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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A surface-adherent cell population developed spontaneously from Friend erythroleukemia cells (FLC745) which previously had grown continuously in suspension cultures. The adherent cells have been transferred through more than 60 passages and apparently represent a stable variant, herein designated FLC745-Ad. The cell size, chromosome complement, and tumorigenicity in DBA/2 mice were similar to the parental FLC745 line, although the FLC745-Ad cultures grew at a slightly slower rate and synthesized less hemoglobin in response to dimethyl sulfoxide. Production of C-type particles was abundant in both suspension and adherent cells, but the latter appeared to contain more intracisternal A-type particles. Scanning electron microscopy disclosed that most adherent cells were globoid and nonspreading. They attached to the substrate by a circumferential lamellar skirt of unusual breadth. Adhesion of the FLC745-Ad cells was not influenced by serum concentration, trypsinization, 5-bromodeoxyuridine, or N6, O2'-dibutyryl adenosine 3':5'-monophosphate. Treatment with cytochalasin B increased the cell size and the area of cell attachment.
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PMID:Characteristics of a surface-adherent subline derived from Friend erythroleukemia cells in continuous suspension culture. 17 97

Adhesion of myeloid leukemia cells to the bone marrow (BM) microenvironment is mediated in part by Beta 1 and Beta 2 integrins. Cells of the erythroleukemia line K562, derived from a patient with chronic myeloid leukemia, bind to BM fibroblasts (BMFs) but the adhesion cannot be accounted for by integrins or other known adhesion proteins including CD44 or members of the Ig or selectin families. Membrane fragments from K562 cells were radioiodinated and allowed to adhere to BMF monolayers. Adherent proteins were solubilized together with the fibroblasts, analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and visualized by autoradiography. Four adherent proteins were consistently observed. Two of these, with reduced molecular weights of 52 kD and 35 to 37 kD, were prominent. Addition of soluble thrombospondin and heparin but not fibronectin inhibited binding of K562 membrane proteins to adherent BMFs and immobilized thrombospondin- and heparin-bound K562 proteins. The 52-kD protein has a multimeric structure nonreduced and has characteristics of a glycoprotein. Its adhesion to fibroblasts is divalent cation and temperature sensitive. The 35- to 37-kD protein, whose function is divalent cation but not temperature sensitive, is phosphoinositol-linked and has characteristics identical to an adherent 35- to 37-kD protein identified on murine progenitor cells. Membrane preparations from two cases of acute myeloid leukemia showed an adherent 35- to 37-kD protein and in one case an adherent 52-kD protein without other adherent bands. A K562 subclone with reduced adherence to BMFs showed reduced amounts of adherent 52-kD and 35- to 37-kD proteins. These proteins may be responsible for the adhesion of malignant and normal hematopoietic progenitor cells to the BM microenvironment.
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PMID:Identification of novel K562 membrane proteins that adhere to bone marrow fibroblasts. 870 84

The effect of alpha- and beta-tocopherol on human erythroleukemia cell (HEL) adhesion induced by phorbol 12-myristate 13-acetate (PMA) has been studied. Adhesion induced by PMA stimulation was prevented by 44.5% by physiological concentrations of alpha-tocopherol. Under the same experimental conditions, beta-tocopherol, an analogue of alpha-tocopherol, produced 11% inhibition of adhesion. Cell response gradually increased from 0 to 24 h of alpha-tocopherol treatment. Only a slight time dependency of beta-tocopherol inhibition was observed. Another human erythroleukemia cell line (K562) and the human monocyte tumor cell line U937 showed 5.0 and 11.2% inhibition, respectively. Similar to alpha-tocopherol, the protein kinase C inhibitor, Calphostin C, and the MAPK inhibitor, PD98059, prevented PMA-induced cell adhesion. An inhibition of ERK-1 phosphorylation was observed for alpha-tocopherol only in HEL, implying that MAP kinase pathway is involved in this cell line. Fluorescence-activated cell sorting (FACS), by using various integrin-specific monoclonal antibodies, has shown that alpha (1-6), beta1, and alphav integrins are less expressed at the cell surface after alpha-tocopherol treatment. Beta-tocopherol treatment was less effective.
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PMID:Differential inhibition by alpha- and beta-tocopherol of human erythroleukemia cell adhesion: role of integrins. 1139 Jan 83