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G P Herr

Publications and source records attributed to G P Herr.

14 recordsLinked to original sources
PubMed1998

Expression of neutrophil antigens after 10 days of granulocyte-colony-stimulating factor.

BACKGROUND: Granulocyte-colony-stimulating factor (G-CSF) is becoming the standard agent for mobilizing granulocytes. Most granulocyte donors are given a single dose of G-CSF, but in some cases they are given G-CSF for several days, and multiple granulocyte concentrates are collected. The administration of a single dose of G-CSF induces several changes in the expression of neutrophil antigens, but the effects of multiple daily doses of G-CSF are not known. STUDY DESIGN AND METHODS: Seven healthy people received 5 microg per kg of G-CSF for 10 days. Their expression of several neutrophil antigens before, during, and after the administration of G-CSF was analyzed through the use of flow cytometry. RESULTS: The expression of L-selectin (CD62L), Fcgamma receptor (FcgammaR) III (FcgammaRIII, CD16), and the leukocyte function antigen (CD11a) decreased throughout the course of G-CSF administration, while the expression of FgammaR I (FcgammaRI, CD64) and lipopolysaccharide-binding protein receptor (CD14) increased. The expression of FcgammaR II (FcgammaRII, CD32) also increased, but not until the fourth day of G-CSF administration. The expression of amino peptidase N (CD13), C3bi receptor (CD11b), and the neutrophil beta2 integrin unit (CD18) did not change during the administration of G-CSF, but that of both CD13 and CD18 increased 3 days after the last dose. The expression of neutrophil-specific antigen NB1 initially increased, returned to pre-G-CSF levels after 4 days, and then increased again after 10 days of G-CSF administration. CONCLUSION: Changes in the expression of several neutrophil antigens occurred throughout a 10-day course of G-CSF Most of the changes occurred after one dose, but additional changes occurred later in the 10-day course and after its completion. These changes may affect the function of G-CSF-mobilized granulocytes.

Adult↗
PubMed1996

Analysis of the expression of NB1 antigen using two monoclonal antibodies.

BACKGROUND: Neutrophil-specific antigen NB1 is expressed on neutrophil subpopulations in 97 percent of healthy individuals and is located on 56- to 64-kDa glycoprotein. While the molecule carrying NB1 has been identified, the nature of the NB1 epitope has not been well characterized. STUDY DESIGN AND METHODS: Two monoclonal antibodies (MoAbs), 1B5 and the recently produced 7D8, and four alloantibodies, all specific for NB1, were used to investigate the expression of NB1 on neutrophils from several donors. RESULTS: MoAb 7D8 was shown to be specific for NB1. It reacted with NB1-positive neutrophils from 52 donors in the granulocyte immunofluorescence assay and did not react with NB1-negative neutrophils from 8 donors. MoAb 7D8 immunoblotted a 56- to 64-kDa molecule on neutrophils from eight NB1-positive donors and did not react with this molecule on NB1-negative neutrophils from two donors. When 7D8 was tested in the monoclonal antibody immobilization of granulocyte antigens assay, it reacted with two NB1 alloantibodies, but not with NA1 or NA2 alloantibodies. To determine if MoAbs 7D8 and 1B5 recognized the same epitope, both were tested against the same NB1-positive neutrophils and the cells were analyzed by two-color flow cytometry. Both antibodies bound independently to neutrophils, which indicated that the antibodies recognized different epitopes. When similar studies were performed with MoAb 7D8 and three NB1 alloantibodies, 7D8 partially inhibited the binding of two of the alloantibodies. The size of the NB1-positive subpopulation was analyzed in 25 people using flow cytometry with both MoAbs and three alloantibodies. The subpopulation of antigen-positive cells was similar in all donors when 7D8 and the three NB1 alloantibodies were tested; however, the subpopulation recognized by MoAb 1B5 was smaller in two of the donors. Neutrophils from one of these people were analyzed by immunoblotting, and no differences were detected in the molecule carrying NB1 in those neutrophils and that molecule in control neutrophils. CONCLUSION: NB1 specificity is made up of at least two separate epitopes. The expression of NB1 varied among antigen-positive individuals. While NB1 is expressed by a 56- to 64-kDa glycoprotein, the structure of this protein on antigen-negative cells has not been determined.

Animals↗
PubMed1995

The chemical and immunoglobulin structural features necessary for reactions of quinine-dependent antibodies to neutrophils.

