| 1. |
- Amin, Awin, et al.
(författare)
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Patient-reported participation in hepatopancreatobiliary surgery cancer care : A pilot intervention study with patient-owned fast-track protocols
- 2022
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Ingår i: European Journal of Cancer Care. - : Wiley. - 0961-5423 .- 1365-2354. ; 31:3
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Tidskriftsartikel (refereegranskat)abstract
- Objective Fast-track concepts have been implemented in hepatopancreatobiliary surgery cancer care to improve postoperative recovery. For optimal postoperative care, patient participation is also required. The aim was to investigate and analyse whether an intervention with patient-owned fast-track protocols (PFTPs) may lead to increased patient participation and improve information for patients who underwent surgery for hepatopancreatobiliary cancer. Methods A quantitative comparative design with a control and intervention group was used. The participants in the intervention group followed a PFTP during their admission. After discharge, the patients answered a questionnaire regarding patient participation. Data analyses were performed with descriptive statistics and ANCOVA. Results The results are based on a total of 222 completed questionnaires: 116 in the control group and 106 in the intervention group. It is uncertain whether the PFTP increased patient participation and information, but its use may indicate an improvement for the patient group. Conclusion A successful implementation strategy for the use of PFTP, with daily reconciliations, could be part of the work required to improve overall satisfaction with patient participation.
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| 2. |
- Aspholm, Marina, et al.
(författare)
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SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans.
- 2006
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Ingår i: PLoS pathogens. - : Public Library of Science (PLoS). - 1553-7374 .- 1553-7366. ; 2:10
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Tidskriftsartikel (refereegranskat)abstract
- Adherence of Helicobacter pylori to inflamed gastric mucosa is dependent on the sialic acid-binding adhesin (SabA) and cognate sialylated/fucosylated glycans on the host cell surface. By in situ hybridization, H. pylori bacteria were observed in close association with erythrocytes in capillaries and post-capillary venules of the lamina propria of gastric mucosa in both infected humans and Rhesus monkeys. In vivo adherence of H. pylori to erythrocytes may require molecular mechanisms similar to the sialic acid-dependent in vitro agglutination of erythrocytes (i.e., sialic acid-dependent hemagglutination). In this context, the SabA adhesin was identified as the sialic acid-dependent hemagglutinin based on sialidase-sensitive hemagglutination, binding assays with sialylated glycoconjugates, and analysis of a series of isogenic sabA deletion mutants. The topographic presentation of binding sites for SabA on the erythrocyte membrane was mapped to gangliosides with extended core chains. However, receptor mapping revealed that the NeuAcalpha2-3Gal-disaccharide constitutes the minimal sialylated binding epitope required for SabA binding. Furthermore, clinical isolates demonstrated polymorphism in sialyl binding and complementation analysis of sabA mutants demonstrated that polymorphism in sialyl binding is an inherent property of the SabA protein itself. Gastric inflammation is associated with periodic changes in the composition of mucosal sialylation patterns. We suggest that dynamic adaptation in sialyl-binding properties during persistent infection specializes H. pylori both for individual variation in mucosal glycosylation and tropism for local areas of inflamed and/or dysplastic tissue.
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| 3. |
- Drott, Jenny, et al.
(författare)
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Patient preferences and experiences of participation in surgical cancer care
- 2022
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Ingår i: Worldviews on Evidence-Based Nursing. - : John Wiley & Sons. - 1545-102X .- 1741-6787. ; 19:5, s. 405-414
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Tidskriftsartikel (refereegranskat)abstract
- Background Quality cancer care necessitates opportunities for patient participation, supposedly recognizing the individual's preferences and experiences for being involved in their health and healthcare issues. Previous research shows that surgical cancer patients wish to be more involved, requiring professionals to be sensitive of patients' needs. Aims To explore preference-based patient participation in surgical cancer care. Methods A cross-sectional study was conducted. The Patient Preferences for Patient Participation tool (4Ps) was used, which includes 12 attributes of preferences for and experiences of patient participation. Data were analyzed with descriptive and comparative statistical methods. Results The results are based on a total of 101 questionnaires. Having reciprocal communication and being listened to by healthcare staff were commonly deemed crucial for patient participation. While 60% of the patients suggested that taking part in planning was crucial for their participation, they had experienced this only to some extent. Learning to manage symptoms and phrasing personal goals were items most often representing insufficient conditions for preference-based patient participation. Linking Evidence to Action To support person-centered surgical care, further efforts to suffice preference-based participation are needed, including opportunities for patients to share their experiences and engage in the planning of healthcare activities.
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| 4. |
- Henriksson, Sara, et al.
(författare)
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Clinical isolates of Helicobacter pylori demonstrates alternative BabA-mediated adherence to human gastric mucosa
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Annan publikation (övrigt vetenskapligt/konstnärligt)abstract
- Helicobacter pylori infection is life-long and can cause peptic ulcer disease and gastric cancer. The H. pylori BabA adhesin binds the ABO/Leb blood group (bg) antigens (Leb), which mediates attachment to the gastric epithelium. The prevalence of ABO binding is high worldwide and also in northern Europe. However, prevalence is reduced by 50% in Germany and is further reduced in Spain and Portugal. An inventory of strains from different European populations resulted in strains with high level of BabA expression but very little or no binding to Leb. The majority of such strains could not bind to human gastric mucosa in vitro. We further characterized a Spanish isolates, strain 812, that binds only weakly to soluble Leb-conjugate but still adheres firmly to gastric mucosa indicative of that it might bind to an alternative set of receptor. Receptor analysis by glycan arrays revealed higher binding of strain 812 to ALeb and Bleb glycans than to Leb, indicating that BabA from strain 812 has shifted its binding epitope somewhat away from the central Fuca1.2Gal bg domain and closer to the very terminal bg A and B determinants, i.e. GalNAca1.3Gal (bgA) or the Gala1.3Gal (bgB). By a colony screening approach we identified a subpopulation of 812 clones adapted for stronger Leb binding. Such affinity shifts comes from replacement of distinguishing amino acids by mechanisms of recombination with a BabA-related outer membrane protein.
