| 1. |
- Baird, D L H, et al.
(author)
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Endovascular treatment of isolated iliac artery aneurysms using a custom-made stent graft with proximal barb fixation : early outcome
- 2013
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In: Vascular. - : SAGE Publications. - 1708-5381 .- 1708-539X. ; 21:2, s. 92-96
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Journal article (peer-reviewed)abstract
- Current endovascular treatments for isolated iliac artery aneurysms (IIAAs) include the use of aortoiliac stent grafts with coverage of the distal aorta or stent grafts confined to the iliac artery without active proximal fixation. We report our experience in the use of custom-made Cook ZenithTM iliac limb stent grafts with proximal barb fixation. Patients treated from July 2009 to February 2011 were included. All imaging and patient records were assessed for perioperative and early outcomes. Nine IIAAs (seven patients) were treated. The mean patient age was 80 years (range 58–91 years). The mean aneurysm size was 48 mm (35–80 mm), and the mean length of the proximal landing zone (PLZ) was 29 mm (10–50 mm). The distal landing zone was in the external iliac artery after coil embolization of the internal iliac artery. The Mean diameter of the PLZ was 21 mm (20–24 mm). Technical success was achieved in eight cases. Perioperative complications included reoperation in one patient for groin bleeding and ischemia. On follow-up (mean 12 months, range 1–26), all aneurysms were successfully excluded from the circulation and there was no stent graft migration or thrombosis. Use of custom-made stent grafts with proximal barb fixation in treatment of IIAAs is a feasible option which may reduce the risk of migration when compared with stent grafts with lack of proximal fixation.
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| 2. |
- HAKANSSON, A, et al.
(author)
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Apoptosis induced by a human milk protein
- 1995
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In: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424. ; 92:17, s. 8064-8068
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Journal article (peer-reviewed)abstract
- To the breast-fed infant, human milk is more than a source of nutrients; it furnishes a wide array of molecules that restrict microbes, such as antibodies, bactericidins, and inhibitors of bacterial adherence. However, it has rarely been considered that human milk may also contain substances bioactive toward host cells. While investigating the effect of human milk on bacterial adherence to a human lung cancer cell line, we were surprised to discover that the milk killed the cells. Analysis of this effect revealed that a component of milk in a particular physical state--multimeric alpha-lact-albumin--is a potent Ca(2+)-elevating and apoptosis-inducing agent with broad, yet selective, cytotoxic activity. Multimeric alpha-lactalbumin killed all transformed, embryonic, and lymphoid cells tested but spared mature epithelial elements. These findings raise the possibility that milk contributes to mucosal immunity not only by furnishing antimicrobial molecules but also by policing the function of lymphocytes and epithelium. Finally, analysis of the mechanism by which multimeric alpha-lactalbumin induces apoptosis in transformed epithelial cells could lead to the design of antitumor agents.
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| 3. |
- Håkansson, Anders P, et al.
(author)
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A folding variant of alpha-lactalbumin with bactericidal activity against Streptococcus pneumoniae
- 2000
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In: Molecular Microbiology. - : Wiley. - 0950-382X .- 1365-2958. ; 35:3, s. 589-600
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Journal article (peer-reviewed)abstract
- This study describes an alpha-lactalbumin folding variant from human milk with bactericidal activity against antibiotic-resistant and -susceptible strains of Streptococcus pneumoniae. The active complex precipitated with the casein fraction at pH 4.6 and was purified from casein by a combination of anion exchange and gel chromatography. Unlike other casein components, the active complex was retained on the ion-exchange matrix and eluted only with high salt. The eluted fraction showed N-terminal and mass spectrometric identity with human milk alpha-lactalbumin, but native alpha-lactalbumin had no bactericidal effect. Spectroscopic analysis demonstrated that the active form of the molecule was in a different folding state, with secondary structure identical to alpha-lactalbumin from human milk whey, but fluctuating tertiary structure. Native alpha-lactalbumin could be converted to the active bactericidal form by ion-exchange chromatography in the presence of a cofactor from human milk casein, characterized as a C18:1 fatty acid. Analysis of the antibacterial spectrum showed selectivity for streptococci; Gram-negative and other Gram-positive bacteria were resistant. The folding variant of alpha-lactalbumin is a new example of naturally occurring molecules with antimicrobial activity.
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| 4. |
- Sabharwal, H, et al.
(author)
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Blood group specific oligosaccharides from faeces of a blood group A breast-fed infant
- 1984
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In: Molecular Immunology. - : Elsevier BV. - 1872-9142 .- 0161-5890. ; 21:11, s. 1105-1112
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Journal article (peer-reviewed)abstract
- Four different oligosaccharides were isolated from faeces collected from a blood group A, secretor, breast-fed infant. Three of these, GalNAc alpha 1-3[Fuc alpha 1-2]Gal beta 1-4Glc (A-tetrasaccharide), GalNAc alpha 1-3[Fuc alpha 1-2]Gal beta 1-4[Fuc alpha 1-3]Glc (A-pentasaccharide) and 1-3[Fuc alpha 1-4]GlcNAc beta 1-3Gal beta 1-4Glc (A-heptasaccharide) have previously found in urine, whereas GalNAc alpha 1-3[Fuc alpha 1-2]Gal beta 1-3GlcNAc beta 1-3Gal beta 1-4Glc (A-hexasaccharide) is a new compound. Structures were deduced by mass spectrometry of permethylated and N-trifluoroacetylated oligosaccharide alditols. The latter gave more structural information than the corresponding N-acetyl derivatives. The four oligosaccharides were tested for blood group A activity and all were found to inhibit the binding of anti-A antibody to blood group A substance.
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| 5. |
- Song, Tianyan, et al.
(author)
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Vibrio cholerae Utilizes Direct sRNA Regulation in Expression of a Biofilm Matrix Protein
- 2014
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In: PLOS ONE. - : PLOS. - 1932-6203. ; 9:7
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Journal article (peer-reviewed)abstract
- Vibrio cholerae biofilms contain exopolysaccharide and three matrix proteins RbmA, RbmC and Bap1. While much is known about exopolysaccharide regulation, little is known about the mechanisms by which the matrix protein components of biofilms are regulated. VrrA is a conserved, 140-nt sRNA of V. cholerae, whose expression is controlled by sigma factor sigma(E). In this study, we demonstrate that VrrA negatively regulates rbmC translation by pairing to the 5' untranslated region of the rbmC transcript and that this regulation is not stringently dependent on the RNA chaperone protein Hfq. These results point to VrrA as a molecular link between the sigma(E)-regulon and biofilm formation in V. cholerae. In addition, VrrA represents the first example of direct regulation of sRNA on biofilm matrix component, by-passing global master regulators.
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