Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P06126 (CD1a)
 2,221 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We examined the expression of various CD coded or not yet defined antigens in human thymus samples using indirect immunoperoxidase and immunoflourescent techniques. Data obtained are presented in concurrence with Clusters of Thymic Epithelial Staining (CTES) classification for various monoclonal antibodies recognizing CD antigens (CD1, CD1a, CD6, CD9, CD14, CD16, CD29, CD30, CD32, CD44, CD45RB, CD47, CD48, CD49a, CD49b, CD49c, CD49d, CD49e, CD49f, CD51, CD53, CD54, CD56, CD57, CD63, CD85, CD95, CD98, CD102, CD103, CD106, CD109, CD146, CD147, CD148, CD151, CD152, CD158a, CD158b, CD164, CD165, CD166) and for monoclonal antibodies 1B10, 5G7, A4, BD46, BLTZ, HP1C5, IND.64, M72, WU947 whose specifities are not yet defined. Some of the mAbs such as CD49f, IND.64 and BD46 are detected as good markers for specific cell types or compartments. Significance of the presence of these antigens on thymic epithelial cells at certain locations is briefly discussed.
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PMID:Antigenic profile of human thymus in concurrence with "Clusters of Thymic Epithelial Staining" classification. 1272 40

To investigate the influence and mechanisms of CD47 engagement by its soluble mAb B6H12 on the maturation and function of cultured dendritic cells (DCs), monocyte-derived DCs were propagated in granulocyte-macrophage colony stimulating factor (GM-CSF) combined with lipopolysaccharide (LPS) and interleukin (IL)-4, in the presence or absence of soluble anti-CD47 monoclonal antibodies (anti-CD47 mAbs, B6H12). The characteristic morphology of DCs was identified by using the transmission electron microscopy. Flow cytometry was used to detect the cell surface phenotypes. The concentration of IL-12 P70 in supernatant was measured by ELISA. The antigen-presenting functions of DCs were determined in one-way mixed leukocyte reaction by BrdU-ELISA. Electrophoretic mobility shift assay (EMSA) was applied to examine the activity of NF-kappaB. The results indicated that the anti-CD47 mAbs markedly suppressed the expression of CD80, CD86, CD83, CD1a and HLA-DR on the surface of DCs (P < 0.05). The data of the mixed leukocyte reaction and IL-12 P70 production were consistent with the results by flow cytometry (P < 0.01). Pre-exposure to B6H12 mAb during the development of DCs resulted in a dramatic depletion of the DNA binding activity of NF-kappaB toward nucleus protein. Moreover, such an inhibition effect seemed to be dose dependent. In conclusion, the soluble mAb B6H12 inhibits the expression of the costimulatory molecules and MHCII molecules on the DCs. The antigen-presenting function of DCs was also impaired by B6H12. And these modulations are closely related with the depletive DNA binding activity of NF-kappaB. It is suggested that the soluble B6H12 exerts a negative effect on the maturation and function of in vitro cultured DCs due to inhibition of NF-kappaB binding activity.
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PMID:Anti-CD47 monoclonal antibody (B6H12) impairs the maturation and function of human dendritic cells. 1585 75

A panel of 380 commercially available monoclonal antibodies (mAbs) against human CD molecules from various sources was tested during the 8th Human Leukocyte Differentiation Antigen Workshop (HLDA8) for cross-reactivity on canine peripheral blood leukocytes by flow cytometry. In addition, all mAbs were used to label a 50:50 mixture of platelets and erythrocytes of the same dogs. This testing resulted in 51 cross-reacting mAbs. mAbs with specificity for CD9, CD29, CD42a, CD61, and CD41/CD61 showed cross-reactivity with canine platelets in a non-polymorphic and one mAb with the erythrocyte antigen CD235a in a polymorphic reaction pattern. Canine leukocyte-reactive mAbs included those with specificity for CD11a, CD11b, CD14, CD18, CD21, CD22, CD47, CD49d, CD49e, CD56, CD62L, CD91, CD94, and CD172a. In addition, several mAbs resulted in a staining pattern of canine cells which suggest that the canine epitope equivalents have an alternate expression pattern from that expected for humans (CD1a, CD35, CD44, CD45, CD75s, CD81). In summary, this study confirmed the reactivity of previously described cross-reactive mAbs with canine cells and resulted in the characterization of mAbs recognizing so far undetectable canine CD molecules.
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PMID:Reactivity of cross-reacting monoclonal antibodies with canine leukocytes, platelets and erythrocytes. 1764 96

