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PubMed2002

Sentinel node mapping for colorectal cancer with radioactive tracer.

PURPOSE: The aim of this study was to test the feasibility and accuracy of radioactivity-guided mapping of the first lymph nodes found in draining the primary tumor site for colorectal cancer. METHODS: We enrolled 56 consecutive patients with preoperative diagnosis of curatively resectable colorectal cancer. Endoscopic injection of technetium Tc 99m-labeled tin colloid (15 MBq) was performed preoperatively, and radioactive sentinel nodes were identified intraoperatively with a gamma probe. Standard radical resection with lymph node dissection was performed in all patients, and all resected nodes were evaluated by routine histopathologic examination. RESULTS: Radioactivity-guided methods were used to detect sentinel nodes in 51 (91 percent) of 56 patients. The number of lymph nodes resected was 23.9 +/- 15.2 per case. The number of sentinel nodes was 3.5 +/- 2.1 (range, 0-8) per case. In 18 of 22 patients with lymph node metastasis, the sentinel node was positive. The incidence of metastasis in the sentinel node (22 percent) was significantly higher than that in nonsentinel nodes (3 percent, P < 0.01). Diagnostic accuracy according to sentinel node status was 92 percent (47/51). Four false-negative cases in this study were advanced cases with T3 primary tumors. The detection rate and diagnostic accuracy for patients with T1 or T2 primary tumors (29 cases) were 100 percent each. CONCLUSION: Intraoperative radioactivity-guided sentinel node mapping was accurate for patients with colorectal cancer with T1 or T2 tumors. The results suggest that sentinel node mapping and intraoperative biopsy may be a sensitive and specific diagnostic method for detecting metastasis in regional lymph nodes in patients with colorectal cancer.

Adult↗
PubMed1984

The use of radioactive cysteine methyl ester for labeling glycosylated molecules oxidized by periodate or neuraminidase plus galactose oxidase.

Treatment of rat lymph node cells with periodate or neuraminidase plus galactose oxidase initiates blast transformation and cell division of T lymphocytes. Either treatment introduces aldehyde functions onto glycosylated molecules of the plasma membrane. Reduction of the aldehydes with borohydride leads to a concentration-dependent inhibition of the mitogenic response. Cysteine methyl ester (Cys(Me], which can form a stable thiazolidine adduct with aldehydes, also inhibits mitogenesis in a concentration-dependent manner. Maximum inhibition is achieved at Cys(Me) concentrations about 10-fold lower than those required for borohydride (0.4 and 5 mM, respectively). [35S]Cys(Me) has been synthesized and compared with [3H]borohydride as a labeling reagent for molecules on the plasma membrane oxidized by periodate or neuraminidase plus galactose oxidase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of labeled whole cell lysates or of crude membrane fractions prepared from labeled cells revealed that the same oxidized molecules are specifically labeled with both reagents. Homogenates of cells labeled with either radioactive reagent were fractionated by differential and isopycnic centrifugation. The fractions were analyzed for radioactivity and for a number of marker constituents localized in various subcellular organelles. Following treatment with either reagent, the radioactivity that was covalently incorporated into macromolecules was primarily associated with sedimentable components that distributed among the fractions like plasma membrane markers. When compared with [3H]borohydride, Cys(Me) offers several advantages as a surface labeling reagent for glycosylated plasma membrane molecules, chiefly the possibility of preparing reagents labeled with isotopes other than tritium, including those like 35S, which are much stronger radioactive emitters.

Animals↗
PubMed1988

Labeling of porphobilinogen deaminase by radioactive 5-aminolevulinic acid in isolated developing pea chloroplasts.

A protein had been previously described, which was labeled by radioactive 5-aminolevulinic acid in isolated developing chloroplasts. In the present study we have shown that this protein (Mr approximately equal to 43,000) probably exists as a monomer in the chloroplast stroma. The labeling is blocked if known inhibitors of 5-aminolevulinic acid dehydratase are added to the incubation mixture, and is markedly decreased in intensity if nonradioactive 5-aminolevulinate or porphobilinogen are added to the incubation mixture; other intermediates in the porphyrin biosynthetic pathway, uroporphyrinogen III, uroporphyrin III, and protoporphyrin IX, do not decrease the labeling of the 43-kDa protein appreciably. Nondenaturing gels of the proteins isolated from the incubation with radioactive 5-aminolevulinic acid were stained for porphobilinogen deaminase activity. A series of red fluorescent bands was obtained which coincided with the radioactive bands visualized by autoradiography. It is concluded that the soluble chloroplast protein that is labeled in organello by radioactive 5-aminolevulinic acid is porphobilinogen deaminase.

