Radiographers' confidence in handling iodine based contrast media hypersensitivity reactions.

INTRODUCTION: Adverse reactions to iodinated contrast media, which is used during computed tomography (CT) examinations, are rare. As a result, radiographers have limited experience handling those situations and may feel uncertainty and a lack of confidence. The aim of this study was to investigate radiographers' confidence in handling hypersensitivity reactions to contrast media during CT examinations. METHODS: A survey in the form of a questionnaire was conducted to gather both quantitative and qualitative data. There were 31 clinics that participated in this study, of which four were university hospitals, 17 were medium-sized hospitals and 10 were small hospitals. In total, the questionnaires were distributed to 700 radiographers. The questionnaire contained 12 questions and was distributed via email with a link to the questionnaire. RESULTS: Two hundred-ninety radiographers participated in the survey. 72% of the respondents answered in the middle of the four-point scale (2-3) in response to the statement "I feel confident in handling hypersensitivity reactions". 65% answered that they did not have routines for training regularly regarding hypersensitivity reactions. Qualitative data showed that many of the respondents wished to receive education and training regularly. CONCLUSIONS: The confidence of radiographers regarding the management of hypersensitivity reactions was deficient and most of the respondents wished they felt more confident. IMPLICATION FOR PRACTICE: To increase radiographers' confidence in handling hypersensitivity reactions, it is recommended that the radiology clinics review their routines and the possibility to implement regular training.

Retrospective comparison between MRI examinations during radiographer-administered intranasal sedation or general anesthesia.

INTRODUCTION: In order for young children to be able to undergo a Magnetic Resonance Imaging (MRI) examination, general anesthesia is often required. The aim of this study was to compare the image quality, times, and costs of the examinations of infant brains performed with MRI either during sedation with dexmedetomidine administered by radiographers or anesthesia with propofol administered by anesthesia staff. METHODS: This study was a quantitative retrospective study of 27 consecutive standard brain examinations performed under sedation or anesthesia, involving 15 children under sedation and 12 under anesthesia. The age of the children was from 0.5 to five years old. The image quality was evaluated by three radiologists experienced in pediatric MRI examinations. Information such as examination time and the expense of the examination was also collected. RESULTS: There was no statistically significant difference in the general image quality, but one image series was assessed to have significantly better image quality under sedation than under anesthesia, but all images had very high quality. However, it emerged that children under anesthesia were at the hospital on average 55 min longer and the scanner room was occupied 20 min longer on average. The anesthesia examinations were three times more expensive. CONCLUSION: This study demonstrated equivalent image quality between sedation and anesthesia. In addition, sedation was less time-consuming and had a lower price, partly because no extra anesthetic staff were required. The use of intranasal sedation offers a possibility to expand the competence area for radiographers. IMPLICATIONS FOR PRACTICE: If radiographers learn to perform intranasal sedation, examinations can be performed in less time, at a third of the staff costs while maintaining image quality.

Quantifying differences in hepatic uptake of the liver specific contrast agents Gd-EOB-DTPA and Gd-BOPTA: a pilot study.

OBJECTIVES: To develop and evaluate a procedure for quantifying the hepatocyte-specific uptake of Gd-BOPTA and Gd-EOB-DTPA using dynamic contrast-enhanced (DCE) MRI. METHODS: Ten healthy volunteers were prospectively recruited and 21 patients with suspected hepatobiliary disease were retrospectively evaluated. All subjects were examined with DCE-MRI using 0.025 mmol/kg of Gd-EOB-DTPA. The healthy volunteers underwent an additional examination using 0.05 mmol/kg of Gd-BOPTA. The signal intensities (SI) of liver and spleen parenchyma were obtained from unenhanced and enhanced acquisitions. Using pharmacokinetic models of the liver and spleen, and an SI rescaling procedure, a hepatic uptake rate, K (Hep), estimate was derived. The K (Hep) values for Gd-EOB-DTPA were then studied in relation to those for Gd-BOPTA and to a clinical classification of the patient's hepatobiliary dysfunction. RESULTS: K (Hep) estimated using Gd-EOB-DTPA showed a significant Pearson correlation with K (Hep) estimated using Gd-BOPTA (r = 0.64; P < 0.05) in healthy subjects. Patients with impaired hepatobiliary function had significantly lower K (Hep) than patients with normal hepatobiliary function (K (Hep) = 0.09 ± 0.05 min(-1) versus K (Hep) = 0.24 ± 0.10 min(-1); P < 0.01). CONCLUSIONS: A new procedure for quantifying the hepatocyte-specific uptake of T (1)-enhancing contrast agent was demonstrated and used to show that impaired hepatobiliary function severely influences the hepatic uptake of Gd-EOB-DTPA. KEY POINTS: • The liver uptake of contrast agents may be measured with standard clinical MRI. • Calculation of liver contrast agent uptake is improved by considering splenic uptake. • Liver function affects the uptake of the liver-specific contrast agent Gd-EOB-DTPA. • Hepatic uptake of two contrast agents (Gd-EOB-DTPA, Gd-BOPTA) is correlated in healthy individuals. • This method can be useful for determining liver function, e.g. before hepatic surgery.

