Sodium oligomannate disrupts the adherence of Rib bacteria to gut epithelia to block SAA-triggered Th1 inflammation in 5XFAD transgenic mice.

Sodium oligomannate (GV-971), an oligosaccharide drug approved in China for treating mild-to-moderate Alzheimer's disease (AD), was previously found to recondition the gut microbiota and limit altered peripheral Th1 immunity in AD transgenic mice. As a follow-up study, we here made advances by pinpointing a Lactobacillus murinus (L.m.

[Clinical Significance of Mean Platelet Volume Determination in Multiple Myeloma].

Objective: To investigate the clinical significance of mean platelet volume(MPV) in patients with multiple myeloma(MM).

Methods: The clinical data of 198 patients with MM admitted in our hospital from March 2008 to March 2015 were collected and analyzed. The clinical data included the Ig type, hemoglobin level, platelet count, creatinine, calciumion albumin, β2-MG, LDH, plasmocytes in bone marrow, MPV, complications such as diabetes, a history of venous thromboembolism (VTE) and arterial events such as coronary artery disease, cerebrovascular disease, thrombosis and blood clotting.

Stereocomplex micelle efficiently transports Doxorubicin for enhanced lymphoma suppression in vivo.

The application of Doxorubicin (DOX) in the chemotherapy for lymphoma is seriously hampered by the side effects of DOX, especially the cardiotoxicity and nephrotoxicity. Nanoscale micelle as a promising drug delivery system has gained more and more interest in malignancy chemotherapy. In this study, we successfully fabricated DOX-loaded stereocomplex micelle (SCM/DOX) from the equimolar mixture of the enantiomeric four-armed poly(ethylene glycol)-polylactide (PDM and PLM) copolymers.

[Efficacy and safety of anagrelide in treatment of essential thrombocythemia: multicenter, randomized controlled clinical trial].

Objective: To evaluate the efficacy and safety of anagrelide in essential thrombocythemia (ET).

Methods: Patients who diagnosed as ET according to the World Health Organization classification were enrolled. Each patient was assigned to take anagrelide hydrochloride capsule or hydroxyurea tablet by random 1∶1 ratio.

ELECTRON DETACHMENT DISSOCIATION AND INFRARED MULTIPHOTON DISSOCIATION OF HEPARIN TETRASACCHARIDES.

Heparin glycosaminoglycans (GAGs) present the most difficult glycoform for analytical characterization due to high levels of sulfation and structural heterogeneity. Recent contamination of the clinical heparin supply and subsequent fatalities has highlighted the need for sensitive methodologies of analysis. In the last decade, tandem mass spectrometry has been increasingly applied for the analysis of GAGs, but developments in the characterization of highly sulfated compounds have been minimal due to the low number of cross-ring cleavages generated by threshold ion activation by collisional induced dissociation (CID).

Structural characterization of heparins from different commercial sources.

Seven commercial heparin active pharmaceutical ingredients and one commercial low molecular weight from different manufacturers were characterized with a view profiling their physicochemical properties. All heparins had similar molecular weight properties as determined by polyacrylamide gel electrophoresis (M(N), 10-11 kDa; M(W), 13-14 kDa; polydispersity (PD), 1.3-1.

Asparagine 405 of heparin lyase II prevents the cleavage of glycosidic linkages proximate to a 3-O-sulfoglucosamine residue.

Heparin and heparan sulfate contain a rare 3-O-sulfoglucosamine residue critical for anticoagulation and virus recognition, respectively. The glycosidic linkage proximate to this 3-O-sulfoglucosamine is resistant to cleavage by all heparin lyases (Heps). HepII has a broad specificity.

Negative electron transfer dissociation Fourier transform mass spectrometry of glycosaminoglycan carbohydrates.

Electron transfer through gas phase ion-ion reactions has led to the widespread application of electron- based techniques once only capable in ion trapping mass spectrometers. Although any mass analyzer can in theory be coupled to an ion-ion reaction device (typically a 3-D ion trap), some systems of interest exceed the capabilities of most mass spectrometers. This case is particularly true in the structural characterization of glycosaminoglycan (GAG) oligosaccharides.

Binding affinities of vascular endothelial growth factor (VEGF) for heparin-derived oligosaccharides.

