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Biomedical subjects

L Edelman

Publications and source records attributed to L Edelman.

At least 55 records · Page 3Linked to original sources

An Analysis of Growth Regulator Interactions and Gene Expression during Auxin-Induced Cell Elongation Using Cloned Complementary DNAs to Auxin-Responsive Messenger RNAs.

We have examined the effects of cytokinin, fusicoccin, and ethylene on auxin-induced changes in gene expression during auxin-promoted cell elongation in soybean (Glycine max L. Merr. cv Wayne) using cloned cDNAs to two auxin-responsive mRNAs (Walker, Key 1982 Proc Natl Acad Sci USA 79: 7185-7989). RNA blot analyses demonstrate that under conditions of cytokinin inhibition of auxin-promoted cell elongation the levels of these two auxin-responsive mRNAs is unaltered. Fusicoccin-promoted elongation is not associated with an enhanced expression of these two mRNAs, suggesting that the increased levels of these mRNAs observed during auxin-promoted cell elongation are not simply due to enhanced rates of cell elongation. We have also determined that ethylene plays no apparent role in the regulation of expression of these mRNAs. However, the auxins indole-3-acetic acid, 2,4-dichlorophenoxyacetic acid, and alpha-naphthalene acetic acid all enhance an accumulation of these mRNAs. We conclude that the regulation of these mRNAs is directly dependent on auxin. That auxin-promoted cell elongation is dependent upon the increased accumulation of these mRNAs remains to be determined.

Journal Article↗

A comparative trial of the clinical efficacy and pharmacokinetics of 12-hour and 24-hour controlled release theophylline preparations in patients with chronic asthma.

A double-blind crossover comparison of a 12-hour theophylline preparation (Theo-Dur) and a 24-hour theophylline preparation (Theo-24) was conducted with 20 young adult chronic asthmatic patients requiring daily bronchodilator therapy. The study group included 11 males and nine females ranging in age from 12 to 28 years. Clinical status and serum theophylline levels were monitored during the 4-week dosing interval on each medication. On the last day of each test period subjects were monitored closely throughout a 24-hour period. The results indicated little clinical difference between the two medications although there were statistically significant differences in the pharmacokinetic behavior between the two theophylline preparations.

Adolescent↗

Carbonic anhydrase I is an early specific marker of normal human erythroid differentiation.

The expression of carbonic anhydrase (CA) as a marker of erythroid differentiation was investigated by immunologic and enzymatic procedures. A polyclonal anti-CA antibody was obtained by immunizing rabbits with purified CA I isozyme. This antibody is reactive with CA I but not with CA II. Within blood cells, CA I was only present in erythrocytes, whereas CA II was also detected in platelet lysates by enzymatic assay. Concerning marrow cells, identifiable erythroblasts and some blast cells expressed CA I. Most of the glycophorin A-positive marrow cells were clearly labeled by the anti-CA I antibody. However, rare CA I-positive cells were not reactive with anti-glycophorin A antibodies. We therefore investigated whether these cells were erythroid precursors or progenitors. In cell sorting experiments of marrow cells with the FA6 152 monoclonal antibody, which among hematopoietic progenitors is reactive only with CFU-E and a part of BFU-E, was performed, CA I+ cells were found mainly in the positive fraction. The percentage of CA I+ cells nonreactive with anti-glycophorin A antibodies contained in the two fractions was in the same range as the percentage of erythroid progenitors identified by their capacity to form colonies. In addition, the anti-CA I antibody labeled blood BFU-E-derived colonies as early as day 6 of culture, whereas in similar experiments with the anti-glycophorin A antibodies, they were stained three or four days later. No labeling was observed in CFU-GM- or CFU-MK-derived colonies. The phenotype of the day 6 cells expressing CA I was similar to that of erythroid progenitors (CFU-E or BFU-E): negative for glycophorin A and hemoglobin, and positive for HLA-DR antigen, the antigen identified by FA6 152, and blood group A antigen. Among the cell lines tested, only HEL cells expressed CA I, while K562 was unlabeled by the anti-CA I antibody. In contrast, HEL and K562 cells expressed CA II as detected by a biochemical technique. Synthesis of CA I, as with other erythroid markers such as glycophorin A and hemoglobin, was almost abolished after 12-O-tetradecanoyl-phorbol-13 acetate treatment of HEL cells. In conclusion, CA I appears to be an early specific marker of the erythroid differentiation, expressed by a cell with a similar phenotype as an erythroid progenitor.

