Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019621 (Langerhans cell histiocytosis)
 3,250 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Histiocytic cells infiltrating the lesions in eosinophilic granuloma of bone as well as in cutaneous histiocytosis X were studied using a murine monoclonal antibody (MA) produced with proliferating cells from an eosinophilic granuloma of bone. This MA reacts with Langerhans cells (LC) of normal human skin or mucous membranes and with proliferating cells of eosinophilic granuloma of bone and skin lesions of Letter-Siwe disease, as shown by immunohistochemistry and immunogold labelling. As other murine MA's obtained after immunization with human cortical thymocytes, this MA immunoprecipitates the 49-kDa CD1a antigen found on human LC and thymic-cell surfaces but not its breakdown product after treatment with trypsin, as demonstrated by analysis of immunoelectron labelling, cytofluorometry and gel electrophoresis. This first production of a CD1a MA from an eosinophilic granuloma supports the concept of Langerhans-cell histiocytosis.
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PMID:Eosinophilic granuloma of bone and biochemical demonstration of 49-kDa CD1a molecule expression by Langerhans-cell histiocytosis. 172 15

In order to study the localization of Lentil lectin (LCH)-binding glycoresidues in glomeruli from patients with a variety of glomerulopathies, and to elucidate the relationship between LCH-binding sugars and the components of the extracellular matrix, laminin and type IV collagen, investigations of formalin-fixed, paraffin-embedded kidney tissues digested with trypsin were carried out by the direct and indirect immunofluorescence microscopy techniques. The glomerular basement membrane (GBM) and the mesangium reacted well with LCH, whereas areas with sclerotic lesions exhibited a decreased reactivity. The pattern of LCH binding to the GBM in various glomerulopathies was similar to that of laminin but different from that of type IV collagen. The pattern of localization of LCH-reacting sites and of laminin in the GBM included the double linear lines in diabetic nephropathy, inner linear line with outer projections (spikes) in membranous nephropathy, and reduplicated basement membrane in membranoproliferative glomerulonephritis. The results obtained by enzyme-linked immunoadsorbent assay showed that LCH had a stronger reactivity for laminin than for type IV collagen or fibronectin. These findings suggest that LCH is more reactive with laminin than with other components of the glomerular extracellular matrix.
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PMID:Histochemical and immunohistochemical studies of diseased human glomeruli. 203 28

Human epidermal Langerhans cells express two (CD1a and CD1c) of the three human thymic cell surface differentiation antigens (CD1a, CD1b, and CD1c). The first cluster of differentiation antigens (CD1) is defined by a group of monoclonal antibodies (MCA). All these MCA were obtained after immunization of mice or rats with human cortical thymocytes. OKT6 MCA (a CD1a MCA) was the first to be described as reactive with human epidermal Langerhans cells. We produced a murine MCA, called DMC1, after immunization with proliferating Langerhans cells of Eosinophilic Granuloma of the bone (Histiocytosis X). In tissues DMC1 MCA reacted with epidermal dendritic cells (Langerhans cells) in the skin and cortical thymocytes in the thymus as observed on indirect immunofluorescence. At the ultrastructural level, DMC1 MCA was specific for Birbeck granule-containing Langerhans cells and did not react with melanocyte and keratinocyte populations. The quantitative analysis of immunoelectron labeling and the cytofluorometric study showed that the intensity of labeling was inversely correlated with the concentration of trypsin used in the preparation of epidermal cell from skin samples. DMC1 MCA precipitated a protein with a relative mass of 49,000 (CD1a molecule) from lysates of iodinated epidermal Langerhans cells under reducing conditions. It recognized the original CD1a molecule (Mr 49,000) but not the membrane breakdown product of CD1a (Mr 27,000) brought about by trypsin.
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PMID:DMC1: a monoclonal antibody produced from histiocytosis X cells which reacts with the native CD1a molecule of human epidermal Langerhans cells. 246 37

Monoamine storage in secretory granules is mediated by the vesicular monoamine transporters 1 and 2 (VMAT1 and VMAT2). The aim of our study was to identify monoamine-handling normal and neoplastic inflammatory cells in the skin by their expression of VMAT1 and VMAT2. Normal skin from various parts of the body, as well as 21 cases of cutaneous mastocytosis and 10 cases of cutaneous Langerhans cell histiocytosis were analyzed by immunohistochemistry, radioactive in situ hybridization, and double-fluorescence confocal microscopy. VMAT2-positive cells in the subepidermal layer were identified as mast cells by their expression of tryptase. Neoplastic mast cells in all cases of cutaneous mastocytosis retained their VMAT2 positivity. The intraepidermal VMAT2-expressing cells were identified as Langerhans cells by their CD1a positivity. VMAT2 was absent from Langerhans cell histiocytosis. VMAT2 is an excellent marker for normal and neoplastic mast cells. The expression of VMAT2 demonstrates the capacity of mast cells for monoamine storage and handling. The presence of VMAT2 in epidermal Langerhans cells revealed a previously unrecognized monoamine-handling phenotype of these cells and indicates possible involvement of amine storage and release associated with antigen presentation. Absence of VMAT2 in neoplastic Langerhans cells indicates a loss of monoamine handling capacity of these cells during tumorigenesis.
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PMID:The vesicular monoamine transporter 2 (VMAT2) is expressed by normal and tumor cutaneous mast cells and Langerhans cells of the skin but is absent from Langerhans cell histiocytosis. 1515 Feb 86