Thrombosis of the external jugular vein: a rare complication of a proximal humerus fracture treated with collar and cuff immobilisation.

We report the case of an 87-year-old woman who developed a thrombosis of her external jugular vein after sustaining a proximal humerus fracture managed nonoperatively with a collar and cuff. At review in fracture clinic she was found to have an enlarged external jugular vein which was subsequently found to be thrombosed. Her collar and cuff had been applied very tightly and it was felt by the ENT team to be the cause of the thrombosis of her external jugular vein. She was fully anticoagulated with warfarin after subsequently developing a deep vein thrombosis in the subclavian and axillary veins. She made a full recovery following anticoagulation. In this case, we review the potential causes of this rare and underdiagnosed condition, as well as the usual investigations and treatments. We also review the common complications of this fracture and the alternative treatment options available.

Proteomic profiling of breast tissue collagens and site-specific characterization of hydroxyproline residues of collagen alpha-1-(I).

In a quantitative proteomics-based breast cancer study of complementary normal and tumor biopsies, 22 collagen isoforms were detected by LC-MALDI TOF/TOF MS. By applying proline oxidation, representing hydroxyproline, in database search parameters a substantial increase in assigned MS/MS was achieved, boosting the average (three experiments) number of peptides from 306 to 8126 for collagen alpha-1(I). The plethora of peptide identities for alpha-1(I) was disproportionate with full length protein sequence coverage which only increased from 28.3 to 64.4%. The peptides, in fact, constituted an extensive two-dimensional array of isomers exhibiting heterogeneity in degree and location of hydroxyproline residues. A total of 3433 peptides, scores>36 (p<0.01), constituting 94% of the triple helix region of collagen alpha-1(I) provided a census of proline hydroxylation levels defined as the rate of site occupancy for each peptide isomer (r) and the total site occupancy for each proline residue (t). MS/MS and MS/MS/MS analysis, by MALDI-QIT-TOF MS, was used to corroborate site-specific proline hydroxylation of the original data. In addition, iTRAQ data for each collagen isoform in each of 10 patients (grouped by disease) was determined and indicated an increase in fibrillar collagens in invasive carcinoma but little change in fibroadenoma or DCIS.

Still unhealthy 2009: building community research to identify risk factors and health outcomes in childhood obesity.

The goal of the this study was to track and assess children's health status in Nevada and build relationships between researchers and school districts through the collection of mutually beneficial health data at a local level. All elementary schools in Nevada were sent a health survey for parents of kindergarten students to complete. A total of 3,628 surveys were received with usable height and weight needed to calculate Body Mass Index (BMI). African American and Hispanic children had significantly higher BMI scores compared to Caucasian and Asian/Pacific Islander children, regardless of income. Children who had diabetes or mental health concerns also had significantly higher mean BMIs compared to children without these health concerns. Overall staff within the school districts felt that this surveillance system should be continued as data from this study provided important information subsequently used to guide programming and when applying for grants. Our children's welfare depends on community collaboration to create and implement data-driven initiatives to combat childhood obesity.

Characteristics of internationally educated nurses in the United States: an update from the 2004 National Sample Survey of Registered Nurses.

Internationally educated nurses (IENs) have become an integral part of the U.S. registered nurse workforce. To understand the U.S. RN workforce and conduct nurse workforce planning, it is fundamental to know the who, what, and where about IENs. Analysis of the 2004 National Sample Survey of Registered Nurses revealed demographic and employment characteristics of IENs practicing in the United States. The results can help employers, recruiters, and policymakers stay abreast of the changing profile of IENs in order to make informed decisions regarding the recruitment of lENs, and U.S. workforce planning and policy. More importantly, systematic actions such as developing tailored transitional programs should be implemented to better integrate and retain IENs who are playing an increasingly important role of caring for Americans.

Glycation pattern of peptides condensed with maltose, lactose and glucose determined by ultraviolet matrix-assisted laser desorption/ionization tandem mass spectrometry.

