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)

Cells of several strains of Streptococcus gordonii attached in much higher numbers to experimental pellicles formed from samples of submandibular or parotid saliva on hydroxyapatite (HA) beads than to buffer controls. The nature of the salivary components responsible were investigated by preparing experimental pellicles from chromatographic fractions of submandibular saliva obtained from Trisacryl GF 2000M columns. Adhesion of S. gordonii Blackburn was promoted by two groups of fractions. The adhesion-promoting activity in the first group of fractions was associated with the family of acidic proline-rich proteins (PRPs), while that of the second group is as yet unidentified. Experimental pellicles prepared by treating HA with 2 micrograms of pure 150-amino-acid-residue PRPs (PRP-1, PRP-2, and PIF-s) promoted adhesion of S. gordonii Blackburn cells to an extent comparable to that obtained with unfractionated saliva. However, pellicles prepared from a 106-residue PRP (PRP-3) were significantly less effective, and those prepared from the amino-terminal tryptic peptide (residues 1 to 30) of the PRP and the salivary phosphoprotein statherin were completely ineffective in promoting adhesion. Although adhesion of several strains of S. gordonii was promoted by adsorbed PRP-1, the adhesion of several strains of Streptococcus sanguis or Streptococcus oralis was either not affected or only weakly enhanced by this protein. S. gordonii cells bound avidly to PRPs adsorbed onto HA beads, but the streptococci did not appear to bind PRPs in solution, since concentrations of PRP as high as 200 micrograms/ml did not inhibit binding of bacterial cells to pellicles prepared from pure PRP. S. gordonii cells also attached well to PRP or a synthetic decapeptide representing residues 142 to 150 of the PRP when the peptide was linked to agarose beads. Studies with a series of synthetic decapeptides indicated that the minimal segment of PRP which promoted high levels of S. gordonii adhesion was the carboxy-terminal dipeptide Pro-Gln (residues 149 and 150).
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PMID:Delineation of a segment of adsorbed salivary acidic proline-rich proteins which promotes adhesion of Streptococcus gordonii to apatitic surfaces. 187 20

The goal of this study was to characterize salivary components of titanium pellicles and to determine how experimental pellicles affect adhesion of several strains of streptococci to titanium surfaces. Titanium experimental pellicles were formed by incubation of fresh human parotid or human submandibular-sublingual saliva on pure titanium beads. Pellicle was recovered from the beads using sodium dodecyl sulfate buffer and was subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting to identify adsorbed salivary components. Streptococcus anginosus, S. oralis, and S. salivarius recovered from in vivo titanium plaque and five reference strains of streptococci were used in adhesion assays to titanium beads with and without experimental salivary pellicles. The experimental pellicle formed on titanium was found to be composed of selected proteins from human parotid and human submandibular-sublingual saliva. Salivary alpha-amylase and proline-rich proteins were found in all experimental pellicles, while sIgA, high-molecular weight mucin, and proline-rich glycoproteins were detected in one of the experimental pellicles examined. Adhesion of fresh isolates and reference stains of S. anginosus, S. oralis, and S. salivarius to saliva-coated titanium was reduced compared to that of titanium without saliva coating. However, adhesion of laboratory strains of S. gordonii and S. sanguis was found to be significantly greater to experimental pellicles of human submandibular-sublingual saliva than was the adhesion of the fresh isolates, suggesting that streptococci-colonizing implant surfaces may be inherently less adhesive than other bacterial strains. This study found that salivary pellicles are selectively formed on titanium and mediate in vitro adhesion of streptococci.
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PMID:Experimental salivary pellicles formed on titanium surfaces mediate adhesion of streptococci. 880 39

Adhesion of Candida albicans to saliva-coated surfaces is an important early step in the colonization of the oral cavity. C. albicans cells also adhere to several species of oral streptococci including Streptococcus gordonii, Streptococcus oralis and Streptococcus sanguinis in what are believed to be multi-modal interactions. It is now demonstrated that incubation of streptococcal cells of these species with human parotid saliva further promotes the adhesion of C. albicans cells by up to 2-3-fold. Various species of streptococci were shown to adsorb different protein components of parotid saliva to their cell surfaces. The basic proline-rich proteins (bPRPs), to which C. albicans cells bind on nitrocellulose blot overlay, were strongly adsorbed to the surface of S. gordonii cells but not to S. oralis cells. Parotid saliva that was pre-adsorbed with S. gordonii cells and then applied to hydroxylapatite beads was <50% effective at supporting adhesion of C. albicans compared with control (non-adsorbed) saliva, demonstrating that bPRPs are major pellicle receptors. C. albicans cells did not adsorb bPRPs from fluid-phase parotid saliva. Following size-exclusion chromatography of parotid saliva samples, pooled fractions enriched in bPRPs promoted maximal adhesion of C. albicans to S. gordonii cells. The results demonstrate that C. albicans cells recognize only surface-bound forms of bPRPs and suggest that these proteins adsorbed to enamel or to streptococcal surfaces promote C. albicans adhesion and oral colonization.
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PMID:Adhesion of Candida albicans to oral streptococci is promoted by selective adsorption of salivary proteins to the streptococcal cell surface. 1065 50

