Background and Purpose: Prenatal substance use continues to be a critical public health concern. Integrating reproductive health promotion with addiction treatment is a promising approach to addressing this issue. This study was designed to understand strengths and challenges of a pilot reproductive health program, consisting of preconception/interconception health classes, childbirth education classes, and access to free doula services, for people in addiction treatment. Methods: The study design was a qualitative formative evaluation. Observations of the program (n=9) were conducted along with interviews (n=12) with clients, counselors, and program facilitators. Results: Strengths included a good fit between the program and clients’ needs and commitment to further integrate the program. Challenges included inconsistent participation and issues of facilitator selection and training. Barriers were noted related to the complex and chaotic lives of the clientele. Techniques to address inconsistent participation through mandated attendance as well as rotating and reviewing content showed mixed success. Conclusion: The study found the program to be well-regarded by stakeholders, but several structural challenges were identified. Future programs should strive for greater integration between treatment providers and reproductive health facilitators. Research is also needed to assess the effectiveness of providing integrated reproductive health education to clients engaged in addiction treatment.
The protein kinase A regulatory type I alpha subunit (PKA RegI) is the cAMP dependent subunit of the PKA holoenzyme. The gene for PKA RegI is located on chromosome 17q23‐17q24 and extends roughly 21 kb in length. PKA RegI is a component of the PKA holoenzyme, which is composed of a dimer of two regulatory subunits bound to a dimer of catalytic subunits (PKA Cat) to create a tetrameric protein in the inactive state. The PKA holoenzyme is activated by each PKA RegI monomer binding two molecules of cAMP at two distinct sites (3). This binding changes the shape of the regulatory subunit, therefore altering its affinity for the catalytic subunit by roughly 4 orders of magnitude (3). This causes the regulatory subunits to dissociate from the catalytic subunits, thereby releasing the catalytic subunits as active monomers to phosphorylate their intracellular targets. In their active state, the catalytic subunits act as active serine‐threonine kinases and have the potential to phosphorylate various targets which may alter muscle contractility as well as cell growth, proliferation and differentiation. PKA RegI is therefore an important protein with a vital role in the cardiovascular system, and its role in other tissues and disease states is being investigated. In particular, the Arg74Cys mutation of PKA RegI is found in Carney Complex, an autosomal dominant disorder that can cause a range of effects including skin lesions, tissue tumors (especially cardiac) and various types of endocrine tumors (1). It is therefore of interest to characterize the functional impact of this missense mutation on PKA RegI function in order to better understand the role of this mutation in the etiology of Carney Complex. Therefore, this study used biochemical and spectroscopic methods to examine the potential impact of the Arg74Cys mutation on the affinity of PKA RegI for both cAMP and its PKA Cat binding partner (2), as well as the effect of this mutation on PKA RegI phosphorylation at a novel downstream serine residue, Ser77.
Purified protein samples are often acquired via recombinant DNA techniques using heterologous E. coli induced expression systems. This bacterial expression and purification technique has been widely utilized for decades, and many researchers have worked under the misconception that eukaryotic proteins are not post‐translationally modified in a significant way during expression and purification in bacteria. Based on contradicting experimental data, we hypothesized that cortactin is phosphorylated by endogenous kinases in E. coli. We analyzed the phosphorylation state of cortactin after in vitro purification from E. coli using western blotting techniques and phosphoprotein stains. We found a heterogenous population of both phosphoserine and phosphotyrosine cortactin after protein purification. As phosphorylation of cortactin has been a significant research focus in many research labs over the last two decades, this result calls for increased scrutiny of experimental results involving in vitro phosphorylated cortactin. This work was supported by the OHSU Medical Research Foundation Award and Linfield College Faculty/Student Collaborative Research Fund.
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