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C A Villee

Publications and source records attributed to C A Villee.

At least 19 recordsLinked to original sources
PubMed1992

Autoantibodies to c-myc protein: elevated levels in patients with African Burkitt's lymphoma and normal Ghanians.

Sera from U.S. patients with SLE, RA, and various malignancies, clinically normal individuals with sero-activity to HIV, AIDS, and from pregnant women were tested for the presence of anti-c-myc antibodies. In an ELISA using recombinant human c-myc protein as the antigen, no difference in mean antibody titer was generally detected in these sera when compared to normal controls. Only three malignancy sera (two myeloid leukemia and only one lymphoma) and two patients with AIDS-related lymphoma exhibited exceedingly higher levels of anti-c-myc antibody. However, significantly elevated anti-c-myc antibody levels were found among 20 patients with African Burkitt's lymphoma (Ghana) and 20 normal Ghanians, thus apparently reflecting an autoimmune phenomenon prevalent in the endemic region. These findings indicated that elevated levels of anti-c-myc antibodies are not a general characteristic of patients with diseases that have been associated with increased expression of c-myc.

Autoantibodies↗
PubMed1986

A cytosolic binding protein for 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in the uterus and deciduoma of rats.

The cytosol fraction of the uterus of proestrous rats and of deciduoma specifically binds 3H-2,3,7,8-tetrachlorodibenzo-p-dioxin (3H-TCDD). The 3H-TCDD binding protein has a sedimentation coefficient of 9 S in low ionic 10-40% sucrose density gradients. The binding of 3H-TCDD in the 9 S region is abolished by a 500-fold molar excess of unlabeled benzo[a]pyrene, 3-methylcholanthrene or by a 100-fold molar excess of unlabeled TCDD. Incubation of the binding protein with TCDD in amounts in excess of 500 nM causes aggregation of the TCDD binding protein. Neither estradiol, progesterone, testosterone, dihydrotestosterone nor cortisol competed with TCDD in binding to this 9 S protein. The decidual tissue contains two binding components for TCDD as shown by Scatchard analysis. One of the components has a high affinity for TCDD (Kd = 1.68 nM) and is saturable. The number of binding sites is about 75 fmol/mg protein. The TCDD binding protein eluted through a DEAE-cellulose column using a gradient of 0.25 M KCl. The binding of estradiol and progesterone to their respective receptors was not affected by TCDD or by other polycyclic aromatic hydrocarbons as shown by sucrose density gradients and by microtiter competition assays. These results suggest that TCDD acts by binding to its own receptor system in the target tissue and not by competing with estrogen or progesterone for binding to their receptors. The possible role of the receptor in teratogenesis is discussed.

Animals↗
PubMed1986

Characterization and control of cytosolic binding proteins for 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) in the rat lung.

The presence of a high-affinity, low-capacity 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) binding complex was demonstrated in cytosol from rat lung. When analyzed by sucrose density gradient centrifugation, the 3H-TCDD binding complex sedimented at 8-9 S and 6.5 S in low and high ionic media, respectively. The apparent dissociation constant (Kd) of the 3H-TCDD binding complex was determined to be 2.9 nM and the number of binding sites (Bmax) was approximately equal to 69 fmol/mg of cytosolic protein. The entity was sensitive to heat and to proteases but not to DNAse or RNAse, indicating that it was a protein. An excess of unlabeled TCDD, benzo[a]pyrene, 3-methylcholanthrene, 7,12-dimethylbenzo[a]anthracene and 9-hydroxy ellipticine all competed with 3H-TCDD for binding. A single injection of either benzo[a]pyrene (20 mg/kg body weight) or 9-hydroxy ellipticine (20 mg/kg body weight) had different effects on the concentrations of 3H-TCDD binding proteins in the lung but none of the chemicals had a significant effect on the synthesis of surfactant as assayed by total phospholipid content, 72 h after the injection.

Animals↗
PubMed1985

A metabolite of riboflavin binds to the 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) receptor.

A cytosolic receptor to which TCDD binds with high affinity has been reported in a number of rodent tissues, but the endogenous/natural ligand is not known. However, lumichrome, a metabolite of riboflavin, competed with 3H-TCDD for binding to the cytosolic receptor. Neither riboflavin nor riboflavin-5-phosphate competed for binding to the TCDD receptor in rat liver cytosol. Lumichrome is the first known endogenous chemical in the rat to exhibit affinity for the TCDD receptor.

Animals↗
PubMed1985

Control of 2,3,7,8-tetrachlorodibenzo-p-dioxin binding protein(s) in the hamster kidney.

Hamster renal cytosol binds [3H]-2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) with high specificity. Sucrose density gradient centrifugation revealed two binding entities- one with a low sedimentation coefficient of 4-5 S which was displaced by neither TCDD nor other polycyclic aromatic hydrocarbons (PAHs) and another with a high sedimentation coefficient of 7-8 S which was displaced by TCDD, benzo[a]pyrene (BP), 2-methylcholanthrene (MC), and 7,12-dimethylbenzo[a]anthracene (DMBA) but not by estradiol (E), progesterone (P), cortisol (F), testosterone (T), 5 alpha-dihydrotestosterone (DHT), or methyltrienolone (R-1881), a synthetic androgen. Cytosol from intact male hamsters showed maximum binding of labelled TCDD to the 7-8 S binding site. Castration or hypophysectomy reduced this binding. Pretreatment with DMBA increased binding, whereas diethylstilbestrol (DES) decreased binding. Sex difference was observed in the binding capacity of renal cytosol. This is the first report of endocrine control over TCDD binding and its modulation by other PAHs and steroids.

9,10-Dimethyl-1,2-benzanthracene↗
PubMed1979

Increased progesterone receptor concentrations in bladder lesions of estrogen-treated Syrian hamsters.