BACKGROUND: Previously described were three patients with quinine-dependent antibodies to neutrophils, platelets, and red cells who had episodic pancytopenia and renal failure. The nature of the antibody-drug-neutrophil interactions was investigated with sera from these patients. STUDY DESIGN AND METHODS: Sera from all three patients were tested against neutrophils in flow cytometry in the presence of several compounds related to quinine. IgG and Fab and F(ab')2 fragments were prepared from the serum of one patient and tested against neutrophils in flow cytometry and immunoprecipitation in the presence of quinine and related compounds. RESULTS: In flow cytometry, sera from all three patients plus quinidine reacted with neutrophils. Sera from Patients 1 and 3 reacted with neutrophils in the presence of cinchonidine (desmethoxy-quinine) and serum from Patient 3 also reacted with neutrophils in the presence of cinchonine (desmethoxy-quinidine). None of the sera reacted with neutrophils in the presence of chloroquine or primaquine. Serum from Patient 3 plus quinolinic acid, a tryptophan metabolite, reacted with neutrophils, but sera from the other two patients did not. Patient 3 serum plus tryptophan or another tryptophan metabolite, quinalidic acid, did not react with neutrophils. IgG from Patient 3 serum reacted with neutrophils in flow cytometry in the presence of quinine, quinidine, cinchonidine, cinchonine, and quinolinic acid. F(ab')2 fragments plus quinine or cinchonidine also reacted with neutrophils, but Fab fragments plus quinine did not. In the presence of quinine, Patient 3 IgG immunoprecipitated the 85- and 60-kDa molecules and F(ab')2 fragments immunoprecipitated the 85-kDa molecule. Patient 3 serum plus quinidine, cinchonidine, cinchonine, and quinolinic acid immunoprecipitated the 130- and 85-kDa molecules, but not the 60-kDa molecule. CONCLUSION: Quinine-dependent neutrophil antibodies often react with neutrophils in the presence of quinidine and related compounds. These reactions were mediated by the F(ab')2 domain of IgG.

Autoantibodies↗
PubMed1994

Identification of a new white cell antigen.

BACKGROUND: Antibodies to white cell antigens can cause alloimmune neonatal neutropenia, autoimmune neutropenia, and transfusion reactions. CASE REPORT: A full-term male infant developed a skin infection and was found to be neutropenic on his fourth day of life. He had a transient increase in his neutrophil count after treatment with intravenous immunoglobulin, but his neutrophil count was not consistently normal until he was 6 weeks old. Serum from the baby's mother reacted in a granulocyte immunofluorescence assay but not in a granulocyte agglutination assay. The mother's serum was tested in the granulocyte immunofluorescence assay against neutrophils from 103 healthy, unrelated people, and it reacted with cells from 66 percent of those people. The expression of SL correlated weakly with the expression of NA1 (r = 0.23; p = 0.02) and 5a (r = 0.20; p = 0.05) antigens. SL antigen expression on neutrophils was not associated with the expression of NA2, NB1, NB2, NC1, 5b, 9a, or Mart. The expression of SL on neutrophils from members of an extended family was analyzed, and the antigen was found to be inherited in an autosomal-dominant manner. Anti-SL also reacted with T-lymphocytes in a flow cytometry assay but did not react with red cells or platelets. No lymphocytotoxic antibodies were detected in the mother's sera. The anti-SL was tested against neutrophils in an immunoprecipitation and immunoblotting assay, but no molecules were identified. The neutrophil-specific antigens NA are located on Fc gamma receptor III (CD16). To determine if the SL antigen was also located on Fc gamma receptor III, anti-SL was also tested in a monoclonal antibody immobilization of granulocyte antigens assay. Anti-SL did not react with molecules recognized by CD16 monoclonal antibodies. CONCLUSION: A new white cell antigen SL, with a frequency of 66 percent, was identified on neutrophils and T-lymphocytes as a result of the evaluation of a case of neonatal alloimmune neutropenia. The molecule bearing the SL antigen was not identified in immunoblotting, immunoprecipitation, or monoclonal antibody immobilization of granulocyte antigens assays.

Adult↗
PubMed1994

Neutrophil-specific antigen NB1 inhibits neutrophil-endothelial cell interactions.

