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)

It is the purpose of this study to investigate the healing process in chronic sinusitis by means of a fiberoptic telescope. The patients were divided into 3 groups, in which various combinations of operative techniques were used. Group 1:53 patients with moderate chronic sinusitis. In this group endonasal ethmoidectomy and endonasal exposure of the sphenoidal sinus were performed. Group 2:73 patients with moderate or severe sinusitis. In this group a Caldwell-Luc operation was added to the operations which were used in group I. Group 3:8 patients, in which only endonasal ethmoidectomy was performed. In most cases, the maxillary sinus was cured, but in some of the cases the drainage opening was closed at an early stage. The epithelization of the ethmoidal sinus is mostly completed in about one month after the surgical operation. Adhesions between middle turbinate and lateral wall were seen regularly. Hypertrophic scars were observed in the posterior ethmoid, the ethmoidal roof and the lamina papyracea. We classified the healing process into 4 types. All postoperative infections were treated by antibiotics. Adhesions and scar tissue formations were treated endoscopically.
Rhinology 1981 Sep
PMID:Endonasal findings using a fiberoptic telescope in postoperative cases of chronic sinusitis. 730 74

Severed and subsequently sutured rabbit flexor tendons were kept free and isolated in the synovial cavity of the knee joint. In one series the tendon specimens were surrounded by a dialyzing membrane to avoid cell seeding from the synovial fluid. At different intervals of time over a period of 3 weeks, the tendons were studied morphologically with special reference to scanning electron microscopy. Adhesions were not observed and, with synovial fluid as the nutrient medium, the tendons showed an intrinsic ability to repair in the superficial layers, also bridging the suture gap. Moreover, cell seeding, mainly of macrophages, from the synovial fluid could be demonstrated on the very surface of the tendon. When this cell seeding was prevented, the fibroplasia in the superficial layer of the tendon did decrease slightly, but tendon cell morphology was that of active fibroblasts. The results support the concept that flexor tendons may show intrinsic fibroplasia when nourished by synovial fluid, while macrophages, mainly of extrinsic origin, contribute to restoration of the tendon surface.
J Hand Surg Am 1980 Sep
PMID:Superficial repair of severed flexor tendons in synovial environment. An experimental, ultrastructural study on cellular mechanisms. 743 May 82

The radiological features of Crohn's disease of the small intestine are described in a report on 100 patients examined by a barium infusion method. The examination is performed by introducing a large volume of barium suspension through a tube directly into the small intestine. A multiplicity of radiological signs were seen in the majority of the examinations. Discrete and fissure ulcers were present in many cases; longitudinal ulcers, sinuses and fistulae were seen less frequently. Other signs commonly seen were strictures, in many cases with proximal dilatation, thickening and distortion of the mucosal folds, cobblestoning, asymmetrical involvement, thickening of the wall of diseased intestine and good demarcation of normal from abnormal small intestine. Adhesions, skip lesions, gross distortion, a featureless outline of the diseased intestine and pseudo polyps were less commonly seen. The disease was more extensive in patients who previously had resections for small intestinal Crohn's disease.
Clin Radiol 1980 Sep
PMID:Crohn's disease of the small intestine: a review of the radiological appearances in 100 consecutive patients examined by a barium infusion technique. 747 38

Chronic inflammatory cells are key components in the progression of atherosclerotic plaques and restenosis after coronary angioplasty. Adhesion molecules are fundamental in inflammatory processes. Therefore, the distributions of intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule (VCAM) were investigated in directional coronary atherectomy specimens obtained from 14 patients, in 6 with acute coronary syndromes (myocardial infarction and unstable angina within 1 month), 6 with old myocardial infarction and 2 with stable effort angina. There were eight primary lesions and six restenotic lesions. Atherectomy tissue fragments were snap frozen and cut into 4 microns thick cryostat sections for immunohistochemical staining by avidin-biotin complex immunoperoxidase techniques using adhesion molecule specific monoclonal antibodies BBIG-I1 (ICAM-1) and BBIG-V1 (VCAM). The cells of lesions were characterized in sequential sections by macrophage marker KP1 (CD68), endothelial marker JC/70A (CD31), and smooth muscle cell marker 1A4 (alpha-smooth muscle actin). Four restenotic lesions that had undergone a prior balloon angioplasty within a few months consisted of intimal proliferation and the other lesions were atherosclerotic plaque. Macrophage-rich areas were seen in the lesions from acute coronary syndromes and/or early restenotic lesions. Expression of ICAM-1 or VCAM was strongly associated with macrophage-rich areas, but VCAM staining was weaker than ICAM-1 except in one restenotic lesion. Macrophages that express ICAM-1 and/or VCAM may be important in the unstable plaques and restenotic lesions related to disease activity of ischemic heart disease.
J Cardiol 1995 Sep
PMID:[Immunohistochemical analysis of adhesion molecules in directional coronary atherectomy specimens]. 747 44