During studies of renal tumorigenesis induced by estrogen in Syrian hamsters, we have observed that about 15 to 20% of animals develop bladder lesions with an increased wet weight of tissue from 0.2 g to 0.4 to 1.7 g. Histological examination of the lesions showed a spectrum of changes from inflammatory reactions to squamous metaplasia and intense hyperplasia of the transitional epithelium. The concentration of progesterone-binding sites was increased in the bladders with lesions. No specific progesterone-binding sites could be detected in the cytosol of bladders from hamsters not treated with estrogen. The affinity constant for the progesterone-binding sites in cytosol from bladders with lesions was 10(9) M-1, the same as that reported for progesterone receptors in other target tissues for estrogen. The binding sites are specific for progesterone and are not competed for by 17 beta-estradiol, 5 alpha-dihydrotestosterone, or aldosterone.

Aldosterone↗
PubMed1977

Changes in estrogen receptor levels during deciduomata development in the pseudopregnant rat.

The presence of a cytoplasmic estradiol receptor with an affinity constant of 10(10)M-1 has been demonstrated in the differentiated fibroblasts comprising the deciduomata in pseudopregnant rats. The receptor had a sedimentation coefficient of 6S in sucrose density gradients containing a physiological concentration of salt, and estradiol binding was completely abolished by a hundred-fold excess of unlabeled estradiol. During the early stages of decidualization (days 2 and 3), the decidualized uterine horn or isolated deciduomal tissue contained a concentration of receptor comparable to that in non-gravid uteri from rats ovariectomized at estrus. By day 5 of decidualization, the concentration of estradiol binding in deciduomal tissue decreased to about one-half the concentration measurable at days 2 and 3 of decidualization despite continued tissue growth until day 7. By day 7 of decidualization, estradiol binding had decreased to about 20% of the concentration on days 2 and 3 of decidualization. Cytosol from untreated uterine horns of rats bearing deciduomata bound the same amount of estradiol through day 7 as that in uteri of rats ovariectomized at estrus. These observations are discussed in terms of steroid hormone involved in deciduomal growth and regression.

Animals↗
PubMed1977

Changes in progesterone receptor levels during deciduomata development in the pseudopregnant rat.

A specific cytoplasmic progesterone receptor has been identified and quantified in the deciduomata of the pseudopregnant rat. The receptor had a sedimentation coefficient of 6-7S on sucrose density gradients and was inactivated by proteolytic enzymes, sulfhydryl blocking agents and elevated temperature. The equilibrium association constant for the binding of progesterone by the deciduomal receptor was determined to be approximately 10(9)M-1. The concentrations of progesterone receptor sites in cytosols prepared from deciduomata on day 3 and 5 of decidualization were 3.4 +/- 0.3 X 10(-10)M and 3.6 +/- 0.4 X 10(10)M, respectively, when normalized to a protein concentration of 1 mg/ml. These concentrations of progesterone receptor sites were similar to that measured in the uterine cytosol of estrous rats or in the contralateral untreated uterine horn of rats undergoing decidualization. Following day 5 of decidualization the concentrations of progesterone receptor sites decreased linearly so that by day 7 the concentration was approximately one-half that at days 3 and 5. The physiological significance of the progesterone receptor and the decrease in its concentration with time are discussed with regard to their influence on the decidualization reaction.

Animals↗
PubMed1976

Structure of eukaryotic chromatin. Evaluation of periodicity using endogenous and exogenous nucleases.

DNA isolated from (a) liver chromatin digested in situ with endogenous Ca2+, Mg2+-dependent endonuclease, (b) prostate chromatin digested in situ with micrococcal nuclease or pancreatic DNAase I, and (c) isolated liver chromatin digested with micrococcal nuclease or pancreatic DNAase I has been analyzed electrophoretically on polyacrylamide gels. The electrophoretic patterns of DNA prepared from chromatin digested in situ with either endogenous endonuclease (liver nuclei) or micrococcal nuclease (prostate nuclei) are virtually identical. Each pattern consists of a series of discrete bands representing multiples of the smallest fragment of DNA 200 +/- 20 base pairs in length. The smallest DNA fragment (monomer) accumulates during prolonged digestion of chromatin in situ until it accounts for nearly all of the DNA on the gel; approx. 20% of the DNA of chromatin is rendered acid soluble during this period. Digestion of liver chromatin in situ in the presence of micrococcal nuclease results initially in the reduction of the size of the monomer from 200 to 170 base pairs of DNA and subsequently results in its conversion to as many as eight smaller fragments. The electrophoretic pattern obtained with DNA prepared from micrococcal nuclease digests of isolated liver chromatin is similar, but not identical, to that obtained with liver chromatin in situ. These preparations are more heterogeneous and contain DNA fragments smaller than 200 base pairs in length. These results suggest that not all of the chromatin isolated from liver nuclei retains its native structure. In contrast to endogenous endonuclease and micrococcal nuclease digests of chromatin, pancreatic DNAase I digests of isolated chromatin and of chromatin in situ consist of an extremely heterogeneous population of DNA fragments which migrates as a continuum on gels. A similar electrophoretic pattern is obtained with purified DNA digested by micrococcal nuclease. The presence of spermine (0.15 mM) and spermidine (0.5 mM) in preparative and incubation buffers decreases the rate of digestion of chromatin by endogenous endonuclease in situ approx. 10-fold, without affecting the size of the resulting DNA fragments. The rates of production of the smallest DNA fragments, monomer, dimer, and trimer, are nearly identical when high molecular weight DNA is present in excess, indicating that all of the chromatin multimers are equally susceptible to endogenous endonuclease. These observations points out the effects of various experimental conditions on the digestion of chromatin by nucleases.

Animals↗