Early Career Training in Addiction Medicine: A Qualitative Study with Health Professions Trainees Following a Specialized Training Program in a Canadian Setting.

Background: There has been a notable deficiency in the implementation of addiction science in clinical practice and many healthcare providers feel unprepared to treat patients with substance use disorders (SUD) following training. However, the perceptions of addiction medicine training by learners in health professions have not been fully investigated. This qualitative study explored perceptions of prior training in SUD care among early-career trainees enrolled in Addiction Medicine fellowships and electives in Vancouver, Canada. Methods: From April 2015 - August 2018, we interviewed 45 early-career physicians, social workers, nurses, and 17 medical students participating in training in addiction medicine. We coded transcripts inductively using qualitative data analysis software (NVivo 11.4.3). Results: Findings revealed six key themes related to early-career training in addiction medicine: (1) Insufficient time spent on addiction education, (2) A need for more structured addictions training, (3) Insufficient hands-on clinical training and skill development, (4) Lack of patient-centeredness and empathy in the training environment, (5) Insufficient implementation of evidence-based medicine, and (6) Prevailing stigmas toward addiction medicine. Conclusion: Early clinical training in addiction medicine appears insufficient and largely focused on symptoms, rather than etiology or evidence. Early career learners in health professions perceived benefit to expanding access to quality education and reported positive learning outcomes after completing structured training programs.

The apical lamina and its role in cell adhesion in sea urchin embryos.

The hyaline layer (HL) is an extracellular matrix surrounding sea urchin embryos which has been implicated in a cell adhesion and morphogenesis. The apical lamina (AL) is a fibrous meshwork that remains after removal of hyalin from the HL and the fibropellins (FP) are glycoproteins thought to be the principal components of the AL. Using anti-FP antibodies (AL-1 and AL-2) we report immunoprecipitations and affinity purifications yield a high molecular weight complex comprised of the FP glycoproteins. The three components form a complex, stabilized by disulphide cross-linking and have stochiometric ratios of 2 FPIa molecules to 1 each of FPIb and FPIII. Pulse chase experiments indicate all 3 FP's are synthesized throughout development with peaks in synthesis during cleavage and a sustained peak beginning at hatching. Using immunogold and immunoperoxidase localization, the FP localize to a fibrillar complex forming the innermost layer of the HL. In cell adhesion experiments, cells adhere to affinity purified FP in a temperature, time and concentration dependent manner. Cell adhesion to Fp is about 70% of that seen when hyalin is used as a substrate. Pretreating with AL-1 and AL-2 reduces in vitro cell adhesion by about 65%. We conclude FP's form a fibrillar complex, which is synthesized throughout early development and functions, with other components of the HL, as a substrate for cell adhesion.