The Access Technology Program of the Indiana Clinical Translational Sciences Institute (CTSI): A model to facilitate access to cutting-edge technologies across a state.

Introduction: Access to cutting-edge technologies is essential for investigators to advance translational research. The Indiana Clinical and Translational Sciences Institute (CTSI) spans three major and preeminent universities, four large academic campuses across the state of Indiana, and is mandate to provide best practices to a whole state.

Methods: To address the need to facilitate the availability of innovative technologies to its investigators, the Indiana CTSI implemented the Access Technology Program (ATP).

Project development teams: a novel mechanism for accelerating translational research.

The trend in conducting successful biomedical research is shifting from individual academic labs to coordinated collaborative research teams. Teams of experienced investigators with a wide variety of expertise are now critical for developing and maintaining a successful, productive research program. However, assembling a team whose members have the right expertise requires a great deal of time and many resources.

Cathepsin E is a specific marker of dysplasia in APC mouse intestine.

Transcriptional profiling of APC(Min/+) mouse intestinal epithelial tissue has revealed that cathepsin E (catE) manifests high relative expression in adenomas and carcinomas relative to normal epithelium. Real-time RT-PCR data presented previously confirm the presence of catE transcript in APC(Min/+) adenomatous cells compared with samples derived from normal APC(Min/+) and wild-type tissue. At the protein level, strong, highly specific immunohistochemical staining for catE is displayed in dysplastic lesions of APC(Min/+) mice.

Structure-function analysis of the streptokinase amino terminus (residues 1-59).

Streptokinase (SK) binds to plasminogen (Pg) to form a complex that converts substrate Pg to plasmin. Residues 1-59 of SK regulate its capacity to induce an active site in bound Pg by a nonproteolytic mechanism and to activate substrate Pg in a fibrin-independent manner. We analyzed 24 SK mutants to better define the functional properties of SK-(1-59).