Aminolevulinic Acid↗
PubMed1992

CDP-choline: 1,2-diacylglycerol cholinephosphotransferase from rat liver microsomes. II. Photoaffinity labeling by radioactive CDP-choline analogs.

Photoaffinity labeling of cholinephosphotransferase from rat liver microsomes directly by its substrate, [32P]CDP-choline or by a synthetic photoreactive CDP-choline analog, 3'(2')-O-(4-benzoyl)benzoyl [32P]CDP-choline (BB-[32P]CDP-choline), was examined for the possible identification of its molecular form on subsequent SDS-PAGE followed by 32P-autoradiography. When the partially purified cholinephosphotransferase was photoirradiated in the presence of [32P]CDP-choline, a considerable amount of 32P-radioactivity was incorporated into the TCA-insoluble component. This incorporation was dependent on irradiation time, Mg2+ or Mn(2+)-requiring and inhibited strongly by the presence of Ca2+. Either CDP-choline or CDP-ethanolamine inhibited the ultraviolet irradiation-dependent incorporation of 32P-radioactivity into the TCA-insoluble component in a dose-dependent manner, whereas neither phosphocholine or 5'-CDP had any effect on this process. These results strongly suggested that the observed 32P-incorporation from [32P]CDP-choline into the protein component could be a consequence of the covalent interaction between cholinephosphotransferase and its substrate, [32P]CDP-choline. Two polypeptides, 25 kDa and 18 kDa, with high 32P-radioactivity were clearly identified on a SDS gel after the direct photoaffinity labeling with [32P]CDP-choline for more than 5 min of ultraviolet irradiation. On the other hand, when BB-[32P]CDP-choline was used as a photoaffinity ligand, a single polypeptide with apparent molecular size of 55 kDa could be rapidly photolabeled within 2.5 min, then this band gradually lost its 32P-radioactivity with increasing time of ultraviolet irradiation. Thus, the overall results strongly indicated that cholinephosphotransferase in rat liver microsomes exists most likely as a 55 kDa polypeptide (or subunit) and that 25 kDa and 18 kDa peptides identified after the direct photoaffinity labeling with [32P]CDP-choline were probably the photo-cleavage products of cholinephosphotransferase during the prolonged ultraviolet irradiation, both of which could contain the catalytic domain of the original enzyme protein(s).

Animals↗
PubMed1985

Peptide mapping of the insulin-binding site of the 130-kDa subunit of the insulin receptor by means of a novel cleavable radioactive photoprobe.

A radioactive photoaffinity probe for the insulin receptor was prepared by derivatizing insulin at its B29 lysine with a novel crosslinking reagent having a cleavable azo linkage. Insulin receptors purified from human placental membranes were photoaffinity labeled with this probe. The photolabeled receptor was treated with dithionite to cleave the azo linkage, thereby removing the insulin ligand and transferring the radioactivity to the receptor protein. The radioactive labeled subunit was isolated and digested with elastase for peptide mapping and separation by high performance liquid chromatography. Results obtained indicated that it will be feasible to use this new photoaffinity probe to obtain radioactive peptides representing the insulin-binding site(s) on the receptor subunit.

Affinity Labels↗
PubMed1978

Regeneration of motor axons in the rat sciatic nerve studied by labeling with axonally transported radioactive proteins.

Labeling regenerating axons with axonally transported radioactive proteins provides information about the location of the entire range of axons from the fastest growing ones to those which are trapped in the scar. We have used this technique to study the regeneration of motor axons in the rat sciatic nerve after a crush lesion. From 2 to 14 days after the crush the lumbar spinal cord was exposed by laminectomy and multiple injections of [3H]proline were made stereotactically in the ventral horn. Twenty-four hours later the nerves were removed and the distribution of radioactivity along the nerve was measured by liquid scintillation counting. There was a peak of radioactivity in the regenerating axons distal to the crush due to an accumulation of label in the tips of these axons. After a delay of 3.2 +/- 0.2 (S.E.) days, this peak advanced down the nerve at a rate of 3.0 +/- 0.1 (S.E.) mm/day. The leading edge of this peak, which marks the location of the endings of the most rapidly growing labeled fibers, moved down the nerve at a rate of 4.4 +/- 0.2 mm/day after a delay of 2.1 +/- 0.2 days; this is the same time course as that of the most rapidly regenerating sensory axons in the rat sciatic nerve, measured by the pinch test. Another peak of radioactivity at the crush site, presumed to represent the ends of unregenerated axons or misdirected sprouts, declined rapidly during the first week, and more slowly thereafter.

