scholarly journals Identification with a monoclonal antibody of a predominantly B lymphocyte-specific determinant of the human leukocyte common antigen. Evidence for structural and possible functional diversity of the human leukocyte common molecule.

1981 ◽  
Vol 153 (4) ◽  
pp. 753-765 ◽  
Author(s):  
R Dalchau ◽  
J W Fabre
Keyword(s):  
Monoclonal Antibody ◽  
B Lymphocyte ◽  
Human Leukocyte ◽  
Affinity Column ◽  
Discrete Population ◽  
And Function ◽  
Leukocyte Populations ◽  
Inhibition Studies ◽  
Cross Inhibition ◽  
Functional Consideration

Initial studies with the monoclonal antibody F8-11-13 described in this paper showed that it reacted strongly with B lymphocytes, did not react at all with granulocytes, and reacted only weakly with a small subpopulation of thymocytes and peripheral T lymphocytes. This picture was entirely different from that seen with monoclonal antibodies to the leukocyte common (LC) antigen, where 100% of all the above-mentioned leukocyte populations were positive. Biochemical studies using detergent solubilized membranes labeled with 3H at the sialic acid residues showed that the molecule bearing the F8-11-13 determinant was a glycoprotein of 215,000 mol wt, and that the peak depleted by F8-11-13 monoclonal antibody affinity columns corresponded to the high molecular weight region of a broad peak previously shown to be completely depleted by monoclonal antibody (F10-89-4) affinity columns directed at the LC antigen. Proof that the F8-11-13 determinant was expressed on some LC molecules was established by cross-inhibition studies with affinity-column-purified and depleted material. This finding of a serologically identifiable conformational or other structural change selectively expressed on the LC molecule of a functionally discrete population of lymphocytes has interesting implications for the structure and function of the LC molecule, and might be relevant to functional consideration of other membrane molecules.

scholarly journals OMIP 077: Definition of all principal human leukocyte populations using a broadly applicable 14‐color panel

2021 ◽  
Author(s):  
Maximilian Boesch ◽  
Martina Sykora ◽  
Silvia Gasteiger ◽  
Florent Baty ◽  
Martin H. Brutsche ◽  
...  
Keyword(s):  
Human Leukocyte ◽  
Definition Of ◽  
Leukocyte Populations

scholarly journals IFN-γ Enhances the Antimyeloma Activity of the Fully Human Anti–Human Leukocyte Antigen-DR Monoclonal Antibody 1D09C3

2007 ◽  
Vol 67 (7) ◽  
pp. 3269-3275 ◽  
Author(s):  
Carmelo Carlo-Stella ◽  
Anna Guidetti ◽  
Massimo Di Nicola ◽  
Cristiana Lavazza ◽  
Loredana Cleris ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Human Leukocyte Antigen ◽  
Human Leukocyte ◽  
Leukocyte Antigen ◽  
Ifn Γ

scholarly journals Mouse Strain Differences in Plasmacytoid Dendritic Cell Frequency and Function Revealed by a Novel Monoclonal Antibody

2003 ◽  
Vol 171 (12) ◽  
pp. 6466-6477 ◽  
Author(s):  
Carine Asselin-Paturel ◽  
Géraldine Brizard ◽  
Jean-Jacques Pin ◽  
Francine Brière ◽  
Giorgio Trinchieri
Keyword(s):  
Monoclonal Antibody ◽  
Dendritic Cell ◽  
Mouse Strain ◽  
Plasmacytoid Dendritic Cell ◽  
Strain Differences ◽  
Cell Frequency ◽  
And Function ◽  
Mouse Strain Differences

scholarly journals Functional study of a monoclonal antibody to IgE Fc receptor (Fc epsilon R2) of eosinophils, platelets, and macrophages.

1986 ◽  
Vol 164 (1) ◽  
pp. 72-89 ◽  
Author(s):  
M Capron ◽  
T Jouault ◽  
L Prin ◽  
M Joseph ◽  
J C Ameisen ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
B Lymphocyte ◽  
Specific Binding ◽  
Polyclonal Antibodies ◽  
Fc Receptor ◽  
The Other ◽  
Functional Study ◽  
Low Density ◽  
Fluorescence Staining ◽  
Ige Binding

An IgM mAb (BB10) was produced by immunization of mice with human eosinophils purified according to their abnormal low density ("hypodense" cells), and previously shown to exhibit increased IgE-dependent antiparasite cytotoxicity. This BB10 antibody, selected for positive fluorescence staining of hypodense blood or lung eosinophils and low or negative staining of normodense eosinophils or neutrophils, could strongly inhibit IgE-dependent cytotoxicity of human eosinophils and platelets. The specificity for the IgE Fc receptor was suggested by the high levels of inhibition of IgE rosettes formed by eosinophils after incubation with the purified IgM fraction of BB10, whereas other receptors (Fc gamma R, CR1) were not affected. On the other hand, BB10, able to inhibit rat eosinophil Fc epsilon R, did not react with the IgE Fc receptor on mast cells or basophils. A technique using radioiodinated BB10 allowed us to quantify the specific binding of BB10 to human eosinophils and platelets. Competition experiments revealed a crossinhibition between the binding of BB10 and IgE, suggesting the specificity of BB10 for the IgE binding site of eosinophil, platelet, and monocyte Fc epsilon R. Three proteins having extrapolated Mr of 32,000, 43,000-45,000, and 97,000 were found in the platelet extract eluted from a BB10 or from an IgE immunosorbent column. These findings confirm the similarities between IgE Fc receptors on human eosinophils, platelets, and macrophages, already observed with polyclonal antibodies directed against the B lymphocyte Fc epsilon receptor. They suggest, moreover, that the mAb BB10 can represent a good reagent for further investigations on the structure and the functions of this IgE Fc receptor (Fc epsilon R2).

