MF2426

Melissa Webb and Karen Pesaresi Penner, Food irradiation, Kansas State University, February 2000

Early Changes in Hepatitis C Virus (HCV) RNA Levels Predict Response to Interferon Treatment in Non-Cirrhotic HCV Patients

The role of hepatitis C virus (HCV) RNA quantification in determining ideal interferon (IFN) treatment of noncirrhotic HCV liver disease is uncertain. The specific aim of this study was to determine whether measurement of baseline HCV RNA or changes in HCV RNA levels ( HCV RNA) early during therapy predict response to IFN in noncirrhotic HCV patients

Early Changes in Hepatitis C Virus (HCV) RNA Levels Predict Response to Interferon Treatment in Non-Cirrhotic HCV Patients

The role of hepatitis C virus (HCV) RNA quantification in determining ideal interferon (IFN) treatment of noncirrhotic HCV liver disease is uncertain. The specific aim of this study was to determine whether measurement of baseline HCV RNA or changes in HCV RNA levels ( HCV RNA) early during therapy predict response to IFN in noncirrhotic HCV patients

Potential-modulated Electrocapacitive Properties of Soft Microstructured Polypyrrole

Microstructured materials are becoming important for high performance electrochemical device especially for energy storage due to their advantageous diffusion and flux properties. Utilizing a rationally designed hollow structured polypyrrole microparticles (PPyMPs) with controllable wall thicknesses of -110 to 340 nm, we observed a significant morphological effect on electrocapacitive kinetics of the PPyMPs modulated by the voltammetric potential window and scan rate. The thinhollow architecture of PPyMPs revealed significant enhancement of charge storage performance (up to 447%), high retention at high scan rate and faster charge/dis-charge kinetics compared to the thick-hollow PPyMPs due to the larger accessible surface area and decrease of diffusion length. These findings demonstrated the electrocapacitive kinetics performance of microstructured soft materials related to morphological effect modulated by operational conditions. Our study provides new insight on electrochemistry of soft electrode materials with controlled nanostructured morphology for understanding the mechanism of charge insertion and mass diffusion for the future development of high performance porous electrode material.Funding Agencies|Graduate School Prince of Songkla University; Higher Education Research Promotion; National Research University Project of Thailand (NRU); Office of higher Education Commission; Office of higher Education Commission; the Center of Excellence for Innovation in Chemistry (PERCH-CIC), Commission on Higher Education, Ministry of Education, Thailand</p

Identification of binding partners interacting with the α1-N-propeptide of type V collagen

The predominant form of type V collagen is the [α1(V)]₂α2(V) heterotrimer. Mutations in COL5A1 or COL5A2, encoding respectively the α1(V)- and α2(V)-collagen chain, cause classic EDS (Ehlers-Danlos syndrome), a heritable connective tissue disorder, characterized by fragile hyperextensible skin and joint hypermobility. Approximately half of the classic EDS cases remain unexplained. Type V collagen controls collagen fibrillogenesis through its conserved α1(V)-N-propeptide domain. To gain an insight into the role of this domain, a yeast two-hybrid screen among proteins expressed in human dermal fibroblasts was performed utilizing the N-propeptide as a bait. We identified 12 interacting proteins, including extracellular matrix proteins and proteins involved in collagen biosynthesis. Eleven interactions were confirmed by surface plasmon resonance and/or co-immunoprecipitation: α1(I)- and α2(I)-collagen chains, α1(VI)-, α2(VI)- and α3(VI)-collagen chains, tenascin-C, fibronectin, PCPE-1 (procollagen C-proteinase enhancer-1), TIMP-1 (tissue inhibitor of metalloproteinases-1), MMP-2 (matrix metalloproteinase 2) and TGF-β1 (transforming growth factor β1). Solid-phase binding assays confirmed the involvement of the α1(V)-N-propeptide in the interaction between native type V collagen and type VI collagen, suggesting a bridging function of this protein complex in the cell-matrix environment. Enzymatic studies showed that processing of the α1(V)-N-propeptide by BMP-1 (bone morphogenetic protein 1)/procollagen C-proteinase is enhanced by PCPE-1. These interactions are likely to be involved in extracellular matrix homoeostasis and their disruption could explain the pathogenetic mechanism in unresolved classic EDS cases