Promoting Active Aging: Lessons Learned in an Implementation Pilot in Primary Care.

BACKGROUND: Physical activity (PA) preserves mobility, but few practices screen older adults for mobility impairment or counsel on PA. DESIGN: "Promoting Active Aging" (PAA) was a mixed-methods randomized-controlled pilot, to test the feasibility and acceptability of a video-based PA counseling tool and implementation into practice of two mobility assessment tools. SETTING: Three primary care practices affiliated with Wake Forest Baptist Health. PARTICIPANTS: Adults aged 65 years and older who presented for primary care follow-up and were willing and able to answer self-report questions and walk 4 meters (n = 59). INTERVENTION: Video-based PA counseling intervention versus control video, "Healthy Eating." MEASUREMENTS: Potential participants completed mobility assessments: self-report (Mobility Assessment Tool-short form (MAT-sf)) and performance based (4-meter walk test). We assessed PAA's implementation-feasibility, acceptability, and value-via interviews and surveys. Effectiveness was measured via participant attendance at a PA information session. RESULTS: Of 92 patients approached, 89 (96.7%) agreed to mobility assessment. Eighty-nine completed MAT-sf, and 97.8% (87/89) completed 4-meter walk test. Sixty-seven (75%) met eligibility criteria, and 59 (88%) consented to be randomized either to the PA counseling intervention (Video-PA) or to active control (Video-C). Most participants viewed the walk test positively (51/59; 86.4%). Staff reported that completion of patient surveys, MAT-sf, and videos required significant staff time and support (median = 26 minutes for all), resulting in low acceptability of MAT-sf and the videos. Attendance at a PA information session did not differ by randomization group (Video-PA = 11/29 (37.9%); Video-C = 12/30 (40%); 95% confidence interval for difference in proportion = -0.29 to 0.25). CONCLUSIONS: Mobility assessment, particularly a 4-meter walk test, was feasible in primary care. Tablet-based assessment (MAT-sf) and video counseling tools, selected to reduce staff effort, instead required significant time to implement. Future work to promote PA should identify effective ways to facilitate adoption of PA in sedentary older adults that do not burden staff.

Identification and cross-species comparisons of CYP2F subfamily genes in mammals.

The cytochrome P450 2F (CYP2F) subfamily genes are currently known only from cDNA sequences in human, mouse, rat and goat. Compared to other divisions of the CYP2 gene family, the CYP2F subfamily is unusual in having few genes per species and in being selectively expressed in lung tissues. Sequencing genomic DNAs from human and gorilla has allowed us to determine the number of CYP2F subfamily loci in these species, the sources of known human transcripts, and the functional status of CYP2F loci in both primates. This information will make accurate genotyping of the functional and medically significant CYP2F1 gene possible in humans. Comparisons across multiple species show that the sequences of CYP2F subfamily genes are very conserved in mammals for intronic as well as exonic DNA.

Determinants of the interaction of the spinal muscular atrophy disease protein SMN with the dimethylarginine-modified box H/ACA small nucleolar ribonucleoprotein GAR1.

Deletion or mutation of the SMN1 (survival of motor neurons) gene causes the common, fatal neuromuscular disease spinal muscular atrophy. The SMN protein is important in small nuclear ribonucleoprotein (snRNP) assembly and interacts with snRNP proteins via arginine/glycine-rich domains. Recently, SMN was also found to interact with core protein components of the two major families of small nucleolar RNPs, fibrillarin and GAR1, suggesting that SMN may also function in the assembly of small nucleolar RNPs. Here we present results that indicate that the interaction of SMN with GAR1 is mediated by the Tudor domain of SMN. Single point mutations within the Tudor domain, including a spinal muscular atrophy patient mutation, impair the interaction of SMN with GAR1. Furthermore, we find that either of the two arginine/glycine-rich domains of GAR1 can provide for interaction with SMN, but removal of both results in loss of the interaction. Finally, we have found that unlike the interaction of SMN with the Sm snRNP proteins, interaction with GAR1 and fibrillarin is not enhanced by arginine dimethylation. Our results argue against post-translational arginine dimethylation as a general requirement for SMN recognition of proteins bearing arginine/glycine-rich domains.