Use of porcelain denture teeth may be desirable in many clinical situations, including implant-supported prostheses. However, lack of space because of frameworks often precludes the use of conventional retention by diatorics and pins. Adhesion of porcelain denture teeth to denture resin could also stiffen and possibly strengthen dentures and decrease stain ingress between porcelain teeth and resin denture bases. Unlike previous studies that investigated the bond between conventional feldspathic metal-ceramic porcelain and bis-GMA based composite resin, this study investigated adhesion of denture tooth porcelain to polymethyl methacrylate (PMMA). High-energy air abrasion, hydrofluoric acid etching, and the use of a general purpose bonding agent resulted in an improved bond strength of heat-cured denture PMMA bonded to denture tooth porcelain. Silane coating did not improve bond strengths, and conventional air abrasion was no more effective than polishing with 600-grit silicon carbide. Storage in water and artificial aging substantially decreased bond strengths. The strongest bond strengths were achieved by a high-energy-abrasion + etching + multi-purpose bonding-agent treatment, but a simpler etching + multiple-purpose bonding-agent treatment also produced reliable results. A laboratory technique was suggested. The role of surface treatment in the mechanism of adhesion was examined with scanning electron microscopy. High-energy abrasion produced a slightly more detailed initial topography than conventional air abrasion, but after etching, the high-energy topography became much more detailed. Surface topography alone did not account for all differences found.
J Prosthet Dent 1995 Sep
PMID:Adhesion of denture tooth porcelain to heat-polymerized denture resin. 747 77

We have found that endothelial cells adhere much more strongly than fibroblasts to domains of tenascin and fibronectin. Endothelial cells adhered weakly, without spreading, to bacterial expression proteins corresponding to the tenth fibronectin type III (FN-III) domain of fibronectin, which contains the RGD. A larger fibronectin protein, containing this domain and the three amino-terminal 'synergy' domains gave strong adhesion and spreading. Two widely separated domains of tenascin gave adhesion. The third FN-III domain, TNfn3, which contains an RGD sequence in human and chicken tenascin, gave very strong adhesion and spreading of endothelial cells when tested as an isolated domain. Larger segments containing TNfn3 and the adjacent TNfn2 gave weaker adhesion, probably because the RGD sequence is partially blocked. Adhesion to this domain required divalent cations, was exquisitely sensitive to soluble GRGDSP peptide, and was blocked by antisera to the integrin alpha v beta 3. The second tenascin adhesion domain was the fibrinogen-like C-terminal knob, TNfbg. Cells adhered to but did not spread on this domain. This adhesion required divalent cations and was also sensitive to GRGDSP peptide, so it may be mediated by an integrin receptor. We have explored a range of conditions for preparing the adhesion substratum, and our results may resolve the controversy over whether tenascin can act as a substratum adhesion molecule. When coated for short times (1-2 hours) on plastic, tenascin had no adhesion activity, in contrast to fibronectin and the expression proteins, which gave strong adhesion under these conditions. When coated for longer times (12-24 hours) on plastic, the tenascin substratum supported good adhesion, but not spreading, of endothelial cells. Tenascin coated on nitrocellulose gave substantially stronger adhesion than on plastic, but still required long coating times for maximal activity. Adhesion of endothelial cells to native TN was inhibited by GRDGSP peptide. The cell adhesion activity demonstrates the presence on endothelial cells of tenascin receptors, which may play a supportive role in angiogenesis, in the structure of blood vessels, or in binding tenascin to the cell surface to elicit or enhance a signalling function.
J Cell Sci 1993 Sep
PMID:Endothelial cells adhere to the RGD domain and the fibrinogen-like terminal knob of tenascin. 750 85