Antibody Specificity↗

The effect of diet on the metabolism of long acting theophylline.

Recently some concern has been expressed of the effect of diet on the metabolism of theophylline. This brief trial in normal healthy adults observed the effect of fasting, high fat, low fat, and liquid fat/low carbohydrate diet on the metabolism of a sustained-release theophylline preparation (Theo-Dur). On analysis of the mean theophylline level values, there were no significant differences in the theophylline levels between the diets. However, in certain individuals there were differences in the theophylline absorption rates between diets. No consistent pattern was seen.

Adult↗

A comparative study between animals and monoclonal anti-digitoxin antibodies.

Anti-digitoxin antibodies have been produced by immunizing rabbits and by monoclonal techniques using the same digitoxin-protein conjugate. Titres, inhibition curves, affinities, dissociation and association rate-constants have been investigated for the two antibodies. It appears that the animal immune serum gives better criteria (except specificity) than the monoclonal ones. However, both can be used for quantitative assays, with less sensitivity for the monoclonal antibody. The main advantage of monoclonal production is to conduct large amounts of specific immunoglobulins which are very useful for human administration after a digitalis overdose.

Animals↗

Monoclonal antibodies against blood group antigens.

Monoclonal anti-A, anti-B, anti-H antibodies have been produced by a murine hybridoma. C57BL/6 mice have been immunized by different red blood cells. The main characteristics of these antibodies are the following: specificity: anti-A agglutination only A cells, including A2, A3, Ax (from a panel of 50 cells); anti-B agglutinates only B cells (B3, Bx, cis Ab and acquired B). Anti-H agglutinates all cells except H-deficient red cells. inhibition: it is only inhibited by the saliva of each corresponding secretor subject. immunofluorescence tests: it is able to detect A,B,H antigens on tissue sections, kidney, pancreas, liver. thermodynamics: the association constant is 2.10(7) 1/ml (for anti-A) and 3.10(8) for anti-B and anti-H. All are IgM. Monoclonal anti-N, and some anti-public antibodies such as anti-gerbich and anti-Rh 17 have been obtained too. All these antibodies could be useful as reagents and for the study of weak groups.

ABO Blood-Group System↗

A monoclonal antibody directed against the homologous N-terminal domain of glycophorin A and B.

A monoclonal antibody (iB5, IgG1 kappa) reacting with human red cells was produced after immunization of BALB/C mice with cord red cells, followed by fusion of the spleen cells with the murine myeloma cell line Ag 8-653. The monoclonal antibody agglutinated blood group N+ much better than M + N-red cells but did not recognize erythrocytes from rare individuals typed as M + N-S-s-U- and those from an En(a-) individual (M.E.P.). However, S-s-U- donors typed as M + N + or M-N+ and En(a-) red cells from donor G.W. were agglutinated. The erythrocyte receptors for iB5 are completely destroyed by papain treatment and significantly decreased by neuraminidase. Interestingly also, the iB5 antibody failed to agglutinate trypsin-treated N+M-S-s-U- erythrocytes. Other investigations have shown that the monoclonal antibody precipitated glycophorin A and B from N+ red cells and only glycophorin B from M+N-erythrocytes. The reactivity of iB5 was further explored by immunostaining following the electrophoretic transfer to nitrocellulose sheets of membrane proteins from common (M and N) and rare erythrocytes [En(a-),S-s-U-, MgMg, McM, St(a+), Mi.V, Mi.III, Tn] separated by SDS-polyacrylamide gel electrophoresis. These studies have clearly demonstrated that the monoclonal iB5 antibody is directed against the homologous N-terminal domain of glycophorin A and B, a specificity which explains the serological reactivity of iB5 against common and rare erythrocytes.

