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PubMed1997

Delay of corneal wound healing in patients treated with colchicine.

BACKGROUND: Colchicine has a known adverse effect on wound healing through its inhibitory effect on tubulin-dependent cell functions and through collagenase activation. In the cornea, it has been shown in animal and in vitro studies to inhibit epithelium mitosis, fibroblast mitosis and migration, as well as to reduce collagen deposition. The authors report on two patients with corneal ulcers refractory to conventional treatment while the patients were undergoing oral colchicine therapy. CASE REPORTS: The first patient was an 86-year-old woman who had been treated with oral colchicine because of rheumatoid arthritis. She was admitted to the authors' department with a deep corneal ulcer in the right eye for which she had been treated for 3 weeks with local antibiotics without any improvement. The second patient, a 60-year-old woman, was hospitalized because of a corneal ulcer in her left eye. She had been receiving oral colchicine therapy for mixed connective tissue disease. Treatment with local antibiotics was initiated but the condition of the eye worsened, ultimately resulting in corneal perforation. RESULTS: Withdrawal of oral colchicine therapy was followed by rapid corneal wound healing in both patients. CONCLUSION: The findings in these two patients suggest that colchicine may delay corneal wound healing. The authors suggest that in patients with corneal ulcers refractory to conventional treatment who are receiving colchicine, cessation of colchicine therapy should be considered.

Aged↗

PubMed1996

Inhibition of LPS-induced tumor necrosis factor-alpha production by colchicine and other microtubule disrupting drugs.

Colchicine has been shown to act as an antiinflammatory agent. In this study, we examined whether colchicine and other microtubule-depolymerizing drugs affected the production of TNF-alpha. When rat peritoneal macrophages were stimulated by LPS, addition of colchicine, vincristine, vinblastine or nocodazole was found to inhibit TNF-alpha release in a concentration-dependent manner. Suppression of TNF-alpha release was not due to interference with secretion as the cytokine did not accumulate intracellularly following colchicine treatment. Colchicine markedly enhanced PGE2 release from LPS-stimulated macrophages. However, addition of the cyclooxygenase inhibitor indomethacin only partially reversed the suppressive effect of colchicine on TNF-alpha production. Colchicine caused a strong reduction of LPS-induced TNF-alpha mRNA accumulation, suggesting that a pretranslational effect may represent the primary mechanism by which colchicine reduced TNF-alpha production. These observations could have clinical relevance in ameliorating undesirable effects due to excessive TNF-alpha production, for example following LPS stimulation of monocytes/macrophages in gram-negative sepsis. Furthermore, these drugs may provide useful tools to study the apparent involvement of the microtubular system in cytokine gene expression and cytokine production.

Animals↗

PubMed2002

Anti-/pro-oxidant effects of phenolic compounds in cells: are colchicine metabolites chain-breaking antioxidants?

Effective scavenging of reactive radicals and low reactivity of generated secondary antioxidant radicals towards vital intracellular components are two critical requirements for a chain-breaking antioxidant. Tubulin-binding properties aside, colchicine metabolites remain largely untested for other possible biological activities, including antioxidant activity. Mourelle et al. [Life Sci. 45 (1989) 891] proposed that colchiceine (EIN) acts as an antioxidant and protective agent against lipid peroxidation in a rat model of liver injury. Since EIN as well as two other colchicine metabolites, 2-demethylcolchicine (2DM) and 3-demethylcolchicine (3DM), possess a hydroxy-group on their carbon ring that could participate in radical scavenging, we tested whether they can act as chain-breaking antioxidants. Using our fluorescence-HPLC assay with metabolically incorporated oxidation-sensitive cis-parinaric acid (PnA) we studied the effects of colchicine metabolites on peroxidation of different classes of membrane phospholipids in HL-60 cells. None of the colchicine metabolites in concentrations ranging from 10(-6) to 10(-4) M was able to protect phospholipids against peroxidation induced by either azo-initiators of peroxyl radicals or via myeloperoxidase (MPO)-catalyzed reactions in the presence of hydrogen peroxide. However, the metabolites did exhibit dose-dependent depletion of glutathione, resembling the behavior of etoposide, a hindered phenol with antioxidant properties against lipid peroxidation. Electron spin resonance (ESR) experiments demonstrated that in a catalytic system containing horseradish peroxidase (HRP)/H(2)O(2), colchicine metabolites undergo one-electron oxidation to form phenoxyl radicals that, in turn, cause ESR-detectable ascorbate radicals by oxidation of ascorbate. Phenoxyl radicals of colchicine metabolites formed through MPO-catalyzed H(2)O(2)-dependent reactions in HL-60 cells and via HRP/H(2)O(2) in model systems can also oxidize GSH. Thus, colchicine metabolites possess the prerequisites of many antioxidants, i.e. a nucleophilic hydroxy-group on a carbon ring and the ability to scavenge reactive radicals and form a secondary radical. However, the latter retain high reactivity towards critical biomolecules in cells such as lipids, thiols, ascorbate, thereby, rendering colchicine metabolites effective radical scavengers but not effective chain-breaking antioxidants.