The regulation of CD11b/CD18 adhesive and phagocytic functions on human polymorphonuclear leukocytes (PMN) in response to LPS was examined. Adhesion of PMN to surfaces coated with LPS had little or no effect on the cells, but pretreating the LPS-coated surfaces with either diluted serum or LPS-binding protein strongly enhanced their ability to bind C3bi-coated E (EC3bi), a ligand for CD11b/CD18. LPS-binding protein is known to enable responses of cells to LPS by facilitating binding of LPS to CD14. Consistent with this, we found that preformed complexes of LPS with soluble rCD14 stimulated binding of ligand by CD11b/CD18 in a concentration-dependent manner. Known agonists that stimulate CD11b/CD18 binding activity on PMN all cause simultaneous enhancement of Fc-mediated phagocytosis. However, LPS presented in complex with either serum proteins or CD14 failed to stimulate the ingestion of ElgG by PMN. The number of FcRs and their ability to bind ligand were not affected by treatment with LPS, nor were they compromised in their ability to respond to other agonists. These results suggest that LPS generates intracellular signals that alter the ability of CD11b/CD18 to bind ligand, but this alteration is not sufficient to promote phagocytosis of IgG-coated particle. This conclusion was confirmed by showing that PMN treated with LPS and serum produced a lipid with the properties of integrin-modulating factor 1: acetone extracts of these cells stimulated CD11b/CD18 adhesive capacity on PMN. However, the lipid did not enhance Fc-mediated phagocytosis. These studies suggest that CD14 affects CD11b/CD18 function by inducing the synthesis of a lipid such as IMF-1, and that this lipid affects only the binding activity, not the phagocytosis-promoting capacity of CD11b/CD18.
J Immunol 1994 Sep 01
PMID:Different signaling pathways for CD18-mediated adhesion and Fc-mediated phagocytosis. Response of neutrophils to LPS. 751 40

We describe a novel approach to study tyrosine-phosphorylated (PY) integrins in cells transformed by virally encoded tyrosine kinases. We have synthesized a peptide (PY beta 1 peptide) that represents a portion of the cytoplasmic domain of the beta 1 integrin subunit and is phosphorylated on the tyrosine residue known to be the target of oncogenic tyrosine kinases. Antibodies prepared against the PY beta 1 peptide, after removal of cross-reacting antibodies by absorption and affinity purification, recognized the PY beta 1 peptide and the tyrosine-phosphorylated form of the intact beta 1 subunit, but did not bind the nonphosphorylated beta 1 peptide, the nonphosphorylated beta 1 subunit or other unrelated tyrosine-phosphorylated proteins. The anti-PY beta 1 antibodies labeled the podosomes of Rous sarcoma virus-transformed fibroblasts, but did not detectably stain nontransformed fibroblasts. The localization of the tyrosine phosphorylated beta 1 subunits appeared distinct from that of the beta 1 subunit. Adhesion plaques were stained by the anti-beta 1 subunit antibodies in Rous sarcoma virus-transformed fibroblasts plated on fibronectin, whereas neither podosomes nor adhesion plaques were labeled on vitronectin or on uncoated plates. Anti-phosphotyrosine antibodies labeled podosomes, adhesion plaques and cell-cell boundaries regardless of the substratum. One of the SH2 domains of the p85 subunit of phosphatidylinositol-3-kinase bound to the PY beta 1 peptide, but not to the non-phosphorylated beta 1 cytoplasmic peptide. Other SH2 domains did not bind to the PY beta 1 peptide. These results show that the phosphorylated form of the beta 1 integrin subunit is detected in a different subcellular localization than the nonphosphorylated form and suggest that the phosphorylation on tyrosine of the beta 1 subunit cytoplasmic domain may affect cellular signaling pathways.
J Cell Biol 1994 Sep
PMID:Altered localization and cytoplasmic domain-binding properties of tyrosine-phosphorylated beta 1 integrin. 752 Apr 49