Neutrophil-specific antigen NB1 is located on a 58 to 64 kd glycosyl phosphatidylinositol-linked plasma membrane glycoprotein. NB1 antigen can be detected on neutrophils from 97% of healthy volunteers, and NB1 antigen is expressed on subpopulations of neutrophils. Neutrophil subpopulations with varying functions have been described, and we hypothesize that NB1 antigen may play an important role in neutrophil function. We compared the function of NB1-positive and NB1-negative neutrophils obtained from several persons. There were no differences in the adhesion of NB1-positive and NB1-negative neutrophils incubated in C5a, N-formyl-Met-Leu-Phe (FMLP), phorbol myristate acetate (PMA), or buffer to type IV collagen, fibronectin, laminin, or polystyrene. However, the adherence to human umbilical vein endothelial cells (HUVEC) monolayers of unstimulated NB1-positive neutrophils was less than to NB1-negative neutrophils (20.0% +/- 4.2% vs 31.7% +/- 5.8%; p < 0.01). When neutrophils were stimulated with C5a, PMA, or FMLP, no differences were found in the adhesion of NB1-positive and NB1-negative cells to the same surfaces. When NB1-positive neutrophils were incubated with rabbit polyclonal anti-NB1 Fab fragments, their adherence to HUVEC was increased (32.9% +/- 10.1% vs 18.3% +/- 5.0%; p < 0.05). Fab fragments prepared from normal rabbit serum had no effect on neutrophil adherence to HUVEC. The chemotaxis of NB1-positive neutrophils to FMLP through nitrocellulose was significantly greater than that of NB1-negative neutrophils (p = 0.03), but there was no difference in chemotaxis to FMLP through polycarbonate membranes.(ABSTRACT TRUNCATED AT 250 WORDS)

Antibodies↗
PubMed1993

Quinine-dependent antibodies to neutrophils react with a 60-Kd glycoprotein on which neutrophil-specific antigen NB1 is located and an 85-Kd glycosyl-phosphatidylinositol-linked N-glycosylated plasma membrane glycoprotein.

We have previously described a 24-year-old woman with quinine-dependent antibodies that reacted with neutrophils, red blood cells (RBCs), platelets, and T lymphocytes. The drug-dependent neutrophil antibody was found to react with 85- and 60-Kd neutrophil membrane molecules. In these studies, we further characterized these molecules and found that both were glycosyl-phosphatidylinositol (GPI)-linked and contained sialic acid residues and N-linked carbohydrate side chains, but neither contained O-linked carbohydrates. The protein backbone of the 60-Kd molecule was 45 Kd, and the 85 Kd glycoprotein (GP) was made up of 33- and 31-Kd proteins. While some GPI-anchored neutrophil GPs are released by stimulated neutrophils, neither the 85- nor the 60-Kd GP was released by neutrophil stimulated with C5a, f-met-leu-phe (FMLP), or phorbol myristate acetate (PMA). Neutrophil-specific antigen NB1 is located on a 58- to 64-Kd GP. To determine if the quinine-dependent antibody and anti-NB1 recognize the same GP, immunoprecipitation studies were performed with the quinine-dependent antibody using neutrophils with varying NB1 phenotypes. The 60-Kd GP was detected on NB1-positive neutrophils from 11 of 12 donors tested, but not on NB1-negative neutrophils from two donors tested. After solubilized 125I-labeled neutrophils were absorbed with anti-NB1, the quinine-dependent antibody immunoprecipitated the 85-Kd GP, but not the 60-Kd GP. These results indicate that anti-NB1 and the quinine-dependent antibody identified the same GP. The 85-Kd GP was detected on neutrophils from all 14 donors tested. The electrophoretic mobility of the 85-Kd GP was similar to the electrophoretic mobility of the major 125I-labeled neutrophil protein.

Adult↗
PubMed1993

Analysis of the expression of neutrophil-specific antigen NB1: characterization of neutrophils that react with but are not agglutinated by anti-NB1.

The neutrophil-specific NB antigen system has been serologically characterized with human alloantisera. Two alleles, NB1 and NB2, have been described. NB1 is expressed on a subpopulation of peripheral blood neutrophils in 97 percent of healthy donors. Human alloantibodies have been used to identify the 58- to 64-kDa glycoprotein (GP) on which NB1 is located. NB1 can usually be detected by both a granulocyte immunofluorescence (GIF) assay and a granulocyte agglutination (GA) assay, but neutrophils from some donors have been found to react with anti-NB1 in GIF but not in GA assays. To determine if the latter neutrophils express NB1 and the corresponding 58- to 64-kDa GP, these neutrophils were probed with rabbit and human sera specific for NB1. First, the proportion of neutrophils that express NB1 was quantitated. Neutrophils from donors that typed as NB1-positive in both GA and GIF assays were analyzed by flow cytometry with antisera to NB1. Human and rabbit anti-NB1 reacted with 71 +/- 17 percent and 70 +/- 17 percent of neutrophils, respectively. There was no difference in the expression of NB1 in NB1-homozygous and NB1-heterozygous individuals. In contrast, significantly fewer neutrophils from four donors that typed as NB1-positive in GIF assay but not GA assay reacted with human (27 +/- 12%; p < 0.001) and rabbit (26 +/- 12%; p < 0.001) anti-NB1. When neutrophils from these same four donors were probed with rabbit and human anti-NB1 by immunoblotting and immunoprecipitation, the 58- to 64-kDa GP was identified.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1982

Comparison of i. m. diazepam and hydroxyzine as premedicants.