Antioxidants↗

PubMed1997

Acute onset of colchicine myoneuropathy in cardiac transplant recipients: case studies of three patients.

Colchicine causes both muscle and peripheral nerve toxicity of subacute onset in patients with renal insufficiency. We report three cardiac transplant recipients, treated with colchicine for cyclosporin A (CyA)-induced gout, who developed acute weakness due to colchicine myoneuropathy. The onset of disabling weakness occurred over a 1-2 week period. All three patients had concomitant renal insufficiency and an elevated serum creatine kinase and two elevated CyA levels at the time of presentation. Electromyography revealed features of myopathy and motor axonal neuropathy in all three patients. Two underwent muscle biopsy which confirmed the presence of sarcoplasmic vacuoles characteristic of colchicine-induced myopathy. All patients rapidly improved with either colchicine dose reduction or drug discontinuation. In conclusion, cardiac transplant recipients treated with CyA and colchicine may be at increased risk of developing colchicine-induced myoneuropathy especially in the setting of concurrent renal insufficiency. In patients with post-transplantation gouty arthritis, other treatment modalities are suggested; and if colchicine is administered, the dose should be reduced, CyA levels should be monitored closely and patients should be assessed for signs of neuromuscular toxicity.

Acute Disease↗

PubMed2003

Fos induction in the rat deep cerebellar and vestibular nuclei following central administration of colchicine: a qualitative and quantitative time-course study.

The present study was conducted to demonstrate Fos expression at four levels (anterior, prefastigial, postfastigial, posterior) of the cerebellar-vestibular nuclear complex in rats exposed to 1, 6, 24, and 48h of colchicine treatment using a light microscopic avidin biotin peroxidase (ABC) immunohistochemistry. Intracerebroventricular administration of colchicine (60microg per 10microl saline) elicited a continuous increase in the number of Fos-positive cells in the main cerebellar (fastigial, interpositus, dentatus) and vestibular (superior, medial, lateral, spinal, Y) nuclei. One and six hours after colchicine treatment, intensive Fos labeling was observed only in the pyriform cortex and the hypothalamic paraventricular nucleus, respectively, and there was no Fos immunolabeling in any of the cerebellar or vestibular structures investigated. On the other hand, moderate number of Fos-positive cells was visible in each of the cerebellar and vestibular nuclei 24h after colchicine treatment. Exposure of the animals to 48h of colchicine treatment induced an additional, more than 50%, rise in the accumulation of Fos-positive profiles in almost all the cerebellar and vestibular nuclei. In addition, at this time-point, a characteristic pattern of Fos distribution appeared almost in all of the cerebellar and vestibular nuclei, however, the numerical incidence of Fos-positive profiles in paired structures along the neuroaxis was bilaterally symmetric. The present data demonstrate for the first time that the central administration of colchicine causes a persistent and, in comparison with other brain areas, time-delayed activation of certain population of neurons in both cerebellar and vestibular nuclei. We assume that the delayed Fos activation in these structures indicate that the cerebellar and vestibular nuclei are not the primary targets of the central effect of colchicine and their activation seems to be rather a result of a postponed functional consequences of the central action of colchicine probably related to the coordination of motor performance.