Radiology departmental policy compliance with Swedish guidelines regarding post-contrast acute kidney injury for examinations with iodinated contrast media.

INTRODUCTION: Guidelines concerning intravenous iodinated contrast media (CM) during computed tomography (CT) examinations are important to follow to minimize the risk for post-contrast acute kidney injury (PC-AKI). The purpose of this study was to investigate the radiology departmental policy compliance with Swedish guidelines concerning PC-AKI. METHODS: In February 2020, an electronic survey was distributed to the responsible radiographer at 41 radiology departments in all university hospitals and medium-sized hospitals in Sweden. The questions focused on routines around renal functional tests, individualized contrast administration and handling of patients with diabetes mellitus taking metformin. RESULTS: The response rate was 83%. Seventy-six percent (n = 26) of radiology departments calculated estimated glomerular filtration rate (eGFR) from serum creatinine prior to CM administration, but only 24% (n = 8) followed the recommendation to calculate eGFR from both serum creatinine and cystatin C. For acute/inpatients, 55% (n = 18) followed the recommendation that renal functional tests should be performed within 12 h before CM administration. For elective patients, 97% (n = 33) followed the recommendation to have eGFR newer than three months which is acceptable for patients with no history of disease that may have affected renal function. Approximately 80% of the radiology departments followed the recommendation that CM dose always should be individually adjusted to patient eGFR. Seventy-six percent (n = 26) followed the recommendation to continue with metformin at eGFR ≥ 45 ml/min. CONCLUSION: Compliance with the national guidelines was high regarding routines around renal functional tests, dose adjustment of CM and metformin discontinuation. Improvements can be made in using both cystatin C and serum creatinine for eGFR calculations as well as ensuring renal function tests within 12 h for acute/inpatients with acute disease that may affect renal function. IMPLICATIONS FOR PRACTICE: This study raises awareness of the importance of adhering to guidelines in healthcare. To have knowledge about the current level of compliance regarding PCI-AKI is important to maintain and develop effective clinical implementation of guidelines. The variation in practice seen in this study emphasizes the need of more effective implementation strategies to ensure adherence with best practice.

Structural basis of pilus subunit recognition by the PapD chaperone.

The assembly of different types of virulence-associated surface fibers called pili in Gram-negative bacteria requires periplasmic chaperones. PapD is the prototype member of the periplasmic chaperone family, and the structural basis of its interactions with pilus subunits was investigated. Peptides corresponding to the carboxyl terminus of pilus subunits bound PapD and blocked the ability of PapD to bind to the pilus adhesin PapG in vitro. The crystal structure of PapD complexed to the PapG carboxyl-terminal peptide was determined to 3.0 A resolution. The peptide bound in an extended conformation with its carboxyl terminus anchored in the interdomain cleft of the chaperone via hydrogen bonds to invariant chaperone residues Arg8 and Lys112. Main chain hydrogen bonds and contacts between hydrophobic residues in the peptide and the chaperone stabilized the complex and may play a role in determining binding specificity. Site-directed mutations in Arg8 and Lys112 abolished the ability of PapD to bind pilus subunits and mediate pilus assembly in vivo, an indication that the PapD-peptide crystal structure is a reflection of at least part of the PapD-subunit interaction.

Transferred nuclear Overhauser effect spectroscopy study of a peptide from the PapG pilus subunit bound by the Escherichia coli PapD chaperone.

Interaction of the Escherichia coli PapD chaperone with the synthetic peptide PapG308-314 (Thr-Met-Val-Leu-Ser-Phe-Pro), corresponding to the seven C-terminal residues of the PapG pilus subunit, was studied by transferred nuclear Overhauser effect (TRNOE) spectroscopy. The observation of cross-peaks corresponding to either intraresidue or sequential C(alpha)H/NH and C(beta)H/NH TRNOEs and the absence of sequential NH(i)/NH(i+1) TRNOEs indicate that the peptide binds to PapD in an extended conformation. In addition, line-broadening effects gave information of the peptide's mode of interaction with PapD. These observations were in excellent agreement with a recent crystal structure of a PapG peptide complexed with PapD.

Major histocompatibility complex class I binding glycopeptides for the estimation of 'empty' class I molecules.

