Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1992-7-10
pubmed:abstractText
The regulation of extracellular matrix (ECM) protein receptor expression was followed in the human promonocytic cell line U937 before and after stimulation either with PMA or various cytokines implicated in monocytopoiesis. On undifferentiated U937 cells, alpha-chains of very late Ag (VLA)-4, VLA-5, and VLA-6 were constitutively expressed whereas alpha-chains of VLA-2 (alpha 2) and vitronectin receptor (alpha V) were not. Maturation of U937 cells with PMA resulted in a marked decrease in alpha 4 expression (25% of control by day 5), and a small but significant increase in the expression of alpha 2 and alpha v over 4 days of stimulation. Unstimulated U937 cells attached to fibronectin (FN) but not to laminin (LM), collagens I/IV-coated surfaces. After PMA stimulation, U937 cells exhibited enhanced adherence on FN and expressed the ability to adhere to LM. PMA stimulation also promoted U937 spreading both on FN and LM. Adhesion on FN all along the maturation pathway was specifically and totally inhibited by anti-alpha 5 mAb but not by anti-alpha 4 mAb. Anti-beta 1, anti-alpha 6, anti-alpha 2, and anti-alpha v mAb, as well as Tyr-Ile-Gly-Ser-Arg and Arg-Gly-Asp synthetic peptides from LM, had no effect on adhesion of PMA-stimulated cells on LM, implying that U937 cell adherence to LM is mediated through hitherto distinct receptors. In the presence of rIFN-gamma, differentiating U937 cells did not adhere to LM and lost the capacity to bind to FN. Loss of adhesion to FN was correlated with the concomitant decrease in the expression of alpha 4 and alpha 5 integrin subunits. In contrast, TGF-beta 1 mimicked most of the effects of PMA by enhancing the attachment of maturating U937 cells on FN through alpha 5 receptors and by promoting adherence to LM. TGF-beta 1 stimulation also promoted U937 cell spreading on both FN- and LM-coated surfaces. The data suggest that inflammatory cytokines such as IFN-gamma and TGF-beta 1 may be critically important in the homing of monocytic cells at sites of inflammation by modulating cell-surface expression of ECM receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
148
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3912-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:1534826-Amino Acid Sequence, pubmed-meshheading:1534826-Cell Adhesion, pubmed-meshheading:1534826-Cell Differentiation, pubmed-meshheading:1534826-Cytokines, pubmed-meshheading:1534826-Fibronectins, pubmed-meshheading:1534826-Humans, pubmed-meshheading:1534826-Integrins, pubmed-meshheading:1534826-Interferon-gamma, pubmed-meshheading:1534826-Laminin, pubmed-meshheading:1534826-Molecular Sequence Data, pubmed-meshheading:1534826-Monocytes, pubmed-meshheading:1534826-Peptides, pubmed-meshheading:1534826-Receptors, Fibronectin, pubmed-meshheading:1534826-Receptors, Immunologic, pubmed-meshheading:1534826-Receptors, Laminin, pubmed-meshheading:1534826-Tetradecanoylphorbol Acetate, pubmed-meshheading:1534826-Transforming Growth Factor beta, pubmed-meshheading:1534826-Tumor Cells, Cultured
pubmed:year
1992
pubmed:articleTitle
IFN-gamma and transforming growth factor-beta 1 differently regulate fibronectin and laminin receptors of human differentiating monocytic cells.
pubmed:affiliation
Unité 196 INSERM, Institut Curie, Paris, France.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't