Animals↗
PubMed1981

Retrograde transport of radioactivity along axons of ascending cerebellar pathways after injection of N-[3H]acetyl-D-mannosamine into the mesencephalon of the rat.

Either the sialic acid precursor N-[3H]acetyl-D-mannosamine ([3H]ManNAc) or horseradish peroxidase (HRP) or both were injected into the mesencephalon of 15 rats. Localisation of radioactivity was performed by light microscopic autoradiography and HRP was histochemically localised with 3,3'-diaminobenzidine. After injection of either [3H]ManNAc or HRP, cell bodies in the central cerebellar nuclei were filled with radioactivity or HRP respectively. The distribution over contra- and ipsilateral interposed, dentate and fastigial nuclei of [3H]ManNAc-labelled and HRP-labelled cells is similar for both types of labelling. Since HRP is known to be transported retrogradely, a similar localisation of radioactivity-accumulating cells and HRP-filled cell bodies in the central cerebellar nuclei, lead us to the conclusion that radioactively-labelled ManNAc or its derivatives are also retrogradely transported in this system. There seem to be two possibilities for label uptake in afferents axons: (1) the uptake into axons which are disrupted by the injection needle and (2) the uptake by intact nerve endings or axons. After injection of [3H]ManNAc, the neuropil of central cerebellar nuclei shows a higher concentration of silver grains than the labelled cell bodies. This could be due to labelled dendrites caused by retrograde transport.

Afferent Pathways↗
PubMed1983

Incorporation of radioactive 35SO4(2-) into immunoreactive pituitary lutropin.

The terminal hexosamines of bovine pituitary lutropin are thought to contain a sulfate moiety. In order to test this, a biosynthetic approach was adopted. When rat and buffalo (bovine) pituitaries were incubated with radioactive 35SO4(2-) for 2 h in vitro it was observed that radioactivity test incorporated into trichloroacetic acid-precipitable proteins. When the radioactive proteins were treated with an anti-sheep lutropin serum, radioactivity was found in the immunoprecipitate. The incorporation into rat lutropin like material was very marginal while it was very significant in the case of buffalo lutropin.

Animals↗
PubMed1982

Concentration of 3-methylindole (3MI) and distribution of radioactivity from 14C-3MI in goat tissues associated with acute pulmonary edema.

3-Methylindole (3MI) can cause acute pulmonary edema in goats. Because of known lipophilic properties and direct effects on biological membranes, the concentration of 3MI and distribution of radioactivity from 14C-3MI in tissues was investigated during development of 3MI-induced APE. Goats were given a 2 hr jugular infusion of 3MI containing 14C-3MI using propylene glycol as the vehicle. Groups of 3 goats were killed at 0, 5, 2 and 4 hr and 2 goats were killed at 8 and 24 hr. Plasma, lung, liver, kidney and other selected tissues were collected. 3MI was rapidly cleared from blood plasma and tissues after infusion, and 81% of the radioactivity was excreted in the urine by 24 hr. Maximum concentrations of unmetabolized 3MI in the tissues ranged from 2.6 to 15 micrograms 3MI/g, including 7.5 micrograms 3MI/g in the lung. The ratios of equivalent radioactivity to unmetabolized eMI indicated rapid metabolism and the presence of metabolites in all tissues studied. The lung contained the highest proportion of metabolites with ratios of radioactivity to unmetabolized 3MI of about 50, 10, 250, 150 and 80 at 0.5, 2, 4, 8 and 24 hr. The data demonstrate that 3MI does not selectively concentrate in the lung and that the concentrations are lower than those usually associated with direct membrane damage. They also indicate that 3MI is rapidly metabolized and that metabolites are present in tissues, especially the lung. These results suggest that direct effects of 3MI on biological membranes are not primarily responsible for lung injury in goats.

Animals↗
PubMed1988

Synthesis and characterization of a radiolabelled derivative of the phencyclidine/N-methyl-D-aspartate receptor ligand (+) MK-801 with high specific radioactivity.

