Search PubMed⌕ Search

Biomedical subjects

G W Bates

Publications and source records attributed to G W Bates.

At least 91 records · Page 5Linked to original sources
PubMed1980

The use of medroxyprogesterone acetate for relief of climacteric symptoms.

Climacteric symptoms in the menopausal woman are perplexing to the physician. Recent literature concerning the relationship of estrogen to carcinogenesis has caused many women to discontinue this medication; thus, there is a need for an alternative therapy for the relief of these symptoms. The drug medroxyprogesterone acetate (Depo-Provera) was assessed in a double-blind, randomized, placebo-controlled study involving 48 subjects. Only one of the placebo-treated patients claimed any relief from climacteric symptoms while only two of the patients who received the study drug noted little or no relief (P < 0.0001). Relief from climacteric symptoms began at 4 to 7 days after entry into the study and extended for 8 to 20 weeks. The only side effects were withdrawal bleeding and a slight, transient weight gain. Depo-Provera appears to be a reliable substitute for estrogen in the treatment of climacteric symptoms. Further investigations with this medication seem indicated.

Adult↗
PubMed1980

Analgesic efficacy of ibuprofen for treatment of primary dysmenorrhea.

Fifty-five women with primary dysmenorrhea were enrolled in a study which each took ibuprofen (400 mg), propoxyphene hydrochloride (64 mg), or a placebo alternately in consecutive menstrual cycles for relief of pain. Fifty-one completed the study during three successive cycles in this triple-blind, crossover, randomized investigation. Ibuprofen was clearly superior to propoxyphene and the placebo in patient preference, degree of relief, and need for supplementary analgesics. In addition, a significantly greater number of patients were able to pursue their normal daily functions during the ibuprofen cycle. Propoxyphene was superior to the placebo but not to the same extent as ibuprofen. Only three side effects were reported during the study, two relative to propoxyphene and one recorded during a placebo cycle. These data show that ibuprofen is an effective agent when used for treatment of dysmenorrhea without organic etiology.

Adult↗
PubMed1980

Neuroendocrine control of gonadotropin secretion.

Luteinizing hormone releasing hormone (LHRH), a hypothalmic peptide that is concentrated in granules of neurons, has the capacity to release gonadotropins (luteinizing hormone (LH) and follicle stimulating hormone) from the pituitary gland. LHRH has been found in hypophysial portal blood of rats, monkeys, and rabbits. Antibodies to LHRH depress plasma LH concentrations in castrated animals and evoke testicular atrophy, but passive immunization against LHRH does not block the LH surge induced by estrogen in monkeys. Estrogens, progestin, prolactin, and dopamine have marked effects on LH secretion, yet an association between these effects and altered hypophysial portal blood concentrations of LHRH is not established. In view of the paucity of evidence demonstrating such a cause and effect relationship, two alternative proposals have become tenable. One, hormones and neurotransmitters may not alter the levels of portal blood LHRH, but rather alter the frequency of pulsatile LHRH secretion. Two, hormones, such as estrogens, progesterone, and prolactin, may alter the responsiveness of the gonadotropin-secreting cells to LHRH by affecting the secretion of dopamine.

Adult↗
PubMed1979

An assay for human erythrocyte catechol-O-methyltransferase activity using a catechol estrogen as the substrate.

A radiometric assay for catechol-O-methyltransferase (COMT) activity in human erythrocytes is described that employs 2-hydroxy[3H]estrone, and non-radiolabeled S-adenosylmethionine (SAM) as the cosubstrates. The ease of separation of the product of the reaction, 2-methoxy[3H]estrone from 2-hydroxy[3H]estrone makes it possible to achieve low reaction blanks. The assay is very sensitive, and only 200 microliter of whole blood are used per determination. The assay is highly reproducible. The interassay variability (coefficient of variation) was 6.5% for 24 assays of COMT activity in red blood cells in blood obtained daily for 24 days from one person. In incubations conducted at 37 degrees C for 30 min, the catechol-O-methyltransferase activity was a linear function of enzyme concentration (equivalent to 11 to 180 microliter of packed red blood cells). Employing this assay, we evaluated the catalytic conversion of 2-hydroxyestrone to 2-methoxyestrone by catechol-O-methyltransferase from human red blood cells and found that the apparent Michaelis constant and the apparent maximal rate of reaction were 3 x 10(-7) M and 6.7 x 10(-9) mol . ml-1 erythrocytes . h-1, respectively. The catechol-O-methyltransferase activity measured in erythrocytes obtained from 100 healthy subjects (men and nonpregnant women) was 8.2 +/- 0.17 (mean +/- S.E.) nmol 2-methoxyestrone . ml-1 erythrocytes . h-1.