The effectiveness of diazepam as premedication when administered by two different i.m. techniques was compared with hydroxyzine in 84 male and 101 female patients. Variables studied were relief of anxiety, sedation, acceptance by both patient and anaesthetist and pain at the injection site. Diazepam 20 mg in male and diazepam 10 mg in female patients administered by a Z-track injection technique were as effective premedicants as hydroxyzine 100mg i.m. In men diazepam was good as hydroxyzine regardless of the injection technique. In women the technique of injection of the diazepam was critical to achieving good results. The Z-track injection method decreased the amount of severe pain on injection in both sexes to levels similar to those achieved with hydroxyzine.

Adolescent↗
PubMed1980

Lorazepam and morphine for i.v. surgical premedication.

The effect of i.v. lorazepam alone, in doses of 2 mg and 4 mg, and combined with morphine 5 mg, were studied. Sedation, relief of anxiety, lack of recall, patient acceptance, physician acceptance and side-effects were evaluated. The addition of morphine to lorazepam significantly improved sedation and relief of anxiety. Physician acceptance and patient acceptance showed no significant difference between any of the combinations. Lack of recall was enhanced by increasing the dose of lorazepam from 2 mg to 4 mg, independent of the addition of morphine. The only significant side-effect was restlessness which occurred in 15% of patients receiving lorazepam 4 mg and 3% of patients receiving lorazepam 2 mg, again independent of the addition of morphine.

Adolescent↗
PubMed1979

Diazepam and droperidol as i.v. premedicants.

The effects of i.v. diazepam and droperidol both alone and in combination administered as premedication were studied in 240 patients. Relief of anxiety, sedation, lack of recall, acceptance by both patient and physician and side-effects were evaluated. Overall, the combination of droperidol 2.5 mg with diazepam 5 mg produced better ratings of these variables than could be achieved with either droperidol 10 mg or diazepam 10 mg alone. Larger doses of droperidol with diazepam produce an increased frequency of anxiety; larger doses of diazepam with droperidol may cause over-sedation.

Adolescent↗
PubMedDate not supplied

Characterization of the neutrophil molecules identified by quinine-dependent antibodies from two patients.

BACKGROUND: Two patients with episodic pancytopenia and renal failure associated with quinine (Qn) ingestion were previously found to have Qn-dependent antibodies that reacted with red cells, platelets, and neutrophils. The purpose of these studies was to characterize the neutrophil antigens recognized by Qn-dependent antibodies from these two patients. STUDY DESIGN AND METHODS: The neutrophil molecules recognized by the Qn-dependent antibodies in the sera from the two patients were analyzed by immunoprecipitation using 125I-labeled neutrophils. Neutrophils from 13 different donors were tested. RESULTS: The Qn-dependent antibodies from Patient 1 immunoprecipitated a 60-kDa molecule on neutrophils from seven donors and an 85-kDa molecule on neutrophils from three donors. The Qn-dependent antibodies from Patient 2 reacted with a 32-kDa molecule on neutrophils from 5 donors, a 60-kDa molecule on neutrophils from 9 donors, and an 85-kDa molecule on neutrophils from 10 donors. Neutrophil-specific antigen NB1 is also located on a 60-kDa glycoprotein (GP). While the antibody in serum from Patient 1 did not show specificity for NB1, the antibody from Patient 2 detected the 60-kDa molecule on NB1-positive neutrophils from 9 of 11 donors tested and did not detect the 60-kDa molecule on NB1-negative neutrophils from 2 donors. In a monoclonal antibody immobilization of granulocyte antigens assay, the Qn-dependent antibody from both patients reacted with the 60-kDa molecule carrying NB1. The Qn-dependent antibody from a third patient, Patient 3, was previously found to react with an 85-kDa GP and the 60-kDa NB1 GP. To determine if the Qn-dependent antibodies from Patients 2 and 3 recognized the same 85-kDa GP, neutrophils were treated with serum from Patient 3 plus Qn to remove the 85-kDa GP. Then, serum from Patient 2 plus Qn no longer immunoprecipitated the 85-kDa GP. CONCLUSION: The antigens recognized by Qn-dependent neutrophil antibodies were located on molecules of 85, 60, and 32 kDa. Qn-dependent antibodies from two patients reacted with the same 85-kDa GP and those from three patients reacted with the same 60-kDa GP. The 60-kDa molecule recognized by the Qn-dependent antibodies carried the NB1 antigen.

Antibodies↗