Heparin and HS (heparan sulfate) exert their wide range of biological activities by interacting with extracellular protein ligands. Among these important protein ligands are various angiogenic growth factors and cytokines. HS binding to VEGF (vascular endothelial growth factor) regulates multiple aspects of vascular development and function through its specific interaction with HS.

Heparin mapping using heparin lyases and the generation of a novel low molecular weight heparin.

Seven pharmaceutical heparins were investigated by oligosaccharide mapping by digestion with heparin lyase 1, 2, or 3, followed by high performance liquid chromatography analysis. The structure of one of the prepared mapping standards, ΔUA-Gal-Gal-Xyl-O-CH(2)CONHCH(2)COOH (where ΔUA is 4-deoxy-α-l-threo-hex-4-eno-pyranosyluronic acid, Gal is β-d-galactpyranose, and Xyl is β-d-xylopyranose) released from the linkage region using either heparin lyase 2 or heparin lyase 3 digestion, is reported for the first time. A size-dependent susceptibility of site cleaved by heparin lyase 3 was also observed.

Mass balance analysis of contaminated heparin product.

A quantitative analysis of a recalled contaminated lot of heparin sodium injection U.S. Pharmacopeia (USP) was undertaken in response to the controversy regarding the exact nature of the contaminant involved in the heparin (HP) crisis.

Heparinase 1 selectivity for the 3,6-di-O-sulfo-2-deoxy-2-sulfamido-alpha-D-glucopyranose (1,4) 2-O-sulfo-alpha-L-idopyranosyluronic acid (GlcNS3S6S-IdoA2S) linkages.

Porcine intestinal mucosa heparin was partially depolymerized by recombinant heparinase 1 (heparin lyase 1, originating from Flavobacterium heparinum and expressed in Escherichia coli) and then fractionated, leading to the isolation of 22 homogeneous oligosaccharides with sizes ranging from disaccharide to hexadecasaccharide. The purity of these oligosaccharides was determined by gel electrophoresis, strong anion exchange and reversed-phase ion-pairing high-performance liquid chromatography. The molecular mass of oligosaccharides was determined using electrospray ionization-mass spectrometry and their structures were elucidated using one- and two-dimensional nuclear magnetic resonance spectroscopy at 600 MHz.

Catalytic mechanism of heparinase II investigated by site-directed mutagenesis and the crystal structure with its substrate.

Heparinase II (HepII) is an 85-kDa dimeric enzyme that depolymerizes both heparin and heparan sulfate glycosaminoglycans through a beta-elimination mechanism. Recently, we determined the crystal structure of HepII from Pedobacter heparinus (previously known as Flavobacterium heparinum) in complex with a heparin disaccharide product, and identified the location of its active site. Here we present the structure of HepII complexed with a heparan sulfate disaccharide product, proving that the same binding/active site is responsible for the degradation of both uronic acid epimers containing substrates.

[The comparison of CD4(+);CD25(high); Foxp3(+); regulatory T cells between neonatal cord blood and adult peripheral blood.].

Aim: To quantify the proportion of CD4(+);CD25(high); Foxp3(+); regulatory T cells (Treg) in neonatal cord blood and adult peripheral blood, and to explore the clinical significance of Treg in neonatal cord blood.

Methods: The percentage of CD4(+); T cells, and ratio of CD4(+);CD25(+);/CD4(+); and CD4(+);CD25(high);/CD4(+);T cells in mononuclear cells in 30 neonatal cord blood and 27 adult peripheral blood were examinea with flow cytometry (FCM). The expression of Foxp3(+); in CD4(+);CD25(+); and CD4(+);CD25(high); T cells was examined with FCM and RT-PCR, respectively RT-PCR.

Structural snapshots of heparin depolymerization by heparin lyase I.

Heparin lyase I (heparinase I) specifically depolymerizes heparin, cleaving the glycosidic linkage next to iduronic acid. Here, we show the crystal structures of heparinase I from Bacteroides thetaiotaomicron at various stages of the reaction with heparin oligosaccharides before and just after cleavage and product disaccharide. The heparinase I structure is comprised of a beta-jellyroll domain harboring a long and deep substrate binding groove and an unusual thumb-resembling extension.