A [3H]-labelled derivative of the drug (+)MK-801 with a high specific radioactivity was synthesized by first preparing a tribromo derivative of (+)MK-801 followed by catalytic reduction in the presence of [3H]-gas and subsequent purification of the radioactive product by reversed-phase high performance liquid chromatography (RP-HPLC). This resulted in pure (+) [3H]MK-801 with a specific radioactivity of 97 Ci/mmol. The (+) [3H]MK-801 was shown to interact with high affinity and selectivity with the phencyclidine (PCP) receptor in guinea pig brain membrane suspensions. The PCP receptor is associated with a cation channel that is chemically gated by glutamate and N-methyl-D-aspartate (NMDA). Drugs that interact with the PCP receptor block this channel. The (+) [3H]MK-801 described here will be useful to investigate the biochemistry of PCP/NMDA receptors in experiments where a high specific radioactivity is essential.

Animals↗
PubMed1984

An enzyme specific method for estimation of pyruvic acid radioactivity in biological samples.

A method for the estimation of pyruvate radioactivity in complex biological samples is presented. After perchloric acid deproteinization, the samples were divided in two aliquots. All pyruvate was removed from the first aliquot with lactate dehydrogenase and NADH; the other was left undisturbed. Then all hydrophilic components of the sample were removed through an Amberlite XAD-7 column. The samples were treated with dinitrophenylhydrazine to obtain the corresponding hydrazones, which were retained in an Amberlite XAD-7 column and then were eluted with acetone and their radioactivity counted. The difference between both aliquots corresponded to the pyruvate radioactivity in the sample. No contamination by lactate, glycerol, glucose or amino acids was observed. The mean recovery of 5 determinations of pyruvate radioactivity was 91.3% +/- 1.0.

Acrylic Resins↗
PubMed1993

A radio-enzymatic method for the estimation of L-leucine-specific radioactivity.

A method is presented for the estimation of L-leucine concentration and radioactivity in biological samples. The sample L-leucine is specifically bound to tRNA and its radioactivity estimated in the presence of either added labelled L-leucine or cold L-leucine (in the same proportion), as well as in the presence of a large excess of cold L-leucine. The latter gave the measurement of non-leucine radioactivity present in the sample. The measurements in the presence and absence of labelled/cold L-leucine allowed the estimation of L-leucine levels and radioactivity by using a simple set of calculations and a standard curve built with known cold L-leucine concentrations in the presence of a fixed known amount of [14C]L-leucine.

Alanine↗
PubMed1986

Tissue distribution and excretion of radioactivity following administration of 14C-labeled deoxynivalenol to White Leghorn hens.

The disposition of [14C]deoxynivalenol ([14C]DON) administered to hens as either a single oral dose or consumed in spiked feed over a 6-day period was determined by tracing the specific radioactivity of tissues and excreta. Following a single intubated dose (2.2 mg [14C]DON; 2.4 microCi/bird), the toxin was found to be poorly absorbed; peak plasma levels (2-2.5 hr post-treatment) accounted for less than 1% of the administered dose. Maximum tissue residues were measured at 3 hr in all tissues (liver, kidney, brain, heart, spleen, proventriculus, gizzard, small intestine) except for fat, muscle, and oviduct which occurred at 6 hr postdosing. Among the organs, the highest activities were measured in kidney, liver, and spleen; however, these levels were equal to less than 500 ng DON equivalents/g tissue, and declined quickly. Clearance of radioactivity from tissue had an average half-life of 16.83 +/- 8.2 hr (range 7.7-33.3 hr, depending on the tissue). Elimination of the labeled toxin in excreta occurred rapidly; recovery of radioactivity accounted for 78.6, 92.1, and 98.5% of the dose by 24, 48, and 72 hr, respectively. In continuously dosed birds fed 2.2 mg unlabeled DON for 6 days followed by 2.2 mg (1.5 microCi) [14C]DON for 6 days, accumulation of radioactivity in tissues did not occur. Maximum residual levels, which occurred in the kidneys, were only 60 ng DON equivalents/g. Estimated level of residues contained in the edible tissues amounted to only 13-16 micrograms DON/1.5 kg hen.

Animals↗
PubMed1979

The fate of [14C]streptozotocin in nicotinamide-pretreated mice: observations on pancreatic islet radioactivity and urinary N1-methyl-14C]nicotinamide-excretion.