Asthma is a disease of airway inflammation and hyperreactivity that is associated with a lymphocytic infiltrate in the bronchial submucosa. The interactions between infiltrating T lymphocytes with cellular and extracellular matrix components of the airway and the consequences of these interactions have not been defined. We demonstrate the constitutive expression of CD44 on human airway smooth muscle (ASM) cells in culture as well as in human bronchial tissue transplanted into severe combined immunodeficient mice. In contrast, basal levels of intercellular adhesion molecule 1 (ICAM-1) and vascular cell adhesion molecule 1 (VCAM-1) expression are minimal but are induced on ASM by inflammatory mediators such as tumor necrosis factor alpha (TNF-alpha). Activated, but not resting T cells, adhere to cultured ASM; stimulation of the ASM with TNF-alpha enhanced this adhesion. Adhesion was partially blocked by monoclonal antibodies (mAb) specific for lymphocyte function-associated antigen 1 (LFA-1) and very late antigen 4 (VLA-4) on T cells and ICAM-1 and VCAM-1 on ASM cells. The observed integrin-independent adhesion was mediated by CD44/hyaluronate interactions as it was inhibited by anti-CD44 mAb 5F12 and by hyaluronidase. Furthermore, the adhesion of activated T lymphocytes induced DNA synthesis in growth-arrested ASM cells. Thus, the interaction between T cells and ASM may provide insight into the mechanisms that induce bronchial inflammation and possibly ASM cell hyperplasia seen in asthma.
J Exp Med 1994 Sep 01
PMID:T lymphocytes adhere to airway smooth muscle cells via integrins and CD44 and induce smooth muscle cell DNA synthesis. 752 Apr 73

Close interaction of human hematopoietic progenitors with the bone marrow microenvironment is important for the ordered progression of human hematopoiesis. Progenitor cell adhesion to stroma has a complex molecular basis, involving various cell-extracellular matrix and cell-cell interactions. We have previously shown that adhesion of colony-forming cells (CFC) to fibronectin, present in stromal extracellular matrix, involves multiple sites, including two heparin-binding synthetic peptides (FN-C/H I and FN-C/H II) and the alpha 4 beta 1 integrin-binding peptide CS1. These synthetic peptides are located in close proximity in the type III repeat 14 and the immediately adjacent type IIIcs region of fibronectin. In the current study, we evaluate receptors expressed by CFC responsible for their adhesion to fibronectin. We show that the alpha 4 beta 1 integrin mediates adhesion to CFC to the peptides FN-C/H I and CS1. Adhesion of CFC to fibronectin is also mediated by proteoglycans, because removal of cell surface chondroitin-sulfate proteoglycans resulted in decreased adhesion of CFC to FN-C/ I and FN-C/H II. The core protein of this proteoglycan was identified by immunoprecipitation as a 90-kD member of the CD44 group of adhesion molecules. Interestingly, although the proteoglycan core protein failed to adhere to FN-C/H II affinity columns, anti-CD44 monoclonal antibodies blocked CFC adhesion to FN-C/H II, indicating that these monoclonal antibodies may interfere with core protein-mediated intracellular signalling. Finally, we show that CD44 and alpha 4 beta 1 may cooperate in establishing progenitor adhesion, because anti-CD44 antibodies potentiated the adhesion-inhibitory effects of suboptimal concentrations of anti-alpha 4 or anti-beta 1 monoclonal antibodies. These results provide a working model for progenitor cell recognition of fibronectin (and possibly the marrow micro-environment) in which the coordinated action of integrins and cell surface proteoglycans is necessary for cell adhesion. This model can now be used to study the complex relationship between progenitor cell adhesion and the regulation of their proliferation and differentiation.
Blood 1994 Sep 15
PMID:Adhesion of committed human hematopoietic progenitors to synthetic peptides from the C-terminal heparin-binding domain of fibronectin: cooperation between the integrin alpha 4 beta 1 and the CD44 adhesion receptor. 752 91


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