of their NGF antigen as well as its solubilization [M.C. Hoener, E. Hewitt, J.M. Conner, J.W. Costello and S. Varon, Nerve growth factor (NGF) content in adult rat brain tissues is several-fold higher than generally reported and is largely associated with sedimentable fractions, Brain Res., 728 (1996) 47-56; M.C. Hoener and S. Varon, Effects of sodium chloride, Triton X-100, and alkaline pH on the measurable contents and sedimentability of the nerve growth factor (NGF) antigen in adult rat hippocampal tissue extracts, J. Neurosci. Res., in press (1997); C. Zettler, D.C.McL. Bridges, X.-F. Zhou and R.A. Rush, Detection of increased tissue concentrations of nerve growth factor with improved extraction procedure, J. Neurosci. Res., 46 (1996) 581-594]. We have further investigated the reversibility of these pH effects. Reversal of the pH of an adult rat hippocampal tissue extract from 10.5 to 7.4 led to an almost complete transfer of NGF back from nonsedimentable to sedimentable fractions and to a remasking of the previously unmasked portion of NGF antigen. Thus, molecules causing masking and sedimentation of NGF at pH 7.4 were likely to be present in the alkaline extract. A gel filtration column in PBS, pH 10.5 was used to separate such putative binding molecules from the NGF. All of the NGF antigen from rat hippocampal alkaline extract was found to elute with 19 kDa fractions. The same apparent molecular weight was found for mouse submaxillary beta-NGF and recombinant human beta-NGF. Masking and sedimentation no longer occurred when newly generated 19 kDa rat brain NGF was returned to pH 7.4. When high molecular weight fractions derived from the same gel filtration (in PBS, pH 10.5) were added back to the 19 kDa NGF pool at pH 7.4 and the mixture incubated and centrifuged, the measurability of 19 kDa rat brain NGF antigen was markedly reduced and half of the antigen was recovered in sedimentable fractions. Similar but less dramatic results were obtained when mixing the same high molecular weight fractions with 19 kDa mouse or human beta-NGF. These findings provide new opportunities to identify molecules to which NGF may be bound within intact brain tissues.

Animals↗