Animals↗

PubMed1995

Vinca site agents induce structural changes in tubulin different from and antagonistic to changes induced by colchicine site agents.

Vinca site agents are antimicrotubule compounds that bind to the same site on tubulin as do the vinca alkaloids. These include agents that induce the formation of nonmicrotubule oligomers of tubulin (vinblastine and vincristine) and agents that do not (maytansine and rhizoxin). All of these quench the fluorescence of tubulin upon binding. Quenching preferentially affects the red side of tubulin emission, likely affecting more than one solvent-exposed tryptophan. Similar quenching is observed upon binding to either tubulin or tubulin-colchicine. None of these agents induces the local unfolding of the amphipathic helix in the carboxyl terminal region of beta-tubulin that colchicine and other colchicine site ligands do. All four vinca site agents inhibit this unfolding in tubulin-colchicine complexes without displacing colchicine. Both groups of vinca site agents enhance the chymotryptic cleavage of beta-tubulin after Tyr-281. Both groups of vinca site agents increase the beta-tubulin specificity of photolabeling with colchicine, and both groups inhibit colchicine-stimulated GTP hydrolysis. All of these effects common to both groups of vinca site agents are interpreted as due to vinca site occupancy alone. The vinca alkaloids differ from maytansine and rhizoxin by causing a large enhancement of chymotryptic cleavage of beta and a large inhibition of typtic cleavage of alpha, after Arg-339. These effects are interpreted as due to vinca induced oligomerization of tubulin. It is argued that the common binding site for the vinca site agents is located on beta-tubulin, close to the helix that is disrupted by colchicine.

Animals↗

PubMed1997

Expression of Fos-like proteins in the preoptic area and hypothalamus of the rat brain following intracerebral or peripheral administration of colchicine.

Colchicine is frequently employed as a pharmacologic tool to enhance perikaryal neuropeptide concentrations, in order to facilitate mapping of functional neuron populations in the brain. However, it is not clear if effects of colchicine on central neurons include transcriptional activation. The following studies utilized immunocytochemical techniques to evaluate the effects of intracerebroventricular (i.c.v.) drug treatment on Fos-like immunoreactivity (Fos-li) in preoptic and hypothalamic neurons. Since colchicine is administered orally in the treatment of gout-associated arthritis, additional experiments examined whether intragastric delivery of colchicine elicits protooncogene expression by neurons in the brain. Groups of adult male rats were treated with colchicine by i.c.v. injection (150 micrograms/3.0 microliters 0.9% saline) or by gavage (4.0 mg/1.0 ml 0.9% saline); vehicle-treated controls received saline alone. All animals were sacrificed 24 hr after drug or vehicle treatment. Serial 25 microns brain sections were processed for Fos-like immunoreactivity using anti-human Fos4-17 antibodies (Ab-2, Oncogene Sciences) in conjunction with avidin-biotin immunoperoxidase cytochemistry. These studies revealed negligible immunolabeling for Fos 24 hr after vehicle treatment, 24 hr after intracerebral delivery of colchicine, Fos-li was observed within the medial preoptic area, the arcuate nucleus, the supraoptic nucleus, and parvocellular neurons in the paraventricular nucleus. Animals treated with colchicine by gavage exhibited Fos-immunopositive neurons in the same sites, but additional immunolabeling for Fos was also observed within the median preoptic nucleus, suprachiasmatic nucleus, dorsomedial nucleus, and magnocellular neurons in the paraventricular nucleus. These results suggest, first of all, that neuronal responses to colchicine exposure include the synthesis of Fos-like proteins in a number of brain sites, at least over the time frame examined here. The present findings that protooncogene expression occurs within central neurons in response to intragastric drug administration suggest that neuronal activation may in response to drug-induced neural afferent and/or endocrine stimuli of peripheral origin.