Animals↗

Preparation and experimentation of an antidigitalin monoclonal antibody: interest in human treatment.

A monoclonal antidigitalin antibody was obtained following the immunization of BALB/mice with digitalin coupled to BSA, and the fusion of lymphocytes from these mice with murin myeloma 8653. The supernatants were screened by a radioimmunoassay in which the supernatant was incubated with digitalin coupled to I125. This monoclonal antibody "Dig 278" has an antigen binding ratio of 95%; is an IgGl; has a titre of 1/1000 and its affinity constant, as determined by a Scatchard plot, was 1,20(9) L/M. By experimenting with the monoclonal antibodies on 15 rabbits, we have obtained the reversal of heart rhythm disorders and the survival of animals injected with a lethal dose of digitalin. All the controls died. This antibody could prove useful in treating advanced cases of digitalin intoxication and for which no satisfactory treatment is available at present.

Animals↗

Murine monoclonal antibodies against Gerbich antigens.

Two murine monoclonal antibodies (E11-1 and MR4-130) agglutinated all samples of human red cells except those of the Ge (-1, -2, -3) phenotype. It was possible to demonstrate that these antibodies recognize two different epitopes of the Gerbich antigen.

Animals↗

A murine monoclonal antibody against blood group H type-1 and -2 structures.

A murine anti-H monoclonal antibody was produced. This antibody, called sp115, is an IgM that does not agglutinate classical Bombay. Sp115 may differentiate the two categories of H-deficient phenotypes. It detects H substance in both plasma and fresh saliva. Tissue antigen is found when using this antibody. The specificity of sp115 antibody was determined by adsorption with, and elution from synthetic oligosaccharide immunoadsorbents. Sp115 does not distinguish H type-1 and H type 2-structures.

ABO Blood-Group System↗

Study of blood group B antigen with a specific monoclonal antibody (anti-B, b-183).

A murine anti-B monoclonal antibody was obtained by the hybridoma technique. This antibody called anti-B (b-183) is of IgM nature; it is capable of agglutinating normal B, B3, Bx, cis AB and some acquired B red cells. Its association constant is 1.1 X 10(8) l/mol, and appears high compared to those of the monoclonal anti-A. This monoclonal anti-B was used to determine the number of B sites on B3 and Bx red cells.

ABO Blood-Group System↗

[Production of an anti-digitalin monoclonal antibody (author's transl)].

Anti-digitalin monoclonal antibodies were obtained by hybridization of lymphoid cells from mice immunized with the drug and the 8653 myeloma cells from BALB/c Mice. Two of these antibodies were submitted to immunochemical analysis which revealed that they belonged to IgM and IgGl classes, and the high affinity of one of them (1,2 x 10(9) M(-1)). The availability os such antibodies opens new perspectives for the treatment of digitalin intoxication and the possibility of establishing a standardized radioimmunoassay.

Animals↗

Thermodynamic and immunological properties of a monoclonal antibody to human blood group A.

A murine anti-A monoclonal antibody was obtained by the hybridoma technique. This antibody, of an IgM nature, is capable of agglutinating A1, A2 and A3 red blood cells. Thermodynamic study confirmed its monoclonal character; its association constant is 1,6 10(6) l/mole. The enthalpy change of the antigen/antibody reaction is nul which indicates the absence of the role of temperature on antibody fixation. This weak affinity makes it necessary to concentrate the supernatant so as to enable use of these reagents under the same conditions as those used at present.

ABO Blood-Group System↗

[Technics and applications of transfer factor (author's transl)].

Transfer factor is produced by dialysis of repeatedly frozen and thawed pooled buffy coats of healthy blood donors. However, "specific Transfer Factor" of bacteriological or mycological type, prepared from hyperimmunized donors would be more effective for restoring cellular immunity.

Hematologic Diseases↗