Management of penicillin allergy in primary care: a qualitative study with patients and primary care physicians

Background Six percent of patients are allergic to penicillin according to their medical records. While this designation protects a small number of truly allergic patients from serious reactions, those who are incorrectly labelled may be denied access to recommended first line treatment for many infections. Removal of incorrect penicillin allergy may have positive health consequences for the individual and the general population. We aimed to explore primary care physicians’ (PCPs) and patients’ views and understanding of penicillin allergy with a focus on clinical management of infections in the face of a penicillin allergy record. Methods We conducted an interview study with 31 patients with a penicillin allergy record, and 19 PCPs in the North of England. Data were analysed thematically. Results Patients made sense of their allergy status by considering the timing and severity of symptoms. Diagnosis of penicillin allergy was reported to be ‘imperfect’ with PCPs relying on patient reports and incomplete medical records. PCPs and patients often suspected that an allergy record was incorrect, but PCPs were reluctant to change records. PCPs had limited knowledge of allergy services. PCPs often prescribed alternative antibiotics which were easy to identify. Both patients and PCPs differed in the extent to which they were aware of the negative consequences of incorrect penicillin allergy records, their relevance and importance to their lives, and management of penicillin allergy. Conclusions PCPs and patients appear insufficiently aware of potential harms associated with incorrect penicillin allergy records. Some of the problems experienced by PCPs could be reduced by ensuring the details of newly diagnosed reactions to antibiotics are clearly documented. In order for PCPs to overturn more incorrect penicillin records through appropriate use of allergy services, more information and training about these services will be needed

Expression of NRG1 and its receptors in human bladder cancer

BACKGROUND: Therapies targeting ERBB2 have shown success in the clinic. However, response is not determined solely by expression of ERBB2. Levels of ERBB3, its preferred heterodimerisation partner and ERBB ligands may also have a role. METHODS: We measured NRG1 expression by real-time quantitative RT–PCR and ERBB receptors by western blotting and immunohistochemistry in bladder tumours and cell lines. RESULTS: NRG1a and NRG1b showed significant coordinate expression. NRG1b was upregulated in 78 % of cell lines. In tumours, there was a greater range of expression with a trend towards increased NRG1a with higher stage and grade. Increased expression o

ESUR prostate MR guidelines 2012

The aim was to develop clinical guidelines for multi-parametric MRI of the prostate by a group of prostate MRI experts from the European Society of Urogenital Radiology (ESUR), based on literature evidence and consensus expert opinion. True evidence-based guidelines could not be formulated, but a compromise, reflected by “minimal” and “optimal” requirements has been made. The scope of these ESUR guidelines is to promulgate high quality MRI in acquisition and evaluation with the correct indications for prostate cancer across the whole of Europe and eventually outside Europe. The guidelines for the optimal technique and three protocols for “detection”, “staging” and “node and bone” are presented. The use of endorectal coil vs. pelvic phased array coil and 1.5 vs. 3 T is discussed. Clinical indications and a PI-RADS classification for structured reporting are presented

Biochemical characterization of the cuticle collagen of the nematode Caenorhabditis elegans.

International audienceProteins of purified cuticles from adults of the small free-living nematode Caenorhabditis elegans are solubilized by reduction in the presence of a strong denaturing agent and then carboxymethylated. As in the large parasitic nematode Ascaris lumbricoides, these soluble proteins appeared to be collagens by their amino acid compositions. C. elegans cuticle collagen is separated into seven major components with different apparent molecular weights by molecular sieve chromatography and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The two main components, which together account for more than 64% of the total cuticle collagen, were extracted from gel after electrophoresis and analyzed. They differ in their amino acid compositions and would seem to represent genetically distinct collagen chains. The results presented lead to the hypothesis of the presence in this collagen of at least two different chains.Proteins of purified cuticles from adults of the small free-living nematode Caenorhabditis elegans are solubilized by reduction in the presence of a strong denaturing agent and then carboxymethylated. As in the large parasitic nematode Ascaris lumbricoides, these soluble proteins appeared to be collagens by their amino acid compositions. C. elegans cuticle collagen is separated into seven major components with different apparent molecular weights by molecular sieve chromatography and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The two main components, which together account for more than 64% of the total cuticle collagen, were extracted from gel after electrophoresis and analyzed. They differ in their amino acid compositions and would seem to represent genetically distinct collagen chains. The results presented lead to the hypothesis of the presence in this collagen of at least two different chains

CHARACTERIZATION OF MORPHOLOGICAL AND BIOCHEMICAL DEFECTS IN THE CUTICLE OF A DUMPY MUTANT OF CAENORHABDITIS-ELEGANS

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CHARACTERIZATION OF MORPHOLOGICAL AND BIOCHEMICAL DEFECTS IN THE CUTICLE OF A DUMPY MUTANT OF CAENORHABDITIS-ELEGANS

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Cloning and sequencing of a Porifera partial cDNA coding for a short-chain collagen.

