Asian Science Citation Index is committed to provide an authoritative, trusted and significant information by the coverage of the most important and influential journals to meet the needs of the global scientific community.  
ASCI Database
308-Lasani Town,
Sargodha Road,
Faisalabad, Pakistan
Fax: +92-41-8815544
Contact Via Web
Suggest a Journal
 
Articles by C. H Huang
Total Records ( 4 ) for C. H Huang
  Y. P Tsai , M. H Yang , C. H Huang , S. Y Chang , P. M Chen , C. J Liu , S. C Teng and K. J. Wu
 

Heat shock protein 60 (HSP60) plays an essential role in assisting many newly synthesized proteins to reach their native forms. Increased HSP60 expression is observed in different types of human cancers with metastasis (e.g. pancreatic cancer and large bowel carcinoma). However, the role of HSP60 in metastasis remains little known. Aberrant activation of β-catenin plays a key role in tumorigenesis and metastasis. Here, we show that overexpression of HSP60 induces metastatic phenotypes in vitro and in vivo. HSP60 interacts with β-catenin, increases β-catenin protein levels through the apical domain and enhances its transcriptional activity. Short-interference RNA-mediated repression of β-catenin reverts metastatic activity caused by HSP60 overexpression. Proteosomal activity is not required for the induction of β-catenin by HSP60. Coexpression of HSP60 and nuclear β-catenin predicts a worse prognosis of metastatic head and neck cancer patients. These results implicate a novel role of HSP60 in metastasis.

  H. Y Lin , K. W Chong , J. H Hsu , H. C Yu , C. C Shih , C. H Huang , S. J Lin , C. H Chen , C. C Chiang , H. J Ho , P. C Lee , C. H Kao , K. H Cheng , C Hsueh and D. M. Niu
 

Background— Fabry disease is a treatable lysosomal storage disorder, which is often misdiagnosed or belatedly diagnosed.

Methods and Results— To determine the disease incidence in the Taiwan Chinese population, a Fabry disease newborn screening study was initiated. A total of 110 027 newborns were screened by assaying the -galactosidase A (-Gal A) activity using dry blood spots. Low plasma -Gal A activity and presence of a Fabry mutation was demonstrated in 45 neonates (3 females). Eight different mutations were identified, including 3 known missense mutations (R112H, A143T, and R356W), 4 novel missense mutations (G104V, M296L, G360C, and K391T), and one known intronic mutation (IVS4+919G->A). The IVS4+919G->A mutation was most common (82% of patients). A total of 20 maternal grandparents of infants harboring this intronic mutation were evaluated by echocardiography, mutation analysis and -Gal A activity assay. The intronic mutation was found in 9 grandfathers and 11 grandmothers. Of these grandparents, 3 grandfathers (33%) but none of the grandmothers had hypertrophic cardiomyopathy. Additionally, 16 males who had been diagnosed with idiopathic hypertrophic cardiomyopathy were screened by mutation analysis and -Gal A activity; 4 (25%) showed deficient plasma -Gal A activity in combination with the intronic mutation.

Conclusion— We found an unexpected high prevalence of the cardiac variant Fabry mutation IVS4+919G->A among both newborns (1 in 1600 males) and patients with idiopathic hypertrophic cardiomyopathy in the Taiwan Chinese population. The early identification of undiagnosed patients allows timely therapeutic intervention providing a better clinical outcome.

  C. H Huang , I. L Lee , I. J Yeh , J. H Liao , C. L Ni , S. H Wu and S. H. Chiou
 

Helicobacter pylori is a spiral Gram-negative microaerophilic bacterium. It is unique and distinctive among various bacterial pathogens for its ability to persist in the extreme acidic environment of human stomachs. To address and identify changes in the proteome of H. pylori in response to low pH, we have used a proteomic approach to study the protein expression of H. pylori under neutral (pH 7) and acidic (pH 5) conditions. Global protein-expression profiles of H. pylori under acid stress were analysed by two-dimensional polyacrylamide gel electrophoresis (2-DE) followed by liquid chromatography (LC)-nanoESI-mass spectrometry (MS)/MS and bioinformatics database analysis. Among the proteins differentially expressed under acidic condition, a non-heme iron-containing ferritin of H. pylori (HP-ferritin) was found to be consistently upregulated at pH 5 as compared to pH 7. It was also found that HP-ferritin can switch from an iron-storage protein with ferroxidase activity to a DNA-binding/protection function under in vitro conditions upon exposure to acidic environment. Prokaryotic ferritins, such as non-heme iron-binding HP-ferritin with dual functionality reported herein, may play a significant urease-independent role in the acid adaptation of H. pylori under physiological conditions in vivo.

  C. H Huang , M. H Chuang , Y. H Wu , W. C Chuang , P. J Jhuang and S. H. Chiou
 

Alkylhydroperoxide reductase (AhpC) is an abundant and important antioxidant protein present in Helicobacter pylori (HP), a spiral Gram-negative microaerophilic bacterium. By sequence alignment and structure comparison, HP-AhpC was found to be more homologous to human peroxiredoxins (hPrx) than to other eubacterial AhpC proteins. Similar to hPrxI, native HP-AhpC existed as a dimer of single subunit, comprising -helix and β-sheet domains with low surface hydrophobicity. AhpC can form high-molecular-weight (HMW) aggregates ranging from 700 to higher than 2,000 kDa under oxidative stress, possessing chaperone activity in the presence of thioredoxin (Trx). Further analysis of peroxide-reductase activities showed that HP-AhpC was more resistant to H2O2 than hPrxI. However, the mechanism of enzyme inactivation to H2O2 appeared to be similar for both HP-AhpC and hPrxI as revealed by native gel electrophoresis followed by proteomic identification using two-dimensional gel electrophoresis (2-DE) and LC-MS/MS. In contrast to T90D-hPrxI mutant with chaperone activity, site-specific mutant T87D-HP-AhpC did not form HMW chaperone complexes. The comparison of these two evolutionarily distant and yet functionally related enzymes may shed some light on the mechanism(s) underlying the evolution and development of the dual functionality in HP-AhpC and hPrxI with similar protein structure.

 
 
 
Copyright   |   Desclaimer   |    Privacy Policy   |   Browsers   |   Accessibility