Carbon Radioisotopes↗
PubMed1979

Catechol-O-methyltransferase activity in erythrocytes of women taking oral contraceptive steroids.

We have measured catechol-O-methyltransferase (COMT) activity in erythrocytes (red blood cells, RBCs) obtained from 64 women taking oral contraceptives steroids and compared these values with those found in RBCs obtained from 73 women using nonsteroidal contraceptives. The COMT activity in the RBCs of women taking oral contraceptives steroids and of women not taking contraceptive steroids was 9.1 +/- 0.28 (mean and standard error) and 8.8 +/- 0.26 nmoles 2-methoxyestrone X ml-1 RBC X hr-1, respectively. This difference in the COMT activity in RBCs from these two groups of women was not statistically significant. This finding differs from that of others who found that COMT activity in RBCs of women taking oral contraceptive steroids was greater than that of women not taking such drugs.

Adult↗
PubMed1979

Mobilization of iron from specifically labeled reticulocyte ghosts.

Specifically labeled 59Fe ghosts have been prepared by incubation of whole reticulocytes with 59Fe3+-transferrin-CO3(2)-- followed by washing and ghost isolation. The binding of 59Fe by the membrane fraction is quite stable over a wide range of conditions, but iron mobilization occurs on incubation with chelating agents or cell lysate. The time course of 59Fe mobilization by unlabeled reticulocyte lysate exhibits five apparently zero-order phases. The rate of iron mobilization is linearly dependent on the concentration of 59Fe ghosts present in the incubation mixture. In contrast, the relative concentration of lysate appears to exhibit a saturation dependence with regard to membrane iron mobilization. Bathophenanthroline sulfonate follows a multiphasic time course of iron mobilization similar to that found with the lysate. Lysate from mature erythrocytes was found to mobilize iron with kinetics that are identical to reticulocyte lysate. The number and duration of the phases is independent of the mobilizing agent. The role of the membrane fraction in regulating the rate of iron release to cytosol was also investigated by the repetitive incubation of 59Fe ghosts with fresh lysate. The rate of 59Fe mobilization depended on the condition of the ghost with regard to prior 59Fe depletion. This publication emphasizes the active role of the membrane fraction in determining the rate at which iron will become available to the cytosol and the possibility that cytosol factors modulate the action of membrane bound components.

Animals↗
PubMed1978

Catechol-O-methyltransferase activity in erythrocytes of pregnant women.

Catechol-O-methyltransferase (COMT) is the enzyme that converts catechols, e.g., catecholamines and catechol estrogens, to their methyl ethers. COMT activity measured in erythrocytes (RBC's) of healthy men (No. = 47) and healthy nonpregnant women (No. = 53) was 8.2 +4- 0.17 nmoles X ml.-1 (mean and standard error). The COMT activity in RBC's of healthy pregnant women (No. = 100) was 10.7 +/- 0.29 nmoles X ml.-1 RBC X hr.-1, a value which is significantly higher than that found in RBC's of men and nonpregnant women (p less than 0.001).

Adolescent↗
PubMed1978

Non-specific serum iron in thalassaemia: an abnormal serum iron fraction of potential toxicity.

Iron binding in the sera of 35 patients with beta thalassaemia major and intermedia was studied. In patients receiving regular blood transfusions since infancy transferrin was completely saturated and about 2.7--7.1 mumol/l of the serum iron could be removed by dialysis or ultrafiltration in the presence of a chelating agent or by filtration on DEAE-Sephadex-catecholdisulphonic acid columns. In contrast, less than 1.0 mumol/l of transferrin bound iron was removed when subjected to the same procedures. The non-specific iron of thalassaemic sera could no longer be demonstrated after incubation with normal serum. These findings indicate that non-specific iron is a chelatable with normal serum. These findings indicate that non-specific iron is a chelatable compound which is readily available for transferrin binding. In view of the known toxicity of unbound iron, its identification in thalassaemic sera might be of relevance to the pathogenesis of tissue damage and the protective effect of iron chelating therapy in this disease.

Adolescent↗
PubMed1977

Metabolism of catechol estrogen by human erythrocytes.

