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Articles 1 - 3 of 3
Full-Text Articles in Medicine and Health Sciences
Distinct Gene Expression Profiles In Different B-Cell Compartments In Human Peripheral Lymphoid Organs., Yulei Shen, Javeed Iqbal, Li Xiao, Ryan C. Lynch, Andreas Rosenwald, Louis M. Staudt, Simon Sherman, Karen Dybkaer, Guimei Zhou, James D. Eudy, Jan Delabie, Timothy W. Mckeithan, Wing C. Chan
Distinct Gene Expression Profiles In Different B-Cell Compartments In Human Peripheral Lymphoid Organs., Yulei Shen, Javeed Iqbal, Li Xiao, Ryan C. Lynch, Andreas Rosenwald, Louis M. Staudt, Simon Sherman, Karen Dybkaer, Guimei Zhou, James D. Eudy, Jan Delabie, Timothy W. Mckeithan, Wing C. Chan
Journal Articles: Eppley Institute
BACKGROUND: There are three major B-cell compartments in peripheral lymphoid organs: the germinal center (GC), the mantle zone (MNZ) and the marginal zone (MGZ). Unique sets of B-cells reside in these compartments, and they have specific functional roles in humoral immune response. MNZ B cells are naive cells in a quiescent state and may participate in GC reactions upon proper stimulation. The adult splenic MGZ contains mostly memory B cells and is also known to provide a rapid response to particulate antigens. The GC B-cells proliferate rapidly and undergo selection and affinity maturation. The B-cell maturational process is accompanied by …
Molecular Dynamics Simulations Of The O-Glycosylated 21-Residue Muc1 Peptides, A. Rubinstein, L. Kinarsky, S. Sherman
Molecular Dynamics Simulations Of The O-Glycosylated 21-Residue Muc1 Peptides, A. Rubinstein, L. Kinarsky, S. Sherman
Journal Articles: Eppley Institute
The conformational propensities of the 21-residue peptide and its Oglycosylated analogs were studied by molecular dynamics (MD) simulations. This polypeptide motif comprises the tandem repeat of the human mucin (MUC1) protein core that is differently glycosylated in normal and cancer cells. To evaluate the structural effects of O-glycosylation on the polypeptide backbone, conformations of the nonglycosylated peptide and its glycosylated analogs were monitored during the 1 ns MD simulations. Radius gyration for whole peptide and its fragments, as well as root-mean-square-deviation between coordinate sets of the backbone atoms of starting structures and generated structures, were calculated. It was shown that …
Nmr-Based Structural Studies Of The Glycosylated Muc1 Tandem Repeat Peptide, G. Suryanarayanan, P. A. Keifer, G. Wang, L. Kinarsky, M. A. Hollingsworth, S. Sherman
Nmr-Based Structural Studies Of The Glycosylated Muc1 Tandem Repeat Peptide, G. Suryanarayanan, P. A. Keifer, G. Wang, L. Kinarsky, M. A. Hollingsworth, S. Sherman
Journal Articles: Eppley Institute
MUC1 is a glycoprotein that plays an important role in cancer pathogenesis. In order to study the effect of glycosylation on the conformational propensities of the tandem repeat domain of MUC1, we have determined the structure of the MUC1 tandem repeat peptide AHGVTSAPDTRPAPGSTAPP, O-glycosylated with the trisaccharide (α-Glc-1,4-β-Glc-1,4-α-GalNAc-) at Thr5. This glycopeptide was synthesized to model a heavily Oglycosylated threonine residue in the tandem repeat domain. The NMR experiments used in this study included TOCSY, NOESY, ROESY, DQF-COSY, HSQC and 1D NMR. The peak volumes determined using the program SPARKY were converted into distance constraints using the program CALIBA. The …