International audienceCollagen is present in Porifera, the lowest multicellular animals, but there is no information available on the primary structure of the collagen chains in this phylum. Developing fresh-water sponges have been used to extract total RNA in order to study in vitro translation products and to construct a cDNA library. Four translated proteins were collagenase-sensitive (200 kDa, 160 kDa, 81 kDa and 48 kDa). The cDNA library was screened with a human collagen probe and a clone, EmC4, covering 1.2 kb was isolated. Nucleotide sequencing of EmC4 revealed a conceptual open reading frame coding for 366 amino acids terminated by a stop codon TGA with 103 nucleotides downstream. The presumed translation product encoded contained several domains: a non-collagenous C-terminal domain of 156 amino acids with 9 cysteines, an uninterrupted collagenous domain of 171 amino acids, a non-collagenous domain of 16 amino acids with 3 cysteines and a probably incomplete N-terminal collagenous domain of 23 amino acids. Comparison with other sequences suggested that this collagen chain might belong to a non-fibrillar collagen family which evolved into several sub-families giving rise to nematode cuticular collagens, and type IV collagens.Collagen is present in Porifera, the lowest multicellular animals, but there is no information available on the primary structure of the collagen chains in this phylum. Developing fresh-water sponges have been used to extract total RNA in order to study in vitro translation products and to construct a cDNA library. Four translated proteins were collagenase-sensitive (200 kDa, 160 kDa, 81 kDa and 48 kDa). The cDNA library was screened with a human collagen probe and a clone, EmC4, covering 1.2 kb was isolated. Nucleotide sequencing of EmC4 revealed a conceptual open reading frame coding for 366 amino acids terminated by a stop codon TGA with 103 nucleotides downstream. The presumed translation product encoded contained several domains: a non-collagenous C-terminal domain of 156 amino acids with 9 cysteines, an uninterrupted collagenous domain of 171 amino acids, a non-collagenous domain of 16 amino acids with 3 cysteines and a probably incomplete N-terminal collagenous domain of 23 amino acids. Comparison with other sequences suggested that this collagen chain might belong to a non-fibrillar collagen family which evolved into several sub-families giving rise to nematode cuticular collagens, and type IV collagens

Changes in location of type I collagen synthesis in two stages of fetal calf skin as revealed by in situ hybridization.

International audienceThe distribution of sites of type I collagen gene expression was studied in frozen sections of skin of 4 and 9 month-old calf fetuses by in situ hybridization using a human pro-alpha 1 type I collagen cDNA. The labelling varied with the different layers of the dermis and with the developmental stage considered. In the 4 month old fetus skin, the label appeared concentrated in the upper layer of the dermis at the lewel of the hair follicles. In the 9 month-old fetus skin, the difference of labelling between upper papillary dermis and lower dermis was less marked. Comparatively the distribution of the extracellular type I collagen was determined by indirect immunofluorescence. This collagen appeared present throughout the whole dermis with slight variations at 4 months, where there was less extracellular collagen near the hair bulbs. These results are in agreement with the idea that the collagen synthesis follows cutaneous differentiation. In addition, they support the hypothesis that collagen is deposited once morphogenetic events have occurred and plays thus a stabilizing role in formation of cutaneous appendages.The distribution of sites of type I collagen gene expression was studied in frozen sections of skin of 4 and 9 month-old calf fetuses by in situ hybridization using a human pro-alpha 1 type I collagen cDNA. The labelling varied with the different layers of the dermis and with the developmental stage considered. In the 4 month old fetus skin, the label appeared concentrated in the upper layer of the dermis at the lewel of the hair follicles. In the 9 month-old fetus skin, the difference of labelling between upper papillary dermis and lower dermis was less marked. Comparatively the distribution of the extracellular type I collagen was determined by indirect immunofluorescence. This collagen appeared present throughout the whole dermis with slight variations at 4 months, where there was less extracellular collagen near the hair bulbs. These results are in agreement with the idea that the collagen synthesis follows cutaneous differentiation. In addition, they support the hypothesis that collagen is deposited once morphogenetic events have occurred and plays thus a stabilizing role in formation of cutaneous appendages

SOME BIOCHEMICAL ASPECTS OF THE CUTICLE COLLAGEN OF THE NEMATODE CAENORHABDITIS-ELEGANS

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SOME BIOCHEMICAL ASPECTS OF THE CUTICLE COLLAGEN OF THE NEMATODE CAENORHABDITIS-ELEGANS

International audiencexx