The aim of the present study was to identify salivary molecules affecting adhesion of Candida albicans and Candida krusei to salivary pellicles and epithelial cells. Strains of C. albicans (GDH18, GDH3339, CA1957, ATCC 28366 and ATCC 10321), but not C. krusei (strains ATCC 14243 and Ck9), bound to saliva-coated hydroxyapatite and buccal epithelial cells. Parotid saliva fractions containing statherin, glycosylated proline-rich proteins (PRP) and as yet unidentified components mediated adhesion of strain GDH18; Fuc alpha 1-2Gal beta 1-4Glc partly inhibited the adhesion to those fractions not containing statherin. Pure statherin, but not PRP-1, mediated dose-dependent adhesion of C. albicans strain GDH18 to hydroxyapatite beads. Candida isolates (GDH18, GDH3339 and CA1957) bound somewhat more avidly to statherin/saliva relative to ATCC strains 28366 and 10321, while the opposite was true for adhesion to buccal epithelial cells. Adhesion of C. albicans strain GDH18 to saliva-coated hydroxyapatite and buccal epithelial cells was completely (93%) and partly (43%) blocked by statherin-specific immunoglobulin G (IgG) antibodies, respectively. Control IgG antibodies did not block Candida adhesion. Blockage of Candida adhesion to epithelial cells also occurred with Fuc alpha 1-2Gal beta 1-4Glc (49%) and N-acetylglucosamine (38%), while statherin specific IgG antibodies in combination with Fuc alpha 1-2Gal beta 1-4Glc almost completely eliminated Candida adhesion (79%). In addition, statherin in solution blocked the adhesion of strain GDH18 to epithelial cells by inducing aggregation of Candida cells.
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PMID:Adhesion of Candida albicans, but not Candida krusei, to salivary statherin and mimicking host molecules. 1115 74

CAIR-1/BAG-3 is a stress and survival protein that has been shown to bind SH3 domain-containing proteins through its proline-rich (PXXP) domain. Because stress and survival pathways are active during invasion and metastasis, we hypothesized that CAIR-1 is a regulator of signaling pathways that modulate cell adhesion and migration. MDA-435 human breast carcinoma cells were stably transfected with full-length CAIR-1 (FL) or a proline-rich domain deleted mutant (dPXXP). FL cells migrated poorly through collagen IV-coated filters to serum (14% of control, p=0.0004), whereas migration of dPXXP cells was more robust (228%, p=0.00001). Adhesion to collagen IV-coated surfaces was reduced in FL cells and augmented in dPXXP cells (FL 64%, p=0.03; dPXXP 138%, p=0.01). Rhodamine-phalloidin staining highlighted more stress fibers and thicker filopodial protrusions in dPXXP cells. Fewer focal adhesions were also seen in FL cells. A reduction in tyrosine phosphorylation of focal adhesion kinase (FAK) and paxillin occurred in FL cells under these conditions. In contrast, increased FAK and paxillin phosphorylation was documented in dPXXP cells. Differential FAK phosphorylation occurred at the major autophosphorylation site Y(397) and Src phosphorylation site Y(861). Concordant with these findings, there was decreased interaction between FAK and its downstream partners p(130)Cas and Crk observed in FL cells but not in dPXXP cells. These results collectively indicate that CAIR-1 may negatively regulate adhesion, focal adhesion assembly, signaling, and migration via its PXXP domain.
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PMID:CAIR-1/BAG-3 modulates cell adhesion and migration by downregulating activity of focal adhesion proteins. 1685 81

Adhesion of microorganisms to dental surfaces is the initial step in the formation of dental bacterial plaque. Streptococcus mutans (S. mutans) is considered the main causal agent of one of the most common diseases in humans: dental caries. Adherence of these bacteria results from the interaction of adhesins that form part of their structure with salivary components, specifically those that compose the acquired pellicle. The complexity of this interaction has been the subject of studies in past years, to the extent of identifying certain salivary components related to adhesion to enamel surfaces, such as proline-rich proteins (PRSs), Staherins, Histatins, Cystatins, etc. One of the objectives of this study was to determine the adhesion capacity of S. mutans to synthetic hydroxyapatite incubated with saliva samples of caries-active and caries-inactive individuals. For the purpose of these assays, both the whole saliva samples and the salivary protein extracts were used. They were obtained by separating the proteins contained in the simple SDS-PAGE, in three ranges of molecular weight, selected in accordance with the electrophoresis profile that was usually found. The results indicated that the adhesion of this microorganism was greater in caries-inactive patients, when tested with whole saliva and proteins in the 120-159 kDa molecular weight range. This suggests that adhesion, per se, does not have a definite effect on the mechanisms that cause the disease in some individuals. However, these are interesting findings that may contribute to the design of strategies to control the adhesion of S. mutans to the tooth's surface.
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PMID:Adhesion of Streptococcus mutans to salivary proteins in caries-free and caries-susceptible individuals. 1764 12

