A substudy evaluating treatment intensification on medication adherence among hypertensive patients receiving home blood pressure telemonitoring and pharmacist management.

WHAT IS KNOWN AND OBJECTIVE: Hypertension is a leading cause of death and major contributor to heart attacks, strokes, heart and kidney failure. Antihypertensive (HTN medication) non-adherence contributes to uncontrolled hypertension. Effective initiatives to improve uncontrolled hypertension include a team-based approach with home blood pressure (BP) monitoring. Our study objective was to evaluate whether objectively measured medication adherence was influenced by home BP telemonitoring and pharmacist management. METHODS: We analysed HTN medication adherence in 240 patients who received home BP telemonitoring and pharmacist intervention (TI). Adherence was measured based on prescription fills and the proportion of days covered (PDC). HTN medications continued pre- to post-baseline were similar for telemonitoring intervention (TI) and usual care (UC) patients (rate ratio = 1·00, P = 0·90). RESULTS AND DISCUSSION: More HTN medications were discontinued pre- to post-baseline in TI patients (rate ratio = 1·38, P = 0·04). Similarly, more HTN medications were added in TI patients (rate ratio = 2·46, P < 0·001). The proportion with a mean PDC ≥ 0·8 for HTN medications added after baseline and overall adherence did not differ between groups. WHAT IS NEW AND CONCLUSION: Medication adherence was high in both groups; however, medication adherence was not significantly altered by the intervention. There were more medication modifications and greater medication intensification among TI patients.

Gene encoding the group B streptococcal protein R4, its presence in clinical reference laboratory isolates & R4 protein pepsin sensitivity.

BACKGROUND & OBJECTIVES: R proteins were first identified by Lancefield in group B Streptococcus (GBS) as resistant to trypsin at pH8 and sensitive to pepsin at pH2. The R4 protein found predominantly in type III and some type II and V invasive isolates conforms to these criteria. The Rib protein, although structurally and epidemiologically similar to R4, was reported as resistant to both proteases. We report here the gene encoding the R4 protein from a type III group B streptococcal isolate (76-043) well characterized in our laboratory. METHODS: Trypsin extracted GBS proteins were assayed for protease sensitivities by double-diffusion Ouchterlony using varying conditions for the enzyme pepsin. Standard haemoglobin assay was used to examine pepsin enzymatic activity. Thirty clinical isolates of varying protein profiles identified by double-diffusion from our reference strain laboratory were screened by PCR and Southern technique. SDS-PAGE gel purified R4 amino acid sequences were determined and used to design oligonucleotide primers for screening a 76-043 genomic library. RESULTS: R4 was sensitive to pepsin at pH2 but appeared resistant at pH4, the reported pH used for Rib. By standard haemoglobin assay and trypsin extract studies of R4 protein, pepsin was shown to be active at pH2, yet easily inactivated; assays of GBS surface proteins are critical at pH2. Of the amino acids initially sequenced from R4, 88 per cent (61/69) showed identity to Rib; the r4 nucleotide sequence was identical to that of rib. All isolates with strong positive protein reactions for R4 were positive in both PCR and Southern technique, whereas isolates expressing alpha, beta, R1/R4, and R5 (BPS) protein profiles were not. INTERPRETATION & CONCLUSION: Sequenced PCR products aligned with identity to the R4 and Rib nucleotide sequences and confirmed the identity of these proteins and their molecular sequences.