Administration, Oral↗

PubMed2001

Colchicine for alcoholic and non-alcoholic liver fibrosis or cirrhosis.

AIMS/BACKGROUND: Colchicine is an anti-inflammatory and anti-fibrotic drug. Several randomized clinical trials have addressed the question whether colchicine has any efficacy in patients with alcoholic as well as non-alcoholic fibrosis and cirrhosis. The objectives were to assess the efficacy of colchicine evaluated in randomized trials on mortality, liver related mortality, liver related complications, liver fibrosis markers, liver histology, alcohol consumption, quality of life, and health economics in patients with alcoholic and non-alcoholic fibrosis or cirrhosis. METHODS: Interventions encompassed peroral colchicine at any dose versus placebo or no intervention. The trials could be double-blind, single-blind or unblinded. The trials could be unpublished or published as an article, an abstract, or a letter, and no language limitations were applied. All analyses were performed according to the intention-to-treat METHOD: MEDLINE, The Cochrane Controlled Trials Register, The Cochrane Hepato-Biliary Group Controlled Trials Register and full text searches were combined. RESULTS: Combining the results of 14 randomized clinical trials including 1138 patients demonstrated no significant effects of colchicine on mortality (odds ratio (OR): 0.91; 95% confidence interval (CI) 0.64, 1.31), liver related mortality (OR: 0.98; CI 0.56, 1.74), complications (OR: 1.06; CI 0.65, 1.73), and the other outcomes. Colchicine was associated with a significantly increased risk of adverse events (OR: 4.41; CI 2.24, 8.70; p< 0.001). CONCLUSIONS: Colchicine should not be used for liver fibrosis or liver cirrhosis irrespective of etiology. Future trials on colchicine for liver diseases ought to be large.

Administration, Oral↗

PubMed1966

Effects of colchicine on nucleic acid metabolism during metamorphosis of Tenebrio molitor L. and in some mammalian tissues.

1. Administration of 10mug. of colchicine/pupa of the beetle Tenebrio molitor L. arrests its differentiation, the pupa remaining alive for 2-3 weeks. 2. The same concentration of colchicine inhibits DNA synthesis and stimulates RNA synthesis (as shown by incorporation into the nucleic acids of labelled adenine, labelled uridine and labelled thymidine). The effects of colchicine on nucleic acid metabolism are first detected 3 days after its administration to first-day pupae. 3. No effects of colchicine are seen on [1-(14)C]glycine incorporation into protein in vivo. 4. Relatively high concentrations of colchicine (e.g. 10mm) suppress incorporation of [8-(14)C]adenine into RNA in dorsal abdominal wall in vitro. Such concentrations have no effect on its incorporation into acid-soluble nucleotides. 5. Colchicine (1mm) suppresses incorporation of [8-(14)C]adenine into DNA to a greater extent than into RNA in various mammalian tissues in vitro (e.g. rat spleen, regenerating rat liver, rat embryo, guinea-pig intestinal mucosa, Ehrlich ascites cells). Colchicine (1mm) has no effect on the rate of respiration of, or on incorporation of radioactivity into acid-soluble nucleotides in, the mammalian tissues tested. 6. Further evidence indicates complex-formation between colchicine and DNA, and it is suggested that the effect of colchicine in suppressing DNA synthesis is due to its combination with the DNA primer (template).

Animals↗

PubMed1997

Colchicine derivatives inhibit neopterin production in human peripheral blood mononuclear cells (PBMC).

