Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Very Little is known about the immunological attributes of human endothelial cells. In this study, we performed immunologic phenotypic analysis of cultured human dermal microvascular endothelial cells in comparison with human umbilical vein endothelial cells and examined the ability of various biologic response modifiers to alter the phenotypes. Using FACS analysis, both types of the cells appear to lack many of the cell surface markers of immunologically proficient cells, E.G. OKT4, OKT8, Leu7, FcIgG receptor, complement receptors, IL-2 receptor and HLA-Dr, but they possess beta 2-microglobulin and DAF. HLA-Dr antigens can be induced on both types of endothelial cells by gamma-IFN in a dose and time dependent manner. Both types of endothelial cells possess several kinds of Cell Adhesion Molecules (CAMs), such as ICAM-1, CD44, LFA-3, but not LFA-1 or CD2. ICAM-1 but not LFA-3 or CD44 can be upregulated by exposure of both types of endothelial cells to gamma-IFN, IL-1 and TNF. These data suggest that endothelial cells of the dermal microvasculature may play central roles in a variety of different cutaneous inflammation.
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PMID:[Immunophenotypic analysis of human endothelial cells]. 197 95

Biochemical and molecular genetic studies have contributed to our molecular knowledge of blood group-associated molecules in the past few years. Among the 23 blood group systems presently identified, almost all have a molecular basis and present investigations are oriented towards the analysis of genetic polymorphisms, tissue-specific expression and structure-function relationships. Antigens defined by carbohydrate structures, among which ABO, Hh, Lewis and Secretor are the main representative species, are indirect gene products. They are synthesized by Golgi-resident glycosyltransferases, which are the direct products of the blood group genes. Many of these enzymes have been cloned and the molecular basis of the silent phenotypes, for instance 0, Bombay/paraBombay, Le(a-b-) and non-secretor, has been elucidated. However, the glycosyltransferases involved in the biosynthesis of Pk, P and P1 antigens are not yet characterized. A large number of blood group antigens carried by red cell polypeptides expressed at the cell surface are not related to a carbohydrate structure, and these proteins are direct blood group gene products. Most have been cloned and characterized recently, for instance MN antigens (glycophorin A), Ss antigens (glycophorin B), Gerbich antigens (glycophorins C and D) and antigens encoded by the RH, LW, KEL, FY, JK, XG, LU and XK loci. Other antigens have been located on proteins already identified, for instance the Cromer antigens on DAF, Knops antigens on CR1, Indian and AnWj antigens on CD44, Yt antigens on AChE, Diego, Wr, Rga and Warr on Band 3, Colton antigens on AQP-1 (water channel). The SC (Scianna) et DO (Dombrock) systems, however, still resist to molecular cloning. On the basis of this information, a tentative classification of blood group antigens into five functional categories is emerging: - Transporters and channels, - Receptors and ligands, - Adhesion molecules, - Enzymes, - Structural proteins. This review will focus on these recent findings and will illustrate how these studies may bring new information for analysis of normal and abnormal phenotypes and for understanding both the mechanisms of tissue specific expression and the potential function of these antigens, particularly those expressed in non-erythroid lineage. In addition, since our knowledge of the molecular basis of blood group polymorphisms has significantly increased, new genotyping techniques potentially useful in clinical applications will become available.
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PMID:[A molecular approach to the structure, polymorphism and function of blood groups]. 892 12

CD97 is a newly identified, activation-associated human leucocyte antigen with seven putative transmembrane domains. It has an extended extracellular segment containing several adhesion molecule structure motifs, and has been shown to interact with the human complement regulator, decay-accelerating factor (DAF, CD55). To understand further the interaction between CD97 and DAF, as well as the structure and function of CD97 in general, we have cloned the mouse CD97 cDNA and studied the encoded protein for its membrane association property and ability to interact specifically with the murine decay-accelerating factor. The full-length mouse CD97 cDNA that we have cloned and characterized encodes a protein that is 60% identical to the three epidermal growth factor (EGF) domain-containing form of human CD97 but does not contain the Arg-Gly-Asp (RGD) motif which is present in human CD97. Two other alternatively spliced forms of mouse CD97 were also identified. These forms differ by the number of EGF-like sequence repeats present in the N-terminal region. Northern blot analysis revealed that CD97 is expressed widely in mouse tissues and in resting as well as activated cultured mouse splenocytes. Transient transfection of human embryonic kidney (HEK) 293 cells with the mouse CD97 cDNA in a green-fluorescence protein vector (pEGFP-N1) showed plasma membrane targeting of the expressed protein. Western blot analysis confirmed its membrane association and identified the existence of a processed C-terminal fragment, supporting the notion that CD97 on the cell membrane is composed of post-translationally generated subunits. Adhesion studies demonstrated that normal, but not DAF knockout mouse erythrocytes and splenocytes adhered to mouse CD97-transfected HEK cells. The interaction of CD97 and DAF was found to be species-restrictive in that human erythrocytes were unable to bind to mouse CD97-transfected HEK cells. These results indicate that the general structure, membrane association property and DAF-binding ability of CD97 are conserved and that the adhesive interaction between CD97 and DAF is independent of the RGD motif. The finding that CD97 is distributed widely among various mouse tissues suggests that CD97 may have other roles beyond lymphocyte activation.
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PMID:Structural characterization of mouse CD97 and study of its specific interaction with the murine decay-accelerating factor (DAF, CD55). 1054 Feb 31

Adhesion of raphid diatoms to surfaces, mediated by the secretion of extracellular polymeric substances (EPS), is an important strategy for growth and survival. Diatom biofilms are also important in the context of biofouling. Diatoms exhibit selectivity in adhering to surfaces, but little is understood about how they perceive the properties of a substratum and translate that perception into altered adhesion properties. In this study, we demonstrate that Seminavis robusta Danielidis et D. G. Mann, like many other pennate diatoms, adheres more strongly to hydrophobic surfaces (such as silicone elastomer foul-release coatings) than to hydrophilic surfaces. To explore the cellular mechanisms that may underlie this selectivity, we tested the hypothesis that diatoms may perceive a hydrophilic surface as unconducive to adhesion through a form of stress response involving nitric oxide (NO) production. Single-cell imaging with the fluorescent indicator DAF-FM DA (4-amino-5-methylamino-2',7'-difluorofluorescein diacetate), revealed NO levels that were 4-fold higher in cells adhered to a hydrophilic surface (acid-washed glass) compared with a hydrophobic surface (polydimethylsiloxane elastomer, PDMSE). Elevated levels of NO caused by the addition of the NO donor S-nitroso-N-acetylpenicillamine (SNAP) did not affect growth, but cells showed reduced adhesion strength to both glass and PDMSE. Addition of the nitric oxide synthase inhibitor NG-monomethyl-l-arginine (NMMA) caused a small but significant increase in adhesion strength. Overall, the results suggest that NO acts as a signal of the wettability properties of substrata for Seminavis.
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PMID:THE ROLE OF NITRIC OXIDE IN DIATOM ADHESION IN RELATION TO SUBSTRATUM PROPERTIES(1). 2704 15