Different forms of major histocompatibility complex (MHC) class I heavy chains are known to be expressed on the cell surface, including molecules which are functionally 'empty'. Direct peptide binding to cells is obvious during sensitization of target cells in vitro for cytotoxic T lymphocyte killing and 'empty' MHC-I molecules are comparatively abundant on TAP-1/2 peptide transporter mutant cells. In the present work we have estimated the fraction of 'empty' MHC class I molecules using glycosylated peptides and cellular staining with carbohydrate specific monoclonal antibodies. Synthetic Db and Kb binding peptides were coupled at different positions with different di- or trisaccharides, using different spacing between the carbohydrate and the peptide backbone. Binding of sugar specific mAbs was compared in ELISA and cellular assays. An optimal Db binding glycopeptide was used for comparative staining with anti-Db and anti-carbohydrate monoclonal antibodies to estimate fractions of 'empty' molecules on different T lymphoid cells. On activated normal T cells, a large fraction of Db molecules were found to be 'empty'. The functional role of such 'empty' MHC class I molecules on T cells is presently unclear. However, on antigen presenting cells they might participate in the antigen presentation process.

Glycosylated peptide hormones: pharmacological properties and conformational studies of analogues of [1-desamino,8-D-arginine]vasopressin.

Two analogues of the antidiuretic drug [1-desamino,8-D-arginine]vasopressin (DDAVP), which have a glycosylated serine at position 4, have been prepared by Fmoc solid phase peptide synthesis. The glycosylated analogues had significantly higher bioavailabilities than the nonglycosylated [D-Tyr2,Ser4]DDAVP and DDAVP on intraintestinal administration in rat. The improved bioavailability resulted from an increased absorption from the small intestine and most likely from an increased stability toward enzymatic degradation, whereas plasma clearance was either unaffected or slightly increased by the glycosylation. The glycosylated analogues displayed only very low agonistic and antagonistic activities at the vasopressin V2-receptor. Conformational studies performed by 1H NMR spectroscopy did not reveal any major influence from glycosylation on the conformation of the peptide backbone. The lack of receptor binding displayed by the analogues is therefore most likely explained by steric repulsion between the carbohydrate moiety and the vasopressin receptor which prevents receptor binding.

Monitoring solid-phase glycoside synthesis with (19)F NMR spectroscopy.

[structure: see text] A simple and efficient method for monitoring and optimizing carbohydrate synthesis on polymeric support by using (19)F NMR spectroscopy is described. The method relies on the use of fluorinated variants of protective groups that are in common use in oligosaccharide synthesis.

The synthesis of antibody binding-site probes: a hexasaccharide and two pentasaccharides related to the Brucella A antigen and prepared by in situ activation of thioglycosides with bromine.

Two pentasaccharide analogues and a hexasaccharide fragment of the Brucella A antigen [----2)-alpha-D-Rhap4NFo-(1----]n have been prepared as their methyl glycosides. The pentasaccharide analogues each have two formamido groups replaced by hydroxyl groups. Protected derivatives of the three oligosaccharides were prepared by in situ activation with bromine of mono- and di-saccharide thioglycosides of D-rhamnose and 4-azido-4,6-dideoxy-D-mannose in the presence of a glycosyl acceptor and silver triflate as promoter. Reduction of the azido groups with hydrogen sulfide, N-formylation with ethyl formate, and hydrogenolysis then gave the target pentasaccharide glycosides.

The design and synthesis of antibody binding site probes: three pentasaccharide analogues of the Brucella A antigen prepared by activation in situ of thioglycosides with bromine.

Three pentasaccharide analogues of the Brucella A antigen [----2)-alpha-D-Rhap4NFo-(1----], each with one formamido group replaced by a hydroxyl group, have been prepared as their methyl glycosides. Mono- and di-saccharide thioglycosides of D-rhamnose and 4-azido-4,6-dideoxy-D-mannose were used as glycosyl donors for the preparation of protected pentasaccharide derivatives with trisaccharides as intermediates. Glycosylations were performed by activation in situ of the thioglycosides with bromine in the presence of a glycosyl acceptor and silver triflate as promoter. Reduction of the azido groups with hydrogen sulfide. N-formylation with ethyl formate, and hydrogenolysis then gave the target pentasaccharides.

Synthetic receptor analogues: the conformation of methyl 4-O-alpha-D-galactopyranosyl-beta-D-galactopyranoside (methyl beta-D-galabioside) and related derivatives, determined by n.m.r. and computational methods.