The Src family kinase/Focal Adhesion Kinase (FAK) complex is a signaling platform playing a crucial role in transformation downstream of oncogenic growth factor receptors. In the case of melanoma in Xiphophorus fish, the oncogenic EGF receptor orthologue Xiphophorus melanoma receptor kinase (Xmrk) effects continuous activation of the Src family kinase Fyn, but not of the other family members Src or Yes. Here, Fyn is strongly involved in promoting many tumorigenic events. Although Fyn is expressed in most mammalian tissues, there are only few reports of its involvement in the development of solid tumors. To find out whether the prominent role of Xiphophorus Fyn is based on an altered binding to its important binding partner FAK when compared to its mammalian Fyn counterparts, we performed yeast-two-hybrid analyses. We compared Xiphophorus and murine Fyn with respect to their binding to full-length and truncated FAK constructs. We found that interaction with FAK occurs similarly for Xiphophorus and mouse Fyn. Both phosphorylated FAK residue Y397 and FAK proline-rich domain are involved in Fyn binding. We also found interaction of FAK and Fyn in human melanoma cell lines. These data suggest a possible, yet unrecognized role of Fyn in the tumorigenesis of human melanoma, too.
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PMID:Interaction of Xiphophorus and murine Fyn with focal adhesion kinase. 1893 Aug 41

Adhesive pili on the surface of the serotype M1 Streptococcus pyogenes strain SF370 are composed of a major backbone subunit (Spy0128) and two minor subunits (Spy0125 and Spy0130), joined covalently by a pilin polymerase (Spy0129). Previous studies using recombinant proteins showed that both minor subunits bind to human pharyngeal (Detroit) cells (A. G. Manetti et al., Mol. Microbiol. 64:968-983, 2007), suggesting both may act as pilus-presented adhesins. While confirming these binding properties, studies described here indicate that Spy0125 is the pilus-presented adhesin and that Spy0130 has a distinct role as a wall linker. Pili were localized predominantly to cell wall fractions of the wild-type S. pyogenes parent strain and a spy0125 deletion mutant. In contrast, they were found almost exclusively in culture supernatants in both spy0130 and srtA deletion mutants, indicating that the housekeeping sortase (SrtA) attaches pili to the cell wall by using Spy0130 as a linker protein. Adhesion assays with antisera specific for individual subunits showed that only anti-rSpy0125 serum inhibited adhesion of wild-type S. pyogenes to human keratinocytes and tonsil epithelium to a significant extent. Spy0125 was localized to the tip of pili, based on a combination of mutant analysis and liquid chromatography-tandem mass spectrometry analysis of purified pili. Assays comparing parent and mutant strains confirmed its role as the adhesin. Unexpectedly, apparent spontaneous cleavage of a labile, proline-rich (8 of 14 residues) sequence separating the N-terminal approximately 1/3 and C-terminal approximately 2/3 of Spy0125 leads to loss of the N-terminal region, but analysis of internal spy0125 deletion mutants confirmed that this has no significant effect on adhesion.
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PMID:Roles of minor pilin subunits Spy0125 and Spy0130 in the serotype M1 Streptococcus pyogenes strain SF370. 2063 32

Adhesion to extracellular matrix (ECM) is crucially important for survival of normal epithelial cells as detachment from ECM triggers specific apoptosis known as anoikis. As tumor cells lose the requirement for anchorage to ECM, they rely on cell-cell adhesion 'multicellular aggregation' for survival. Multicellular aggregation of tumor cells also significantly determines the sensitivity of tumor cells to the cytotoxic effects of chemotherapeutics. In this report, we demonstrate that expression of immunoglobulin containing and proline-rich receptor-1 (IGPR-1) is upregulated in human primary colon cancer. Our study demonstrates that IGPR-1 promotes tumor multicellular aggregation, and interfering with its adhesive function inhibits multicellular aggregation and, increases cell death. IGPR-1 supports colon carcinoma tumor xenograft growth in mouse, and inhibiting its activity by shRNA or blocking antibody inhibits tumor growth. More importantly, IGPR-1 regulates sensitivity of tumor cells to the chemotherapeutic agent, doxorubicin/adriamycin by a mechanism that involves doxorubicin-induced AKT activation and phosphorylation of IGPR-1 at Ser220. Our findings offer novel insight into IGPR-1's role in colorectal tumor growth, tumor chemosensitivity, and as a possible novel anti-cancer target.
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PMID:Targeting tumor multicellular aggregation through IGPR-1 inhibits colon cancer growth and improves chemotherapy. 2892 Sep 28