Supporting Transformation through Delivery System Reform Incentive Payment Programs: Lessons from New York State.

The New York Delivery System Reform Incentive Payment (DSRIP) waiver was viewed as a prototype for Medicaid and safety net redesign waivers in the Affordable Care Act (ACA) era. After the insurance expansions of the ACA were implemented, it was apparent that accountability, value, and quality improvement would be priorities in future waivers in many states. Despite New York's distinct provider relationships, previous coverage expansions, and local and state politics, it is important to understand the key characteristics of the waiver so that other states can learn how to better incorporate value-based arrangements into future waivers or attempts to limit spending under proposed Medicaid per-capita caps or block grants.

DNA bending is induced by binding of vitamin D receptor-retinoid X receptor heterodimers to vitamin D response elements.

The ability of vitamin D receptor-retinoid X receptor (VDR-RXR) heterodimers to induce a DNA bend upon binding to various vitamin D response elements (VDRE) has been investigated by circular permutation and phasing analysis. Recombinant rat VDR expressed in the baculovirus system and purified recombinant human RXR beta have been used. The VDREs were from 1,25-dihydroxyvitamin D3 (1,25-[OH]2D3) enhanced genes (rat osteocalcin, rOC; mouse osteopontin, mOP, and rat 1,25-dihydroxyvitamin D3-24-hydroxylase, r24-OHase), and a 1,25-(OH)2D3 repressed gene (human parathyroid hormone, hPTH).

Bacterial expression and characterization of the ligand-binding domain of the vitamin D receptor.

The ligand-binding domain of the rat vitamin D receptor (amino acids 115-423) was expressed as an amino-terminal His-tagged protein in a bacterial expression system and purified over Ni-nitrilotriacetic acid resin and a Mono S column. The purified protein bound its ligand, 1,25-dihydroxyvitamin D3, with high affinity, similar to that of the full-length protein. Saturation of the protein with ligand quenched 90% of the tryptophan fluorescence, consistent with the purified protein being uniformly able to bind ligand.