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#10541381   1999/11/24 Save this To Up

Fractionated radiolabeled antiferritin therapy for patients with recurrent Hodgkin's disease.

The objective of this study was to determine the therapeutic ratio of fractionated radiolabeled immunoglobulin therapy (RIT) for patients with recurrent Hodgkin's disease. Ninety patients with recurrent Hodgkin's disease received 2 mg of yttrium-90-labeled polyclonal rabbit antihuman ferritin IgG i.v. Fifty-seven patients received a single (unfractionated) administration per treatment cycle; 11 of them were treated with 0.3 mCi/kg body weight, 39 were treated with 0.4 mCi/kg body weight, and 7 received 0.5 mCi/kg body weight per treatment cycle. Thirty-three patients had their radiolabeled immunoglobulin administration separated (fractionated) in 2 x 0.25 mCi/kg body weight (total activity, 0.5 mCi/kg). The interval between fractions was 1 week. Radioimmunoconjugates did not cause serious acute side effects. In vivo radioimmunoconjugates were stable. Human antirabbit IgG antibodies were found in 2 of 50 retreated patients (<5%). Hematological toxicity was the only side effect noted in all patients, and it was usually temporary. Response rates (RRs) were 20%, 61%, and 86% after 0.3, 0.4, or 0.5 mCi/kg unfractionated yttrium-90-labeled antiferritin. The RR for patients treated with fractionated RIT was 42%. In the fractionated RIT group, complete responses were decreased, and progressive disease increased (P < 0.05). Complete responses had a medium duration of 6 months. Median survival times were 390 days for 1 x 0.4 mCi/kg and 300 days for the 2 x 0.25 mCi/kg patient group. Fractionation did not provide the expected decrease in hematological toxicity or the expected increase in tumor RRs.

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#10541380   1999/11/24 Save this To Up

Pharmacokinetics of radiolabeled polyclonal antiferritin in patients with Hodgkin's disease.

The objective was to identify pharmacokinetic parameters predictive for tumor response and normal tissue side effects after i.v. administered radiolabeled rabbit antihuman ferritin IgG. Twenty-eight patients with recurrent Hodgkin's disease received 2 mg of rabbit antihuman ferritin i.v., labeled with 4-7 mCi of In-111 followed by two doses of 0.25, one dose of 0.3, or one dose of 0.4 mCi of Y-90-labeled antiferritin per kg of body weight 1 week later. Radioactivity and HPLC measurements of blood and urine samples and liver and tumor volumes identified on sequential whole-body scans provided the data for a pharmacokinetic analysis covering the first 6 days after the administration of the radioimmunoconjugate. Side effects and tumor response were recorded. Temporary hematological toxicity was noted in all patients. Sixteen patients showed a tumor response. The Y-90 blood level at 1 h after administration correlated with the severity of subsequent hematological toxicity. The rapid blood elimination half-life of radioactivity was 4.4 h. Less than 5% of the administered radioactivity was eliminated in the first 24 h urine. The slow blood elimination half-life was 44 and 37 h for In-111 and Y-90, respectively. One of 12 retreated patients produced anti-rabbit IgG antibodies. The volume of distribution was larger for Y-90 than for In-111-labeled antiferritin (160 versus 110% of estimated blood volume). Accidentally extravasated rabbit IgG was rapidly catabolized in perivascular tissues with an effective half-life of less than 35 h. Slower catabolism was noted for rabbit IgG in blood (t(1/2) = 40 h), liver (t(1/2) = 62 h) or tumor (t(1/2) = 40-80 h). Twelve of 13 patients with an effective tumor half-life > 57 h showed a tumor response. I.v. administered polyclonal rabbit antihuman ferritin, labeled with In-111 or Y-90 is stable in vivo and targets Hodgkin's disease. Intravascular Y-90 causes a vascular leak and a larger volume of distribution for antiferritin. Elevated Y-90 blood levels at 1 h and a tumor half-life of >57 h predict for hematological toxicity and tumor response, respectively.

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#7020426   1981/09/15 Save this To Up

Immunocytochemical studies of neurofibrillary tangles.

The molecular nature of neurofibrillary tangles of senile dementia of the Alzheimer type (SDAT) was studied by immunoperoxidase and immunofluorescence techniques. Five antiserums, including anti-humanbrain-2-cycle-purified-microtubule-fractions (2 x MT), anti-calf-brain-2 x MT, anti-sea-urchin-egg-tubulin, antibeef-brain-tubulin, and anti-human-brain-neurofilament(NF)-210-kilodalton(kd)-protein were tested for their binding to neurofibrillary tangles. The antihuman-2 x MT serum stained structures resembling neurofibrillary tangles, neurites of neuritic plaques, and microglialike cells in SDAT brains, but no such staining pattern was detected in normal brain sections. In neurons isolated from SDAT brains, about 40% of the tangles were labeled by the anti-human-2xMT serum with an identical pattern. Other antiserums tested did not preferentially bind tanglelike structures in tissue sections and bound to less than 5% of the tangles in isolated neurons. These results suggest that the antigenic sites of tubulin and NF proteins are not shared by neurofibrillary tangles. Different from the calf preparation, the human-2 x MT fractions contained a prominent protein band that was identical to ferritin in molecular weight and cross-reacted with anti-human-2 x MT and anti-human-ferritin serums. However, antiserums to this ferritinlike protein, or anti-ferritin, did not stain neurofibrillary tangles. Although neither the calf 2 x MT nor two other human MT fractions failed to elicit an antiserum that stained tangles, these fractions were able to remove the antihuman-2 x MT serum activity that binds to tangles. The data suggest that the protein (or proteins) that makes up neurofibrillary tangles of SDAT is present in various quantities in microtubule fractions of normal brain.