Colchicine is a microtubule disrupting agent, mostly used as treatment in various kinds of inflammatory diseases such as acute familial Mediterranean fever and Behcet's disease, as well as gout. In patients with familial Mediterranean fever treatment with colchicine induces a decline of urinary neopterin concentrations which indicates a decrease of cell-mediated immune activation. In this study, we investigated a potential effect of colchicine on the T cell/macrophage system in vitro. The human myelomonocytic cell line THP-1 and PBMC were treated with colchicine or the colchicine derivative, colcemide, in the presence or absence of 250 U/ml interferon-gamma (IFN-gamma) or 10 microg/ml lipopolysaccharide (LPS) for 48 h or 96 h. Colchicine and colcemide increased neopterin/protein production in unstimulated THP-1 cells, but no such effect was apparent in cells stimulated with IFN-gamma. By contrast, when PBMC were treated with colchicine or colcemide a significant reduction in neopterin formation was evident in cells without and with prestimulation by IFN-gamma or LPS. In parallel, reduced production of IFN-gamma was observed in PBMC. These data suggest that colchicine and colcemide are able to inhibit T cell activation within the cellular immune response.

Biopterins↗

PubMed1999

Colchicine therapy for hepatic murine schistosomal fibrosis: image analysis and serological study.

Colchicine in a dose of 200 micrograms kg body weight/day (5 days/week) was administered to groups of Schistosoma mansoni infected mice 12 weeks post infection, either alone or following previous praziquantel therapy at the 8th week of infection. Certain groups received colchicine for 6 weeks and others received it for 10 weeks. Colchicine alone did not significantly change the light microscopic appearance of schistosomal liver fibrosis, or hepatic collagen content estimated histomorphometrically, and did not reduce the elevated IL-2 serum level. Colchicine induced hepatic injury consisted of intense inflammatory reaction in granuloma and portal tracts, hepatocytic degeneration, and elevation of serum AST and ALT levels. Colchicine seemed to postpone granulomatous reaction healing and collagen deposition rather than inhibiting collagen formation or degrading it. Colchicine inhibited proliferation of hepatocytes of infected mice by expanding G2-M phases of cell cycle, thus reduced Ag NOR count and raised cell ploidy and cyclic AMP serum level. Subsidence of schistosomal infection by praziquantel prior to colchicine therapy greatly reduced inflammatory cellular reaction, significantly diminished hepatic collagen deposition and serum IL-2 level, minimized the elevated nuclear ploidy and cyclic AMP serum level that followed colchicine therapy when administered alone.

Animals↗

PubMed1994

Immunoassays for the quantitative determination of colchicine.

A radioimmunoassay as well as an enzyme immunoassay for the quantitation of fmol amounts of the alkaloid colchicine have been developed. The antiserum used for both assays was raised against a conjugate of colchicoside-bovine serum albumin. The crude serum was satisfactory for the performance of the radioimmunoassay. For the enzyme immunoassay, the antibodies had to be isolated and purified by Rivanol treatment with subsequent (NH4)2SO4 precipitation. The measuring range extends from 0.1 to 100 ng colchicine for the radioimmunoassay and from 0.05 to 350 ng for the enzyme immunoassay with detection limits of 125 fmol and 25 fmol, respectively. Both immunoassays cross reacted with colchicoside and 3-demethyl-colchicine up to 80%. The colchicine content in the newly established suspension culture of Colchicum variegatum as well as the influence of various culture media on the colchicine production of this cell culture were investigated with the radioimmunoassay. The enzyme immunoassay was well suited for the quantitation of colchicine in HPLC fractions of Gloriosa and Colchicum seed extracts allowing the rapid, sensitive, and precise determination of the substance under investigation. The preliminary experiments indicate that both colchicine immunoassays can be a useful tool for the analysis of colchicine in tissue and cell culture studies, for analysis of plant extracts as well as for biosynthetic investigations.

Animals↗

PubMed1986

A prospective trial of colchicine for primary biliary cirrhosis.

