13 резултати
Neutral endopeptidase 24.11 (NEP/CALLA/CD10), an enzyme expressed on early lymphoid progenitors, neutrophils, and various other cell types, inactivates many biologically active peptides, including the bacterial chemotactic peptide N-formylmethionyl-leucyl-phenylalanine (fMLP). Inhibition of CD10/NEP
The common acute lymphoblastic leukemia antigen (CALLA, CD10), which is expressed on early lymphoid progenitors and neutrophils, is the zinc metalloprotease, neutral endopeptidase 24.11 (NEP, "enkephalinase"). The CD10 cell surface enzyme is known to hydrolyze a variety of biologically active
We have previously demonstrated that human neutrophils synthesize the common acute lymphoblastic leukemia antigen (CALLA/CD10). To determine whether CALLA/CD10-positive and -negative neutrophils have similar or distinct functional attributes, we sorted normal peripheral blood neutrophils for
We investigated the ability of isolated human colonic epithelial cells to express the common acute lymphoblastic leukemia antigen (CALLA), the transferrin receptor, and the 4F2 antigen in response to different types of stimuli. The expression of these markers was assessed by immunofluorescence using
Cell surface antigens, such as CR3, Fc gamma RIII, cALLa and Leu 8 antigen, expressed on polymorphonuclear cells (PMN) in the peripheral blood (PB) are associated with certain functions of PMN. Functional alterations of PMN have been reported in some rheumatic diseases. In this study, therefore, the
Antibodies directed against the common acute lymphoid leukemia antigen (CALLA) were obtained from 2 hybridomas: J5 (Schlossman, mice sensitized with patient ALL cells), and Vil-A1 (Knapp, sensitization with the Reh cell line). The percentage of lymphoid cells reacting with these 2 monoclonal
For differentiating between inflammatory and neoplastic intrathecal lymphopleocytosis, analysis of CSF cell surface markers was employed in two patients. In one case, diagnosis of intrathecal spreading of a previously not diagnosed lymphoma was established by identifying a uniform population of
Neprilysin (NEP, CD10, CALLA-common acute lymphoblastic leukaemia antigen, neutral endopeptidase, enkephalinase) is a zinc-dependent metallopeptidase, which is involved in the metabolism of a number of regulatory peptides and plays an important role in turning off peptide signalling at the cell
Neutral endopeptidase (EC 3.4.24.11, NEP) is an integral membrane protein of human neutrophils. NEP is identical with the common acute lymphoblastic leukemia antigen (CALLA) of leukemic cells. The expression of NEP on the surface of neutrophils is down-regulated by endocytosis which can be induced
Neprilysin (neutral endopeptidase, enkephalinase, CALLA, CD10, NEP) is a regulatory Zn metallopeptidase expressed in the brush border membranes of the kidney and has been found in porcine chondrocytes and rat articular cartilage as well as other cell types and tissues. Although its function in
Biology of glomerular visceral epithelial cells ("podocytes") and their role in inflammatory process remain obscure, partly because of the lack of well-differentiated podocyte cultures. We have established a human cell line by transfecting with a replication-defective SV40 plasmid (pSVHB1), a
CD10, also known as neutral endopeptidase or CALLA, is a major metalloproteinase that regulates levels of biologically active peptides that initiate inflammatory, cardiovascular, and neurogenic responses. Relative tissue expression levels of CD10, its peptide substrates, and their receptors
The expression of the endogenous neuropeptide-degrading enzyme, neutral endopeptidase (NEP; CALLA, CD10, E.C.3.4.24.11) on cultured human airway epithelial cells can be upregulated by corticosteroids. We examined whether NEP expression in the airway epithelium or lamina propria in bronchial biopsies