Training in Buprenorphine and Office-Based Opioid Treatment: A Survey of Psychiatry Residency Training Programs.

OBJECTIVE: Psychiatrists are well suited to provide office-based opioid treatment (OBOT), but the extent to which psychiatry residents are exposed to buprenorphine training and OBOT during residency remains unknown. METHODS: Psychiatry residency programs in the USA were recruited to complete a survey. RESULTS: Forty-one programs were included in the analysis for a response rate of 23.7 %. In total, 75.6 % of the programs currently offered buprenorphine waiver training and 78.1 % provided opportunities to treat opioid dependence with buprenorphine under supervision. Programs generally not only reported favorable beliefs about OBOT and buprenorphine waiver training but also reported numerous barriers. CONCLUSIONS: The majority of psychiatry residency training programs responding to this survey offer buprenorphine waiver training and opportunities to treat opioid-dependent patients, but numerous barriers continue to be cited. More research is needed to understand the role residency training plays in impacting future practice of psychiatrists.

Non-enzymatic glycation of type I collagen diminishes collagen-proteoglycan binding and weakens cell adhesion.

Non-enzymatic glycation of type I collagen occurs in aging and diabetes, and may affect collagen solubility, charge, polymerization, and intermolecular interactions. Proteoglycans(1) (PGs) bind type I collagen and are proposed to regulate fibril assembly, function, and cell-collagen interactions. Moreover, on the collagen fibril a keratan sulfate (KS) PG binding region overlaps with preferred collagen glycation sites. Thus, we examined the effect of collagen modified by simple glycation on PG-collagen interactions. By affinity coelectrophoresis (ACE), we found reduced affinities of heparin and KSPGs for glycated but not normal collagen, whereas the dermatan sulfate (DS)PGs decorin and biglycan bound similarly to both, and that the affinity of heparin for normal collagen decreased with increasing pH. Circular dichroism (CD) spectroscopy revealed normal and glycated collagens to assume triple helical conformations, but heparin addition caused precipitation and decreased triple helical content-effects that were more marked with glycated collagen. A spectrophotometric assay revealed slower polymerization of glycated collagen. However, ultrastructural analyses indicated that fibrils assembled from normal and glycated collagen exhibited normal periodicity, and had similar structures and comparable diameter distributions. B-cells expressing the cell surface heparan sulfate PG syndecan-1 adhered well to normal but not glycated collagen, and endothelial cell migration was delayed on glycated collagen. We speculate that glycation diminishes the electrostatic interactions between type I collagen and PGs, and may interfere with core protein-collagen associations for KSPGs but not DSPGs. Therefore in vivo, collagen glycation may weaken PG-collagen interactions, thereby disrupting matrix integrity and cell-collagen interactions, adhesion, and migration.