Volume and function changes of left atrium and left ventricle in patients with ejection fraction preserved heart failure measured by a three dimensional dynamic heart model.

The accurate diagnosis of HFpEF is still challenging and controversial. In this study, we used 3D-DHM technology to compare the differences of cardiac structure and function between HFpEF patients and healthy controls, as well as the differences of two-dimensional and three-dimensional cardiac function in HFpEF patients. Echocardiography with 3D-DHM and conventional two-dimensional (2D) methods were applied to measure the volume and function parameters of left atrium and ventricle of patients with HFpEF and healthy controls.

Measuring of strain parameters reflects changes of right ventricular function before and after thrombolytic therapy in patients with acute pulmonary embolism.

Strain parameters on speckle tracking echocardiography (STE) have been proposed as effective indexes for evaluating right ventricular (RV) function. This pilot study investigated the role of STE-derived strain parameters in assessing global and regional RV myocardial mechanical changes in patients with acute pulmonary embolism (PE) before and after thrombolytic therapy. In this case-control study, a total of 73 PE patients, 34 with pulmonary hypertension (PH) and 39 without PH, who underwent thrombolytic therapy were included.

Efficient production and characterization of soluble active human β-1,2-N-acetylglucosaminyltransferase II in bacteria.

In humans, almost all the cell surface and secreted glycoproteins are modified with complex-type N-glycans. Thus, it is essential to obtain complex-type N-glycans to fully understand the biological properties of glycoproteins. Here, human β-1,2-N-acetylglucosaminyltransferase II (hGnT-II), a Golgi-localized enzyme integral to complex-type N-glycan biosynthesis, was cloned as a truncated transmembrane form (GnT-II-ΔTM) and heterologously overexpressed in Escherichia coli.

Nanomolar β-glucosidase and β-galactosidase inhibition by enantiomeric α-1-C-alkyl-1,4-dideoxy-1,4-imino-arabinitol derivatives.

A series of α-1-C-alkyl DAB (1,4-dideoxy-1,4-imino-d-arabinitol) and LAB (1,4-dideoxy-1,4-imino-l-arabinitol) derivatives with aryl substituents have been designed as analogues of broussonetine W (12), and assayed as glycosidase inhibitors. While the inhibition spectrum of α-1-C-alkyl DAB derivative 16 showed a good correlation to that of broussonetine W (12), introduction of substituents on the terminal aryl (17a-f) or hydroxyl groups at C-1' position of the alkyl chains (18a-e) decreased their α-glucosidase inhibitions but greatly improved their inhibitions of bovine liver β-glucosidase and β-galactosidase. Furthermore, epimerization of C-1' configurations of compounds 18a-e clearly lowered their inhibition potency of bovine liver β-glucosidase and β-galactosidase.

Introduction of -alkyl branches to L-iminosugars changes their active site binding orientation.

L--Deoxynojirimycin (L--DNJ) itself showed no affinity for human lysosomal acid α-glucosidase (GAA), whereas 5--methyl-L--DNJ showed a strong affinity for GAA, comparable to the glucose analog DNJ, with a value of 0.060 μM. This excellent affinity for GAA and enzyme stabilization was observed only when methyl and ethyl groups were introduced.

5--Branched Deoxynojirimycin: Strategy for Designing a 1-Deoxynojirimycin-Based Pharmacological Chaperone with a Nanomolar Affinity for Pompe Disease.

In recent years, the function of pharmacological chaperones as a "thermodynamic stabilizer" has been attracting attention in combination therapy. The coadministration of a pharmacological chaperone and recombinant human acid α-glucosidase (rhGAA) leads to improved stability and maturation by binding to the folded state of the rhGAA and thereby promotes enzyme delivery. This study provides the first example of a strategy to design a high-affinity ligand toward lysosomal acid α-glucosidase (GAA) focusing on alkyl branches on 1-deoxynojirimycin (DNJ); 5--heptyl-DNJ produced a nanomolar affinity for GAA with a value of 0.

Two novel chiral tetranucleate copper-based complexes: syntheses, crystal structures, inhibition of angiogenesis and the growth of human breast cancer and .

