The role of mesenchymal cells in the pathophysiology of inflammatory arthritis.

Rheumatoid arthritis (RA) is a chronic inflammatory disorder of the joints that can cause severe disability. While the role of inflammatory cells in the pathogenesis of RA has been well established, the specific contribution of resident cells within the synovial membrane, especially those of mesenchymal origin, has become the object of closer scrutiny only recently. The central position of these cells in the disease process of RA is underlined by their involvement in its main pathophysiological features: inflammation, hyperplasia and joint destruction.

Interactions of the basic N-terminal and the acidic C-terminal domains of the maize chromosomal HMGB1 protein.

Maize HMGB1 is a typical member of the family of plant chromosomal HMGB proteins, which have a central high-mobility group (HMG)-box DNA-binding domain that is flanked by a basic N-terminal region and a highly acidic C-terminal domain. The basic N-terminal domain positively influences various DNA interactions of the protein, while the acidic C-terminal domain has the opposite effect. Using DNA-cellulose binding and electrophoretic mobility shift assays, we demonstrate that the N-terminal basic domain binds DNA by itself, consistent with its positive effects on the DNA interactions of HMGB1.

Phosphorylation of maize and Arabidopsis HMGB proteins by protein kinase CK2alpha.

In plants, a variety of chromatin-associated high mobility group (HMG) proteins belonging to the HMGB family have been identified. We have examined the phosphorylation of the HMGB proteins from the monocotyledonous plant maize and the dicotyledonous plant Arabidopsis by protein kinase CK2alpha. Maize CK2alpha phosphorylates the maize HMGB1 and HMGB2/3 proteins and the Arabidopsis HMGB1, HMGB2/3, and HMGB4 proteins.