Brief communication: CAPriCORN: Chicago Area Patient-Centered Outcomes Research Network

The Chicago Area Patient-Centered Outcomes Research Network (CAPriCORN) represents an unprecedented collaboration across diverse healthcare institutions including private, county, and state hospitals and health systems, a consortium of Federally Qualified Health Centers, and two Department of Veterans Affairs hospitals. CAPriCORN builds on the strengths of our institutions to develop a cross-cutting infrastructure for sustainable and patient-centered comparative effectiveness research in Chicago. Unique aspects include collaboration with the University HealthSystem Consortium to aggregate data across sites, a centralized communication center to integrate patient recruitment with the data infrastructure, and a centralized institutional review board to ensure a strong and efficient human subject protection program. With coordination by the Chicago Community Trust and the Illinois Medical District Commission, CAPriCORN will model how healthcare institutions can overcome barriers of data integration, marketplace competition, and care fragmentation to develop, test, and implement strategies to improve care for diverse populations and reduce health disparities.     

Basilar venous plexus of the posterior fossa: a potential source of error in petrosal sinus sampling

Sampling of serum from the inferior petrosal sinus can provide important information about the source of elevated adrenocorticotropic hormone (ACTH) levels. This often leads to improved results of pituitary surgery for Cushing disease. The authors describe a successful catheterization technique and illustrate the venous anatomy of the inferior petrosal sinuses and basilar plexus.     

The evaluation of a new technique for anaerobic sampling of deep periodontal pockets

A new technique for the anaerobic sampling of deep periodontal pockets has been developed and evaluated in vitro and in vivo. The mean percentage difference of total viable counts from pairs of samples from nine deep periodontal pockets was found to be 76.4%. This compared favorably with an established technique for which the equivalent figure was 147.4%. Evidence was obtained that the first sample taken with the new sampler depleted the site. When correction was made for that effect, the mean percentage difference was found to be 31.1%. That value was in good agreement with the variation obtained by taking repeat samples from centrifuged deposits of pure cultures of bacteria.     

Platelet adhesion to collagen types I through VIII under conditions of stasis and flow is mediated by GPIa/IIa (alpha 2 beta 1-integrin)

Platelet adhesion to fibrillar collagens (types I, II, III, and V) and nonfibrillar collagens (types IV, VI, VII, and VIII) was investigated in the presence of physiologic concentrations of divalent cations under conditions of stasis and flow. Under static conditions, platelet adhesion was observed to collagen types I through VII but not to type VIII. Under flow conditions, platelet adhesion to collagen types I, II, III, and IV was almost independent of shear rates above 300/s. Collagen type V was nonadhesive. Platelet adhesion to collagen type VI was shear rate-dependent and optimal at a rate of 300/s. Collagen types VII and VIII showed minor reactivity and supported platelet adhesion only between shear rates 100 to 1,000/s. Monoclonal antibody (MoAb) 176D7, directed against platelet membrane glycoprotein Ia (GPIa; very late antigen [VLA]-alpha 2 subunit), completely inhibited platelet adhesion to all collagens tested, under conditions of both stasis and flow. Platelet adhesion to collagen type III at shear rate 1,600/s was only inhibited for 85%. The concentration of antibody required for complete inhibition of platelet adhesion was dependent on the shear rate and the reactivity of the collagen. An MoAb directed against GPIIa (VLA-beta subunit) partially inhibited platelet adhesion to collagen. These results show that GPIa-IIa is a major and universal platelet receptor for eight unique types of collagen.