The single crystals of two novel chiral tetranucleate copper(II)-based complexes (TNCu-A and TNCu-B) containing -methioninol-derived Schiff-bases were obtained. Their single structures were characterized by X-ray single crystal diffraction, infrared (IR) rays, elemental analysis, and liquid chromatography-mass spectrometry analysis. TNCu-A can effectively inhibit human umbilical vein endothelial cells (HUVECs) to form a tubular structure and it induces apoptosis of human triple-negative breast cancer MDA-MB-231 cells and HUVECs in a mitochondria dependent manner.

Synthesis and glycosidase inhibition of 5-C-alkyl-DNJ and 5-C-alkyl-l-ido-DNJ derivatives.

5-C-Alkyl-DNJ and 5-C-alkyl-l-ido-DNJ derivatives have been designed and synthesized efficiently from an l-sorbose-derived cyclic nitrone. The DNJ and l-ido-DNJ derivatives with C-5 alkyl chains ranging from methyl to dodecyl were assayed against various glycosidases to study the effect of chain length on enzyme inhibition. Glycosidase inhibition study of DNJ derivatives showed potent and selective inhibitions of α-glucosidase; DNJ derivatives with methyl, pentyl to octyl, undecyl and dodecyl as C-5 branched chains showed significantly improved rat intestinal maltase inhibition.

Chemo-enzymatic synthesis of the ALG1-CDG biomarker and evaluation of its immunogenicity.

Congenital disorders of glycosylation (CDG) are a growing group diseases that result from defects in genes involved in glycan biosynthesis pathways. One tetrasaccharide, i.e.

Reconstitution of the lipid-linked oligosaccharide pathway for assembly of high-mannose N-glycans.

The asparagine (N)-linked Man9GlcNAc2 is required for glycoprotein folding and secretion. Understanding how its structure contributes to these functions has been stymied by our inability to produce this glycan as a homogenous structure of sufficient quantities for study. Here, we report the high yield chemoenzymatic synthesis of Man9GlcNAc2 and its biosynthetic intermediates by reconstituting the eukaryotic lipid-linked oligosaccharide (LLO) pathway.

Situational Analysis of Low-density Lipoprotein Cholesterol Control and the Use of Statin Therapy in Diabetes Patients Treated in Community Hospitals in Nanjing, China.

Background: Comprehensive management of diabetes should include management of its comorbid conditions, especially cardiovascular complications, which are the leading cause of morbidity and mortality among patients with diabetes. Dyslipidemia is a comorbid condition of diabetes and a risk factor for cardiovascular complications. Therefore, lipid level management is a key of managing patients with diabetes successfully.

[Prokaryotic expression of the extracellular region of human CD1d and preparation of its polyclonal antibody].

Aim: To explore the prokaryotic expression of the extracellular region of human CD1d (hCD1d) and prepare its polyclonal antibody.

Methods: The gene encoding the extracellular region of hCD1d was amplified by PCR and cloned into prokaryotic expression vector pET28, then expressed in E.coli BL21 (DE3) with IPTG induction.

[Preparation and characterization of the rabbit polyclonal antibody against the alpha3 domain of human CD1d].

Aim: To prepare the rabbit antibody against the alpha3 domain of the human CD1d (hCD1d-alpha3).

Methods: The gene fragment coding for hCD1d-alpha3 was amplified by PCR and cloned into prokaryotic expression vector pET28, then expressed in E.coli BL21(DE3).

[Prokaryotic expression of human mast cell chymase gene and preparation of its polyclonal antibody].

Aim: To express the human mast cell chymase cDNA in E.coli and prepare the antibody against human mast cell chymase with recombinant chymase.

Methods: The human mast cell chymase cDNA was cloned by RT-PCR.

[Preparation and characterization of rabbit antibody against human mast cell carboxypeptidase].

Aim: To prepare antibody against human mast cell carboxypeptidase (hMC-CP) by using recombinant hMC-CP expressed in E.coli, and to characterize the antibody.

Methods: hMC-CP was expressed in E.