Protein glycation is the non-enzymatic condensation of sugars with proteins. Although commonly occurring in both the therapeutic and food/beverage industries, protein glycation has not been the focus of many proteomic investigations. This study aims to establish a reliable mass spectrometric method for screening large tandem mass spectrometric (MSMS) datasets for protein glycation with glucose, lactose and maltose. Control experiments using a standard peptide containing a single glycation site led to the discovery of characteristic neutral loss fragmentation patterns in MSMS analysis for glucose, lactose and maltose condensed with peptides. Valid in both tandem time-of-flight (TOFTOF) and quadrupole ion trap time-of-flight matrix-assisted laser desorption/ionization (QIT TOF MALDI) mass spectrometers, these neutral loss signatures were then applied to elucidation of modified peptides from a complex human serum albumin (HSA) digest glycated with each of the proposed sugars. Screening of these large datasets was made possible by specifically designed software solutions that enable the input of detailed user-defined post-translational modifications that are not included in the universally available databases such as Unimod.

MS characterization of apheresis samples from rheumatoid arthritis patients for the improvement of immunoadsorption therapy - a pilot study.

Identification of proteins from apheresis samples was performed by both SDS-PAGE and 2-D gel separation of eluted proteins from staphylococcal protein A-based immunoadsorption columns (Prosorba(®) ) followed by MS peptide mass fingerprinting and MS/MS peptide sequencing on a MALDI QIT TOF mass spectrometer. MS/MS peptide sequencing was performed in conjunction with a micro reversed phase HPLC configured with an online MALDI plate-spotting device. Apheresis treatment had been performed in three patients with longstanding therapy refractory rheumatoid arthritis. 2-D gels displayed ca. 500 spots representing proteins that were eluted from the Prosorba(®) columns. From 54 gels, a total of 1256 protein spots had been picked and yielded in the identification of 56 non-redundant proteins without counting isoforms. Proteins from the eluates belong to five major groups comprising (i) immunoglobulins (IgG, IgA, IgM heavy and light chains; about 40% of the spots), (ii) proteins involved in coagulation, (iii) HDL/LDL-associated proteins, (iv) proteins from the complement system, and (v) acute phase proteins. MS analysis showed that the full-length C3 complement protein had been cleaved upon complement activation, presumably on the column, such that the anaphylatoxin C3a was produced and released during therapy. Our results are consistent with clinical observations on both patient responses to therapy and reported adverse events. For the first time, direct molecular information has become available to support mechanistic reasoning for the principle of function of staphylococcal protein A-based immunoadsorption therapy and for the explanation of adverse events. According to our results, removal and/or modulation of immune complexes together with complement activation can be regarded as the major events that are taking place during Prosorba(®) therapy. In order to avoid complement activation and induction of an inflammatory cascade, we suggest the prevention of C3a anaphylatoxin-related reactions during immunoadsorption therapy.

Guanidino labeling derivatization strategy for global characterization of peptide mixtures by liquid chromatography matrix-assisted laser desorption/ionization mass spectrometry.

Guanidination performed with isotopic isoforms of O-methylisourea was used in combination with reversed-phase liquid chromatography (LC) matrix-assisted laser desorption/ionization to characterize, both qualitatively and quantitatively, protein mixtures. Synthesis of (13)C- and (15)N(2)-labeled O-methylisourea sulfate produces a molecule that is 3 Da heavier than the light isotopic variant. Protein mixtures containing identical components in different concentration are pooled together following parallel derivatization. Relative quantification of protein mixtures is achieved by mass spectrometry. A difference of 3 Da allows negligible interference between the two isotopic clusters for quantification of peptides up to 1400 Da. Under these conditions, the chromatographic resolution achieved allows separation of different pairs of derivatized peptides without altering the retention time of structurally identical isotopic isoforms. Concomitant isolation of both chemically modified precursors is followed by tandem mass analysis. Activation of the ions via collisions with an inert gas produces isotopically derivatized fragment ions, which appear as doublets in the product ion spectrum. Since the modification occurs on the C-terminal lysine, ions incorporating the guanidino moiety on the C-terminus can be distinguished from those containing the original unmodified peptide N-terminus. Knowledge of the location of the proton can be beneficial to data interpretation and peptide sequencing.