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Articles by B Yang
Total Records ( 2 ) for B Yang
  Q Wang , J. L. C Lin , B. E Reinking , H. Z Feng , F. C Chan , C. I Lin , J. P Jin , E. A Gustafson Wagner , T. D Scholz , B Yang and J. J. C. Lin
 

Rationale: The Xin repeat–containing proteins mXin and mXinβ localize to the intercalated disc of mouse heart and are implicated in cardiac development and function. The mXin directly interacts with β-catenin, p120-catenin, and actin filaments. Ablation of mXin results in adult late-onset cardiomyopathy with conduction defects. An upregulation of the mXinβ in mXin-deficient hearts suggests a partial compensation.

Objective: The essential roles of mXinβ in cardiac development and intercalated disc maturation were investigated.

Methods and Results: Ablation of mXinβ led to abnormal heart shape, ventricular septal defects, severe growth retardation, and postnatal lethality with no upregulation of the mXin. Postnatal upregulation of mXinβ in wild-type hearts, as well as altered apoptosis and proliferation in mXinβ-null hearts, suggests that mXinβ is required for postnatal heart remodeling. The mXinβ-null hearts exhibited a misorganized myocardium as detected by histological and electron microscopic studies and an impaired diastolic function, as suggested by echocardiography and a delay in switching off the slow skeletal troponin I. Loss of mXinβ resulted in the failure of forming mature intercalated discs and the mislocalization of mXin and N-cadherin. The mXinβ-null hearts showed upregulation of active Stat3 (signal transducer and activator of transcription 3) and downregulation of the activities of Rac1, insulin-like growth factor 1 receptor, protein kinase B, and extracellular signal-regulated kinases 1 and 2.

Conclusions: These findings identify not only an essential role of mXinβ in the intercalated disc maturation but also mechanisms of mXinβ modulating N-cadherin–mediated adhesion signaling and its crosstalk signaling for postnatal heart growth and animal survival.

  Z Xiao , W Zhao , B Yang , Z Zhang , H Guan and R. J. Linhardt
 

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. Five of the characterized oligosaccharides represent new compounds. The most prominent oligosaccharide comprises the common repeating unit of heparin, UA2S-[-GlcNS6S-IdoA2S-]n-GlcNS6S, where UA is 4-deoxy--l-threo-hex-4-eno-pyranosyluronic acid, GlcN is 2-deoxy-2-amino-d-glucopyranose, IdoA is l-idopyranosyluronic acid, S is sulfate and = 0–7. A second prominent heparin oligosaccharide motif corresponds to UA2S-[GlcNS6S-IdoA2S]n-GlcNS6S-IdoA-GlcNAc6S-GlcA-GlcNS3S6S (where n = 0–5 and GlcA is d-glucopyranosyluronic acid), a fragment of the antithrombin III binding site in heparin. The prominence of this second set of oligosaccharides and the absence of intact antithrombin III binding sites suggest that the -GlcNS3S6S-IdoA2S- linkage is particularly susceptible to heparinase 1.

 
 
 
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