Cytokine release and dynamics of leukocyte populations after CD3/TCR monoclonal antibody treatment

1992 ◽  
Vol 12 (3) ◽  
pp. 170-177 ◽  
Author(s):  
Gerhard J. Zlabinger ◽  
Karl M. Stuhlmeier ◽  
Reinhard Eher ◽  
Sabine Schmaldienst ◽  
Renate Klauser ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cytokine Release ◽  
Antibody Treatment ◽  
Monoclonal Antibody Treatment ◽  
Leukocyte Populations

A human leukocyte antigen identified by a monoclonal antibody

1981 ◽  
Vol 3 (3) ◽  
pp. 231-245 ◽  
Author(s):  
Ann E. Berger ◽  
Janet E. Davis ◽  
Peter Cresswell
Keyword(s):  
Monoclonal Antibody ◽  
Human Leukocyte Antigen ◽  
Human Leukocyte ◽  
Leukocyte Antigen

Assembly and function of Chlamydomonas flagellar mastigonemes as probed with a monoclonal antibody

1996 ◽  
Vol 109 (1) ◽  
pp. 57-62 ◽  
Author(s):  
S. Nakamura ◽  
G. Tanaka ◽  
T. Maeda ◽  
R. Kamiya ◽  
T. Matsunaga ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Beat Frequency ◽  
Distal Portion ◽  
Distal Region ◽  
Ring Structure ◽  
Live Cells ◽  
Swimming Velocity ◽  
Flagellar Beat ◽  
Original Length ◽  
And Function

Mastigonemes are hair-like projections on the flagella of various kinds of lower eukaryotes. We obtained a monoclonal antibody (mAb-MAST1) to mastigonemes of Chlamydomonas reinhardtii, and found that it reacts with a single flagellar glycoprotein of about 230 kDa. Interestingly, immunofluorescence microscopy demonstrated that mAb-MAST1 recognizes not only the flagellar mastigonemes but also a ring composed of 10 or more particles located in the anterior end of the cell body close to the flagellar bases. The ring structure may be the pool of the mastigoneme protein. When the flagella are amputated, they regenerate to their original length in 90–120 minutes. We found that mastigonemes appear on the new flagellar surface as early as 15 minutes after deflagellation, and that new mastigonemes are mostly assembled onto the distal region of the flagellar surface. Mastigonemes thus appear to be inserted into the membrane only in the distal region of the flagellum. Alternatively, mastigonemes may be inserted at the base and transported very rapidly to the distal portion where they are trapped. When live cells are treated with mAb-MAST1, mastigonemes disappear from the flagellar surface. In these mAb-MAST1 treated cells, the swimming velocity decreases to 70–80% of the normal value, although the flagellar beat frequency increases to approximately 110% of the control. These findings demonstrate vectorial transport of mastigonemes to their assembly sites, and show that mastigonemes function to increase flagellar propulsive force by increasing the effective surface of the flagellum.

scholarly journals The Role of HLA-G in Tumor Escape: Manipulating the Phenotype and Function of Immune Cells

2020 ◽  
Vol 10 ◽  
Author(s):  
Lu Liu ◽  
Lijun Wang ◽  
Lihong Zhao ◽  
Chen He ◽  
Ganlu Wang
Keyword(s):  
T Cells ◽  
Tumor Immunity ◽  
Immune Cells ◽  
Human Leukocyte ◽  
Therapeutic Benefit ◽  
Tumor Escape ◽  
Class I Mhc ◽  
Mhc I ◽  
Suppressive Phenotype ◽  
And Function

Human leukocyte antigen-G (HLA-G) is a non-classical major histocompatibility complex class I (MHC I) molecule, and under physiological conditions, its expression is strictly restricted to the maternal–fetal interface and immune-privileged organs where HLA-G is expected to contribute to establishment and maintenance of immune tolerance. However, the expression of HLA-G has been found in various types of tumors, and the level of its expression frequently correlates with high-grade histology and poor prognosis, raising the possibility that it may play a negative role in tumor immunity. ILT2 and ILT4, present on a broad of immune cells, have been identified as the main receptors engaging HLA-G, and their interactions have been found to allow the conversion of effectors like NK cells and T cells to anergic or unresponsive state, activated DCs to tolerogenic state, and to drive the differentiation of T cells toward suppressive phenotype. Therefore, tumors can employ HLA-G to modulate the phenotype and function of immune cells, allowing them to escape immune attack. In this review, we discuss the mechanism underlying HLA-G expression and function, its role played in each step of the tumor-immunity cycle, as well as the potential to target it for therapeutic benefit.

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