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| 5. |
- Moonens, Kristof, et al.
(författare)
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Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori
- 2016
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Ingår i: Cell Host and Microbe. - : Elsevier BV. - 1931-3128 .- 1934-6069. ; 19:1, s. 55-66
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Tidskriftsartikel (refereegranskat)abstract
- The Helicobacter pylori adhesin BabA binds mucosal ABO/Le b blood group (bg) carbohydrates. BabA facilitates bacterial attachment to gastric surfaces, increasing strain virulence and forming a recognized risk factor for peptic ulcers and gastric cancer. High sequence variation causes BabA functional diversity, but the underlying structural-molecular determinants are unknown. We generated X-ray structures of representative BabA isoforms that reveal a polymorphic, three-pronged Le(b) binding site. Two diversity loops, DL1 and DL2, provide adaptive control to binding affinity, notably ABO versus O bg preference. H. pylori strains can switch bg preference with single DL1 amino acid substitutions, and can coexpress functionally divergent BabA isoforms. The anchor point for receptor binding is the embrace of an ABO fucose residue by a disulfide-clasped loop, which is inactivated by reduction. Treatment with the redox-active pharmaceutic N-acetylcysteine lowers gastric mucosal neutrophil infiltration in H. pylori-infected Le(b)-expressing mice, providing perspectives on possible H. pylori eradication therapies.
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| 6. |
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| 7. |
- Nordén, Jenny
(författare)
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Multifaceted adhesion properties of Helicobacter pylori in promotion of gastric disease
- 2011
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Licentiatavhandling (övrigt vetenskapligt/konstnärligt)abstract
- Helicobacter pylori is a Gram-negative spiral-shaped bacteria that resides in the gastric mucosa and adheres to the epithelial lining of the human stomach. H. pylori adhesion mediates inflammation of the epithelium, which can lead to more severe diseases such as chronic active gastritis and gastric carcinoma. In order to adhere tightly to the mucosal lining, H. pylori expresses adhesion proteins called adhesins. The best-charachterized adhesins are blood group antigen binding adhesin, BabA, and sialic acid binding adhesin, SabA. During chronic infection there is an adhesion/inflammation-associated balance between BabA- and SabA-mediated binding modes. BabA is the major mediator of binding when the stomach is in good health and the corresponding binding receptors are ABO blood group antigens such as the difucosylated Lewis b antigen that is expressed on MUC5AC mucins by the surface epithelium. However, in chronic inflammation of the gastric mucosa there are dynamic shifts in the glycosylation patterns; in inflamed gastric tissue, SabA is an important mediator of bacterial binding and adherence. The corresponding binding receptors for the SabA adhesin are complex sialylated antigens such as sLewis x (sLex) and sLewis a (sLea). In this thesis, I describe our findings that SabA also promotes H. pylori binding to red blood cells in the gastric mucosal small blood vessels. The minimal binding epitope on the erythrocyte surfaces is the sialylated NeuAcα2-3Gal-disaccharide and this bacterial adherence promotes hemagglutination, i.e. the rapid aggregation of the erythrocytes. Another important finding is that the binding properties of SabA are of polymorphic nature. In particular, clinical isolates demonstrate variant types of relative binding affinity for the series of sialyl-di Lewis x (sdiLex), sialyl-Lewis a (sLea) and sialyl-lactosamine (sLn). The relative binding to sialylated glycans is strain dependent and H. pylori strains J99 and SMI9 display different SabA-mediated binding modes for sialylated glycans. By introduction of the sabA gene from strain J99 into strain SMI9, the detailed binding mode of SMI9sabAJ99 was altered and preferably displayed the original binding mode of strain J99. Thus, the polymorphism of SabA-mediated binding is an inherent property of the adhesion protein itself, i.e. the polypeptide itself and is not encoded or influenced by the strain genome background. The individualized binding properties or polymorphism in binding modes provides SabA with the opportunity to adapt to individual hosts and to the inflammatory changes in glycosylation. SabA expression makes use of slipped-strand mispairing for H. pylori to swiftly attach and detach from the epithelium. Furthermore, the ability to fluently attach and detach from the epithelial surfaces is an important feature of H. pylori and its ability to evade the mucosal inflammatory responses, as well as from the rapid turnover and shedding of gastric mucosa. Here, I describe a novel blood group antigen binding outer membrane protein, FecA3. This is an adhesin candidate, which independently of BabA, binds the series of fucosylated blood group antigens. The similar binding modes of BabA and FecA3 for ABO blood group antigens is not fully understood but the expression of FecA3 is regulated by the nickel-responsive regulator NikR, which acts as a sensor regulated by the availability of free nickel ions. Ni2+increases when pH is lowered, thus regulation of FecA3 is suggested to be governed by local pH. Taken together, the high-affinity binding by BabA, and continuous biopanning for the fittest, in particular for the low-affinity binding of FecA3, might be contrasting but complementary properties and features of the different adhesins that are of importance during different stages of mucosal inflammation and disease development.
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