A high labelling of the pancreatic islets was found 3 and 24 h after a diabetogenic dose of [14C]streptozotocin to mice in which the acids islet injury had been prevented by nicotinamide-pretreatment. In non-pretreated [14C]streptozotocin-injected mice, a much lower radioactivity was observed in the pancreatic islets; at 3 h and at 24 h, there was no detectable radioactivity in the islets. No evidence was found to indicate that nicotinamide-pretreatment had any marked effect on the uptake or retention of radioactivity in other tissues. N1-[methyl-14C]nicotinamide was not found in the urine of non-pretreated [14C]streptozotocin-injected mice. When the animals were pretreated with nicotinamide, N1-[methyl-14C]nicotinamide was detected in the urine, but this represented only a small fraction of the injected radioactivity and of the excreted N1-methylnicotinamide. This result does not support the hypothesis that the disturbance of the NAD-metabolism, which streptozotocin causes, is due to a methylation of nicotinamide.

Animals↗
PubMed1988

Cesium chloride: preventive medicine for radioactive cesium exposure?

Cesium is produced in high yield fission of uranium and plutonium. Radioactive cesium needles are a radiation hazard for radiotherapists. In this age of nuclear reactors, i.e. Chernobyl, radioactive cesium exposure may be a growing problem. Furthermore, there are numerous therapeutic potentials for cesium therapy, i.e. cancer, depression and schizophrenia. We explored the clearance of cesium in man and found that an oral dose of 50 mg maintains elevated blood cesium levels for 80 days. Cesium is accumulated mainly in the red blood cell fraction. Larger doses (6-9 grams) produce no observed harmful effects and maintain elevated blood levels of cesium for more than a year. Our data suggests there is a threshold of maximum cesium saturation in blood; if maintained, any additional cesium exposure, i.e. radioactive cesium, would be excreted at a more rapid rate. It is probable that large cesium doses can protect against radiation toxicity by blocking sites on red blood cells and thereby result in increased excretion and clearance of the radioactive forms of cesium. This hypothesis should be easily testable in laboratory animals.

Binding, Competitive↗
PubMed1992

The distribution of radioactivity in brains of rats given [N-methyl-11C]PK 11195 in vivo after induction of a cortical ischaemic lesion.

PK 11195 is a selective ligand for the peripheral-type benzodiazepine binding site (PTBBS). There are few such sites in normal brain but their number increases in association with tissue necrosis. The time-course of appearance of PTBBS around a focally induced ischaemic lesion in frontal cortex of rat brain was established by autoradiography using [N-methyl-3H]PK 11195. Using this information and the same experimental model of ischaemia, the distribution of radioactivity after injection of carbon-11 (t1/2 = 20.3 min, beta+ = 99.8%) labelled PK 11195 was studied. The purpose was to synthesize [N-methyl-11C]PK 11195 and to test its suitability as a tracer for depicting the presence of PTBBS in ischaemic lesions. The time-profiles of distribution of radioactivity in brain regions after intravenous injection of tracer and the ratio of radioactivity in lesioned compared with unlesioned cortex were determined. Data for the temporal (days after lesion induction) and for the regional retention of radioactivity were consistent with independent evidence (autoradiographic and immunohistochemical) for the occurrence of increased numbers of PTBBS, predominantly in association with macrophages, in areas undergoing necrosis.

Animals↗
PubMed1988

Procedures for radioactive I-131.

Details of the radioactive I-131 administration and radiation safety considerations are presented. Topics covered include patient survey, radioactive labelling, levels in patients containing radioactivity, hospital discharge of radioactive patients, and nursing procedures.

Brachytherapy↗
PubMed2004

An assay for adenosine 5'-diphosphate (ADP)-glucose pyrophosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase.

Adenosine 5'-diphosphate (ADP)-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the conversion of glucose 1-phosphate and adenosine 5'-triphosphate to ADP-glucose and pyrophosphate. We present a radioactive assay of this enzyme with a higher signal/noise ratio. After stopping the reaction that uses [14C]glucose 1-phosphate as a substrate, the ADP-[14C]glucose formed as a product is converted to [14C]glycogen by the addition of glycogen synthase and nonradioactive glycogen as primer. The final product is precipitated and washed, and the radioactivity is measured in a scintillation counter. The [14C]glucose 1-phosphate that did not react is easily eliminated during the washes. We have found that this assay produces much lower blanks than previously described radioactive methods based on binding of ADP-[14C]glucose to O-(diethylaminoethyl)-cellulose paper. In addition, we tested the kinetic parameters for the effectors of the Escherichia coli ADP-Glc PPase and both assays yielded identical results. The presented method is more suitable for Km or S(0.5) determinations of ADP-Glc PPases having high apparent affinity for glucose 1-phosphate. It is possible to use a higher specific radioactivity to increase the sensitivity at lower concentrations of [14C]glucose 1-phosphate without compromising the blanks obtained at higher concentrations.

Adenosine Diphosphate Glucose↗