The conformations of galabiose and its methyl and ethyl beta-glycosides as well as the 3-deoxy, 3-O-methyl, 3-deoxy-3-C-methyl, 3-deoxy-3-C-ethyl, and 6-deoxy analogues were investigated by n.m.r. (1H, 13C, n.O.e.) and computational (HSEA) methods. A good correlation was found between the computational data and the n.m.r. data for aqueous solutions. The conformations in aqueous solution were similar, whereas crystalline galabiose or methyl beta-D-galabioside in solution in methyl sulfoxide adopted different conformations that showed intramolecular hydrogen bonds (O-5'. . . O-3 and O-2'. . . O-6, respectively).

Solid-phase synthesis and conformational studies of glycosylated derivatives of helper-T-cell immunogenic peptides from hen-egg lysozyme.

3-Mercaptopropionic acid and N alpha-Fmoc serine, both with unprotected carboxyl groups, were stereospecifically glycosylated in 62-82% yields, using saccharide 1,2-trans peracetates and Lewis acid catalysis. The resulting glycosylated building blocks were used in the synthesis of derivatives of helper-T-cell stimulating peptides, with the carbohydrate moiety located at the amino terminus, or internally in the peptide chain. 1H NMR spectroscopy in Me2SO-d6 showed that the glycopeptides assumed random conformations, which were not influenced by the glycosylation or by single substitutions of amino acids in the peptide moiety.

Synthesis of a water-soluble serine-based neoglycolipid which can be covalently linked to solid phases.

N alpha-Fmoc-serine pentafluorophenyl ester was glycosylated with perbenzoylated lactosyl bromide. The resulting product was coupled to a resin functionalized with 6-aminohexanoic acid and then N alpha-acylated to give a serine-based analogue of lactosylceramide. The water-soluble neoglycolipid was covalently linked to microtiter plates via its carboxyl group and was recognized by a lactose-binding lectin in an ELISA.

Synthetic receptor analogues: preparation and calculated conformations of the 2-deoxy, 6-O-methyl, 6-deoxy, and 6-deoxy-6-fluoro derivatives of methyl 4-O-alpha-D-galactopyranosyl-beta-D-galactopyranoside (methyl beta-D-galabioside).

The 2-deoxy (7), 6-O-methyl (15), 6-deoxy (22), and 6-deoxy-6-fluoro (31) derivatives of methyl beta-D-galabioside (1) have been synthesised. Thus, 7 was prepared by xanthate reduction using tributyltin hydride, whereas 22 was obtained by catalytic hydrogenation of a 6-deoxy-6-iodogalabioside. Regioselective monofluorination of methyl 2,3-di-O-benzoyl-beta-D-galactopyranoside with Et2NSF3 and subsequent alpha-D-galactosylation provided 31. Molecular mechanics calculations yielded similar conformations for 1, 7, 15, 22, and 31 with differences in phi H and psi H of less than 5 degrees. No indications of intramolecular hydrogen bonds, as displayed by 1 in the crystal, were found for 7, 15, 22, or 31.

Preparation and calculated conformations of the 2'-, 3'-, 4'-, and 6'-deoxy, 3'-O-methyl, 4'-epi, and 4'- and 6'-deoxy-fluoro derivatives of methyl 4-O-alpha-D-galactopyranosyl-beta-D-galactopyranoside (methyl beta-D-galabioside).

The glycosyl chlorides of the 3-O-methyl (6) and 4-deoxy-4-fluoro (8) O-benzylated derivatives of D-galactopyranose and 2,3,4,6-tetra-O-benzyl-D-glucopyranose were condensed with methyl 2,3,6-tri-O-benzoyl-beta-D-galactopyranoside to give, after deprotection, the 3'-O-methyl (23), 4'-deoxy-4'-fluoro (25), and 4'-epi (27) derivatives, respectively, of methyl beta-D-galabioside (1). The glycosyl fluorides of 2,3,4-tri-O-benzyl-D-fucopyranose and the 3-deoxy (12) and 4-deoxy (16) O-benzylated derivatives of D-galactopyranose were condensed with methyl 2,3,6-tri-O-benzyl-beta-D-galactopyranoside (21), to give, after deprotection, the 6'-deoxy (31), 3'-deoxy (34), and 4'-deoxy (37) derivatives of 1, respectively. The 2'-deoxy (41) derivative of 1 was prepared by N-iodosuccinimide-induced condensation of 3,4,6-tri-O-acetyl-D-galactal and 21 followed by deprotection. Treatment of methyl 2,3,6-tri-O-benzoyl-4-O-(2,3-di-O-benzoyl-alpha-D-galactopyranosyl)-beta -D- galactopyranoside with Et2NSF3 (DAST), followed by deprotection, provided the 6'-deoxy-6'-fluoro (46) derivative of 1. Molecular mechanics calculations yielded conformations for 23, 25, 27, 31, 34, 37, 41, and 46 with small deviations from the calculated conformation for 1 (phi H/psi H: -40 degrees/-6 degrees).