Three hundred and seventy six monoclonal antibodies (mAbs) raised against human leukocyte surface antigens were analyzed by flow cytometry for cross reactivities against mink leukocytes. We found 53 mAbs (14%) to cross react. This study defined cross reactions to the following human markers: CD1a, CD9 (4 mAbs), CD10, CD11a (2 mAbs), CD14 (3 mAbs), CD18 (5 mAbs), CD20 (atypical reaction), CD21, CD25 (atypical reaction), CD29 (3 mAbs), CD32, CD41, CD42a, CD44 (4 mAbs), CD45, CD45RO, CD47 (2 mAbs), CD49d (3 mAbs), CD61 (2 mAbs), CD62P, CD66abcd, CD71, CD75s, CD79b (2 mAbs), CD86, CD88, CD104 (atypical reaction), CD172a, CD236R (glycophorin C, (atypical reaction)), Xg(a) carbohydrate antigen, Rhesus antigen and two unspecified PAN-reactive mAbs. In order to characterize the molecular mass of the corresponding cross reacting mink markers, the mAbs were used to immunoprecipitate the surface antigens. Fourteen mAbs out of the 53 mAbs reactive with mink leukocytes gave reproducible IP findings. The masses of the precipitated antigens were generally in good agreement with those of the homologous human markers. We also performed immunohistochemical staining analyses on formalin fixed, paraffin embedded mink tissue from lymph node and spleen, and found 7 out of 22 mAbs to give a positive signal. Generally, the immunohistological analyses resulted in expected staining patterns.
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PMID:Reactivity of monoclonal antibodies to human CD antigens with cells from mink. 1768 85

A subset of Pts develops dysfunctional MO to inflammatory DC differentiation and immunosuppression. MDDC, a newly described DC subset, is pivotal in initiating antibacterial responses. Endogenous proteins are known to alter MO to MDDC differentiation. In particular, trauma-elevated TSP-1, a protein that is known to affect MO functions, could trigger MDDC differentiation defects. We hypothesized that TSP-1-deranged differentiation of inflammatory CD1a(+)MDDC would negatively alter activation of immune functions, thereby increasing the risk of postinjury infections. Post-trauma increased TSP-1 levels in patients' plasma and MO correlated with two distinct MDDC differentiation dysfunctions: the previously described decreased CD1a(+)DC yields but also, development of an immunoincompetent CD1a(+)MDDC. The Pts' development of Dysf DC correlated to increased infectious complications. TSP-1 triggered its inhibitory receptor, CD47, activating an inhibitory phosphatase, SHP-1. Increased pSHP-1, decreased antigen processing, and depressed T cell stimulation characterized Pt Dysf DC. TSP-1 mimics added during Cnt MDDC differentiation depressed CD1a(+)DC yields but more importantly, also induced defective CD1a(+)MDDC, reproducing Pts' MDDC differentiation dysfunctions. CD47 triggering during Cnt MDDC differentiation increased SHP-1 activation, inhibiting IL-4-induced STAT-6 activation (critical for CD1a(+)MDDC differentiation). SHP-1 inhibition during MDDC differentiation in the presence of TSP-1 mimics restored pSTAT-6 levels and CD1a(+)MDDC immunogenicity. Thus, postinjury-elevated TSP-1 can decrease CD1a(+)DC yields but more critically, also induces SHP-1 hyperactivity, deviating MDDC differentiation to defective CD1a(+) inflammatory MDDCs by inhibiting STAT-6.
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PMID:Elevated postinjury thrombospondin 1-CD47 triggering aids differentiation of patients' defective inflammatory CD1a+dendritic cells. 2500 59