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#6166524   1981/09/25 Save this To Up

Immunoelectron microscopy of Kell and Cellano antigens on red cell ghosts.

The ultrastructural arrangement of Kell (K1) and Cellano (K2) antigens on red cells was studied using ferritin-conjugated rabbit antihuman IgG to stain ghosts derived from antibody-sensitized intact red cells. Estimates of the number of sites under equilibrium binding were obtained by counting both ferritin grains and ferritin clusters on electron micrographs. Values for Kell sites on heterozygous red cells ranged from 2300 to 5900 and for Cellano sites from 2000 to 5000 with no discernible dosage effects. Both the Kell and Cellano antigens were clustered, which was due to conjugate staining of the ghost membranes and does not reflect the topological arrangement of these antigens on the native membrane. The ferritin grain patterns found with the Kell and Cellano antigens was similar to those observed with the Rh antigens except for the markedly reduced antigen site density.

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#386711   1979/12/27 Save this To Up

Electron microscopy of treponemes subjected to the Treponema pallidum immobilization (TPI) test. II. Immunoelectron microscopy.

The experiments were carried out in order to investigate whether human IgG globulin is absorbed on to the surface of T. pallidum cells during incubation with human syphilis serum in the Treponema pallidum immobilization (TPI) test. Cells of T. pallidum Nichols subjected to the TPI test were further incubated with ferritin conjugated rabbit antihuman IgG globulin. Human IgG globulin could only be demonstrated on immunoimmobilized cells, i.e. cells incubated with human syphilis serum and unheated guinea pig serum (GPS). The surface of the swollen cells was completely covered by a fuzzy layer on to which the ferritin molecules appeared to be attached. In ultrathin sections of cells obtained from the same suspensions the surface of the outer cell membrane was outlined by ferritin molecules. In these cells a rather wide gap was observed between the outer membrane and the cytoplasmic membrane. The ribosomes seemed to have disappeared from the cytoplasm of the immunoimmobilized treponemes, but were present in motile cells obtained from control incubations.

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#362909   1979/01/26 Save this To Up

Methods for establishing a working immunoradiometric assay for serum ferritin.

The two-site immunoradiometric assay for measurement of serum ferritin requires purified human ferritin and an avid high-titer antihuman ferritin antibody. Some of the antibody is radioiodinated following purification by immunoadsorption. All methods for preparation of these materials for the assay are described in minute detail. Performance of the assay itself and calculation of results are also described, and attention is drawn to several potential pitfalls. Adherence to these detailed descriptions will help to eliminate difficulties experienced by centers wishing to establish their own working serum ferritin assay.

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#197043   1977/10/20 Save this To Up

Immunoelectron microscopic localization of herpes simplex virus antigens in rabbit cornea with antihuman IgG-antiferritin hybrid antibodies.

Sheep antihuman IgG-antiferritin hybrid antibodies were used for the ultrastructural localization of herpes simplex virus (HSV) antigens in rabbit corneas from animals with herpetic keratitis. In animals with epithelial keratitis in which active viral replication is occurring (6 days after infection), viral antigen was found within nuclei, on nuclear membranes, and on cell surface membranes of epithelial cells. In animals with early necrotizing keratitis in which active viral replication cannot be demonstrated (14 to 21 days after infection), viral antigen was found in association with the cell surface of stromal keratocytes. Since lymphocytic cells in intimate contact with degenerating keratocytes have previously been identified in the cornea, these observations provide a basis for the view that cell-mediated immunopathogenesis is involved in the etiology of herpetic stromal keratitis.

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#4372550   1975/02/18 Save this To Up

Ultrastructural localization of herpes simplex virus antigens on rabbit corneal cells using sheep antihuman IgG antihorse ferritin hybrid antibodies.


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#4997756   1971/09/23 Save this To Up

Quantitative two-dimensional ultrastructural distribution of Rh o (D) antigenic sites on human erythrocyte membranes.

A method is described for determining the two-dimensional distribution of specific antigens on cell surfaces, and is applied to the D antigen of the Rh antigenic system. Rh-positive human erythrocytes are allowed to react with purified (125)I-labeled human anti-Rh(o)(D) gamma-globulin antibodies, and the sensitized cells are then lysed at an air-water interface. The residual cell membranes are spread flat by surface forces, and are picked up on a carbon-strengthened collodion-coated electron microscope grid. The membranes are then stained with ferritin-conjugated goat antibodies directed against human gamma-globulins. Only Rh-positive cells sensitized with anti-Rh(o)(D) antibodies bind the ferritin-conjugated antihuman gamma-globulins. The ferritin particles are found in small clusters on the membrane surface, and the number of such clusters per unit area agrees with the number of (125)I-labeled anti-Rh(o)(D) antibodies bound per unit area. The Rh(o)(D) antigenic sites appear to be molecularly dispersed on the membrane surface, but in a random two dimensional array.

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