Epigenetic regulation of HYAL-1 hyaluronidase expression. identification of HYAL-1 promoter.

HYAL-1 (hyaluronoglucosaminidase-1) belongs to the hyaluronidase family of enzymes that degrade hyaluronic acid. HYAL-1 is a marker for cancer diagnosis and a molecular determinant of tumor growth, invasion, and angiogenesis. The regulation of HYAL-1 expression is unknown.

Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta.

Chemokines (chemotactic cytokines) comprise a large family of proteins that recruit and activate leukocytes, giving chemokines a major role in both immune response and inflammation-related diseases. The poxvirus-encoded viral CC chemokine inhibitor (vCCI) binds to many CC chemokines with high affinity, acting as a potent inhibitor of chemokine action. We have used heteronuclear multidimensional NMR to determine the structure of an orthopoxvirus vCCI in complex with a human CC chemokine, MIP-1beta (macrophage inflammatory protein 1beta).

Glycosaminoglycan disaccharide alters the dimer dissociation constant of the chemokine MIP-1 beta.

Chemokines are immune system proteins that recruit and activate leukocytes to sites of infection. This recruitment is believed to involve the establishment of a chemokine concentration gradient by the binding of chemokines to glycosaminoglycans (GAGs). In previous studies, we elucidated the GAG binding site of the chemokine MIP-1beta and implicated the involvement of the chemokine dimer in GAG binding through residues across the dimer interface.

The binding surface and affinity of monomeric and dimeric chemokine macrophage inflammatory protein 1 beta for various glycosaminoglycan disaccharides.

Chemokines comprise a family of proteins that function in the immune response to recruit leukocytes to sites of infection. This recruitment is believed to be carried out by the establishment of a chemokine gradient by the binding of chemokines to sulfated polysaccharides known as glycosaminoglycans (GAGs) located on the extracellular surface of endothelial cells. In the present studies, multidimensional NMR spectroscopy was used to study the interaction of monomeric and dimeric chemokine macrophage inflammatory protein (MIP)-1 beta variants with a series of differentially sulfated disaccharides.