We entered 60 patients with primary biliary cirrhosis in a double-blind randomized controlled trial to determine whether colchicine is therapeutically effective. Thirty patients had early disease (Stages 1 and 2), and 30 had advanced disease (Stages 3 and 4). Fifteen patients with early disease and 15 with advanced disease received colchicine (0.6 mg twice daily), and the remainder received placebo. Patients were studied about every two months; those remaining in the blind phase at two years underwent repeat liver biopsy and were then placed on open-label colchicine (0.6 mg twice daily). With a few exceptions, the results in patients with early disease were similar to those in patients with advanced disease; hence, data on patients in all stages were combined in the main analysis. During the two-year study period the colchicine-treated patients, as compared with the placebo-treated patients, had improvement in levels of serum albumin, serum bilirubin, alkaline phosphatase, cholesterol, and aminotransferases. However, there was no such improvement in the severity of symptoms or physical findings; moreover, there was no significant difference in the histologic changes noted at liver biopsy in the two treatment groups. At four years after entry, the cumulative mortality from liver disease was 21 percent in patients given colchicine and 47 percent in those given placebo (P = 0.05). The only side effect of colchicine was diarrhea, noted in three patients. The consistent and significant improvement in a number of markers of liver disease and the apparent decreased mortality from liver disease suggest that colchicine may provide some long-term clinical benefit in patients with primary biliary cirrhosis. However, the failure of colchicine to reduce hepatic inflammation and fibrosis leaves uncertain the effect of the drug on the longterm outcome of this disease.

Alkaline Phosphatase↗

PubMed1974

Promotion of fluorescence upon binding of colchicine to tubulin.

Colchicine, which does not fluoresce in aqueous media and organic solvents, exhibits marked fluorescence on combination with brain tubulin, with a corrected excitation maximum at 362 nm, an emission maximum at 435 nm, and a quantum yield of about 0.03. From fluorescence measurements it was found that rat brain tubulin binds 0.83 moles of colchicine per dimer (molecular weight 110,000) with an association constant of 3.2 muM(-1) at pH 7.0 and 37 degrees . These results are in excellent agreement with those obtained with the binding of [(3)H]-colchicine. The enthalpy of binding is 10 kcal/mole, with an entropy change of 62 entropy units. The fluorescence can be ascribed to the tropolone moiety. However, the A ring of colchicine is also involved in binding. Denaturing agents abolish fluorescence, whereas podophyllotoxin, another antimitotic agent, decreases fluorescence competitively. Fluorescence is a convenient method for determining the binding of colchicine to tubulin that does not require the separation of free colchicine from bound colchicine and yields values for physical and biochemical parameters that are in excellent agreement with those obtained from the binding of [(3)H]colchicine.

Animals↗

PubMed1979

Molecules in mammalian brain that interact with the colchicine site on tubulin.

Colchicine, a plant alkaloid, is a potent inhibitor of mitosis and other physiological processes that involve microtubules. These effects are mediated by the specific binding of colchicine to a high-affinity receptor site on tubulin, the major protein of microtubules. It seemed possible that the colchicine site on tubulin might also be the receptor for endogenous cellular molecules. We now report that mammalian brain does, in fact, contain a class of molecules that interact with the colchicine site on tubulin. Tubulin-agarose affinity chromatography has been used to isolate factors from soluble extracts of bovine brain that interact with tubulin. Certain of these factors inhibit the binding of [3H]colchicine to tubulin. Using the inhibition of colchicine binding as an assay, I have partially resolved at least two species. One is a protein and another may be a heat-stable peptide. In parallel to the action of colchicine, the smaller species inhibits the assembly of isolated microtubules. This class of molecules may include the endogenous ligands for which the colchicine site on tubulin is the receptor. They may have a significant role in the regulation of cellular microtubule function and assembly.

Animals↗

PubMed1984

Imbalance of total cellular nucleotide pools and mechanism of the colchicine-induced cell activation.