In a study designed to evaluate the kinetics of catechol estrogen formation from plasma estrone in vivo, we obtained evidence that the red blood cell (RBC) enzyme, catechol-O-methyl transferase, catalyzes the transformation of 2-hydroxyestrone to 2-methoxyestrone. Under in vitro conditions, the rate of conversion of 2-hydroxyestrone to 2-methoxyestrone by human RBC's was such that 7 nmol of 2-methoxyestrone were formed per h per ml of RBC.

Catechol O-Methyltransferase↗
PubMed1976

Approaches to the standardization of serum unsaturated iron-binding capacity.

An important aspect in the development and use of serum unsaturated iron-binding capacity (UIBC) procedures is the standardization of reference serum. Spectrophotometric titration of serum transferrin is the oldest of the UIBC methods; however, the literature on this subject indicates that the technique is not being fully exploited and describes a variety of suboptimal conditions. A spectrophotometric titration protocol is described which gives excellent reproducibility with fresh, frozen, lyophilized, and stored serum samples. An indirect UIBC method utilizing differential chelation and ultrafiltration is also described. In this method Fe3+ -NTA (nitrilotriacetic acid), in excess of the anticipated UIBC, is added to a serum sample supplemented with NaHC03. The addition of EDTA (ethelenediaminetetraacetic acid) allows the mobilization of iron from nonspecific macromolecular sites. The ultrafiltrate is analyzed for iron, and the UIBC is calculated. The results were validated via an ultrafiltration titration which was compared with a spectrophotometric titration. The precision of this method is excellent.

Anemia, Hypochromic↗
PubMed1975

The effect of serum and experimental variables on the transferrin and reticulocyte interaction.

The transfer of iron from transferrin to the developing erythrocyte is a research area of high interest and considerable controversy. We have found that the results of transferrin-reticulocyte incubation studies are quite sensitive to the experimental procedures that are utilized. Reticulocytosis has been induced in rabbits by phelbotomy and phenylhydrazine injections. While the latter gives a higher reticulocyte count, the cells appear to exhibit an altered transferrin-membrane interaction. Transferrin has been iodinated by published methods utilizing chloramine-T and molecular iodine. The iodotransferrin products exhibit the same iron donation ability, however, evidence was found that the chloramine-T treatment leads to a nonspecific binding of transferrin to the reticulocyte. The means of saturating transferrin with 59Fe is also of prime importance. Fe(NH4)2(SO4)2 and especially FeCl3 were found to yield nonspecifically bound iron when added to transferrin or serum. This artifact was reflected in an altered transferrin-reticulocyte interaction. Using what we believe to be optimal conditions, the effect of serum on the transferrin-reticulocyte system was re-examined. The results clearly indicated an enhancement of iron uptake by reticulocytes in the presence of serum, as well as an accelerated incorporation of iron by the cytoplasmic fraction.

Animals↗
PubMed1975

The nonspecific binding of Fe3+ to transferrin in the absence of synergistic anions.

An obligatory role for barbonate (or other synergistic anions) in the specific binding of Fe3+ by transferrin has been a point of controversy for two decades. There are an equal number of confirmatory and negative reports of specific Fe3+-transferrin binary complexes. A criticism of previous studies is the use of only one synthetic route, and limited product testing. This study reports the development of several preparative routes aimed at the formation of a specific Fe3+-transferrin complex, and the characterization of the products by spectrophotometry and chemical reactivity. The preparative routes described include: (a) displacement of carbonate from Fe3+-transferrin-CO32- at low pH followed by removal of CO2 by several techniques; (b) addition of FeCl3 to apotransferrin under CO2-free conditions; (c) oxidation of Fe2+ in the presence of apotransferrin under CO2-free conditions; (d) reaction of apotransferrin with nonsubstituting Fe3+ complexes in the absence of CO2; and (e) attempts to displace anions from weak Fe3+-transferrin-anion complexes. The product were examined with regard to their visible spectra, and their examined with regard to their visible spectra, and their reactivity with: (a) NaHCO3, (b) Fe3+-nitrilotriacetic acid in NaHCO3, and (c) citrate. The results are compared with the characteristics of Fe3+-transferrin-anion complexes and nonspecific Fe3+, transferrin mixtures. The data indicate that in the absence of synergistic anions the affinity of the specific metal binding sites of transfe-rin for Fe3+ is so low as to not compete favorably with hydrolytic polymerization and nonspecific binding effects.

Bicarbonates↗