Treatment with colchicine or vinblastine, both inhibitors of microtubule assembly, renders quiescent 3T3 cells in an "activated state" as evidenced by induction of DNA synthesis and other criteria. Microtubule disassembly caused by colchicine or vinblastine brings about a dramatic expansion of total cellular UTP pools with a concomitant diminution in total cellular ATP pools, thus resulting in a marked imbalance in total cellular nucleotide pools. Colchicine and vinblastine also stimulate total cellular RNA synthesis without enhancing uridine phosphorylation, suggesting that these drugs affect the G1 phase of the cell cycle at a point beyond the enhancement of uridine phosphorylation that usually accompanies mitogenic stimulation of quiescent mammalian cells. The markedly expanded cellular UTP pools appear to be necessary for initiation of the colchicine-stimulated DNA synthesis because decreasing cellular UTP pools by addition of D-glucosamine results in a selective inhibition of DNA synthesis in the colchicine-stimulated, but not control, cells. Furthermore, D-glucosamine exerts its inhibitory effect only when it is present in the cultures within the first 14 hr after colchicine treatment. When added at 21 hr, D-glucosamine still decreases cellular UTP pools, but it is no longer inhibitory for DNA synthesis, which commences 14-16 hr after colchicine stimulation. Taxol, an antitumor drug, prevents microtubule disassembly and also blocks such events as expansion of total cellular UTP pools and stimulation of RNA and DNA synthesis, indicating that microtubule depolymerization acts as a primary event initiating the process of cell activation induced by colchicine.

Adenosine Triphosphate↗

PubMed2006

The effect of colchicine on the peritoneal membrane.

Peritoneal dialysis (PD) is a treatment modality for patients with renal failure. Peritoneal fibrosis is one of the most serious complications after long-term continuous ambulatory peritoneal dialysis (CAPD). Histological studies in both humans and animals show that chronic peritoneal dialysis results in fibrosis of the peritoneal membrane. In our study, we investigated the effect of colchicine on peritoneal alterations induced by hypertonic PD solution in rats. Sprague-Dawley rats intraperitoneally received saline (control group) once daily, for 28 days, or 3.86% glucose (PDF group), or 3.86% glucose plus colchicine (colchicine group). Animals from each group were sacrificed after 28 days with anesthetized ketamine (60 mg/kg BW). For the PD fluid assessment, 1 h before the sacrifice of animals, 10 mL PD fluid of 2.27% glucose was given, and this fluid was obtained after the sacrifice. The levels of transforming endothelial growth factor beta (TGF-beta), tumor necrosis factor alpha (TNF-alpha) and albumin were investigated both in the peritoneal dialysate and blood, and the levels of malondialdehyde (MDA) were investigated only in peritoneal dialysate. The peritoneal membrane was evaluated histologically by light microscopy. When groups were compared in terms of body weight change, the colchicine group significantly lost weight compared to controls and PDF group (-4.7% + 4.5, 3.5% +/- 7.2, 3.0% +/- 1.3, respectively, p = 0.018). Also, the blood albumin level was significantly lower for these in the colchicine group compared to those in the PDF group (2.7 +/- 0.35 versus 3.2 +/- 0.3 g/dL, respectively, p = 0.048). The blood TGF-beta level was significantly lower in the control group, and no difference was observed between the PDF and colchicine groups (294.4 +/- 67.5 versus 787.4 +/- 237.4 versus 615.3 +/- 235.1 pg/mL, respectively, p = 0.004). The mesothelial thickness found in groups was as follows: control group 102 +/- 18.9 microm, PDF group 128.33 +/- 33.1 microm, colchicine group 117 +/- 35.6 microm (p = 0.34). In conclusion, a rat model for peritoneal dialysis associated peritoneal derangement without fibrosis could be induced. Colchicine could not prevent peritoneal derangement in this model.

Animals↗

PubMed1978

Fluorescein colchicine. Synthesis, purification, and biological activity.

The synthesis of a fluorescent colchicine derivative permits the localization of colchicine-binding receptors in cells. Fluorescein colchicine (FC) was prepared by the addition of fluorescein isothiocyanate to deacetyl colchicine. The product, FC, was separated from the reactants by thin-layer chromatography (TLC). The purity of FC was demonstrated by TLC, UV spectral analysis, and analysis of the kinetics of photodecomposition. FC inhibited [3H] colchicine binding to purified brain tubulin. The biological activity of FC was compared to the activity of unlabeled colchicine on mitosis, motility, secretion, and myogenesis. The effects of FC were identical to those of unlabeled colchicine in all biological systems tested. The results demonstrate that FC may be substituted for colchicine in biological experiments without significant loss in specificity or effectiveness.

Colchicine↗