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SENIOR was a phase 3b, randomized, open-label, 2-arm, parallel-group, multicenter, 30-week trial. Randomization was stratified by screening HbA 1c (<8.0 vs ≥8.0 %), previous insulin use (Yes/No), and sulfonylurea or meglitinide use at screening (Yes/No). Insulin was titrated to the ADA-recommended glycemic target for healthy elderly individuals (fasting SMPG: 90–130 mg/dL [5.0–7.2 mmol/L]), a higher glycemic target than utilized previously in randomized controlled trials of insulin glargine 300 U/mL (Gla-300) versus 100 U/mL (Gla-100) in adults. The aim of the SENIOR trial was to compare the efficacy and safety of Gla-300 with Gla-100.

In total, 1014 individuals (≥65 years) with T2DM were included in the trial, of whom 241 were ≥75 years old. The primary endpoint of non-inferiority of mean change in HbA 1c for Gla-300 versus Gla-100 was achieved (least squares mean difference [95% CI]: 0.02, [−0.092 to 0.129] %). Similar percentages of participants in both groups reported confirmed (≤70 mg/dL [≤3.9 mmol/L]) or severe hypoglycemia. The annualized rates of documented symptomatic (≤70 mg/dL [≤3.9 mmol/L]) hypoglycemia were lower with Gla-300 versus Gla-100, both in the overall study population (1.85 vs 2.56 events/participant-year; rate ratio [RR] 0.74 [0.56 to 0.96]) and in the ≥75 years subpopulation (1.12 vs 2.71 events/participant-year; RR 0.45 [0.25 to 0.83]). Frequency of adverse events, including cardiovascular events, falls and fractures was similar between treatments.

These results indicate that Gla-300 was effective in older people with T2DM, with a good safety profile, resulting in comparable reductions in HbA 1c and lower rates of documented symptomatic hypoglycemia versus Gla-100.

Supported By: Sanofi ( NCT02320721)

Issue Section:
© The Author 2017. Published by Oxford University Press on behalf of The Gerontological Society of America.
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The evidence base to optimize CDI testing is weak. Clinical criteria for the diagnosis of CDI have altered as awareness of CDI has increased. Notably, the number and frequency of diarrheal stools required to justify CDI testing have declined over the past 40 years. Tedesco et al defined diarrhea as >5 loose stools per day in 1974 [ 167 ]; Teasley et al as >6 loose stools over a period of 36 hours in 1983 [ 168 ]; Fekety et al as liquid stools or >4 bowel movements per day for at least 3 days in 1989 [ 169 ]; and Johnson et al as ≥3 loose or watery bowel movements in 24 hours in 2013 [ 170 ]. Using the latter definition of diarrhea, Dubberke et al and Peterson et al (also using additional clinical criteria) have examined the frequency of these symptoms in patients whose stool is submitted for CDI testing [ 171 , 172 ]. Peterson et al that found 39% of patients did not meet the minimal diarrhea definition and were dropped from further analysis [ 172 ].

Dubberke et al used a clinical definition of ≥3 diarrheal bowel movements (type 6 or 7 stool on the Bristol Stool Chart) [ 173 ] in the 24 hours preceding stool collection, or diarrhea plus patient-reported abdominal pain or cramping. They found that 36% of patients failed to meet the clinical definition but were retained in the study [ 171 ]. The authors caution that even in the presence of clinical diarrheal symptoms, there may be confounding clinical issues such as laxative use, which was found in 19% within the previous 48 hours [ 171 ].

Clinicians can improve laboratory test relevance by only testing patients likely to have C. difficile disease. This includes not routinely performing testing on stool from a patient who has received a laxative within the previous 48 hours. Laboratories can improve specificity by rejecting specimens that are not liquid or soft (ie, take the shape of the container). In addition, laboratories may wish to collaborate with available quality improvement teams such as infection prevention and control and antibiotic stewardship, to assess appropriateness of testing in the population from which samples are submitted. This may involve periodic chart review in a series of patients to assess for clinical risk factors, signs, and symptoms suggestive of CDI.

Two diagnostic testing recommendations based on institutional and laboratory preagreed criteria for patient stool submission are prefaced by questions VII and VIII ( Figure 2 ).

Use a stool toxin test as part of a multistep algorithm (ie, glutamate dehydrogenase [GDH] plus toxin; GDH plus toxin, arbitrated by NAAT; or NAAT plus toxin) rather than a NAAT alone for all specimens received in the clinical laboratory when there are no preagreed institutional criteria for patient stool submission ( Figure 2 ) (weak recommendation, low quality of evidence).

There is a variety of available options for laboratory testing to support the diagnosis of CDI, and these are well described in several recent reviews [ 174 , 175 ]. In brief, these methods detect either the organism or one or both of its major toxins (A and B) directly in stool. Table 3 lists these methods in decreasing order of analytical sensitivity. Toxigenic culture (TC) uses a prereduced selective agar, cycloserine-cefoxitin-fructose agar or a variant of it, followed by anaerobic incubation for several days. Once there is growth, the organism is identified by several methods including matrix-assisted laser desorption/ionization–time of flight mass spectrometry, although the characteristic “horse barn odor” often heralds its presence. To enhance the recovery of the organism, a spore selection step, whether heat or alcohol shock, is applied to the stool prior to inoculating media. Once an organism is identified, a toxin test must be performed on the isolate to confirm its toxigenic potential. TC, although not standardized, has been one of the reference methods against which other methods are compared.

No reemerging T-type Ca 2+ currents have been recorded in the grossly hypertrophied myocytes of the 2-month feline healed infarct model [Pinto et al., unpublished data].

Thus several characteristics including decreased I CaL density and altered Ca 2+ current inactivation potentially contribute to persistent AP duration prolongation of hypertrophied myocytes of the remote regions of the healed infarct.

AP duration is typically prolonged in remote areas. The extent of AP prolongation appears to depend on the age of the infarct; myocytes from older infarcts (6–11 months) show greater prolongation compared to younger infarcts (1–2 months) [15] . Action potential durations at all phases of repolarization appear to be increased to a greater extent than in the infarct zone [15] ; this may vary depending on whether cells are epicardial or endocardial in origin.

There are no data on function or density of I to in myocytes from areas remote to the healed infarct.

I K : In non-infarcted subendocardial ventricular myocytes adjacent to the healed infarct, I K density but not amplitude is significantly decreased, similar to findings in global left ventricular hypertrophy [57–59] , reflecting cell enlargement under both conditions. Current and current–voltage relationships of I K tails are unchanged in remote area myocytes; however, tail current density is reduced at positive potentials and showed strong inward rectification. Voltage dependence of activation of I K tail is shifted to more positive potentials in myocytes from the remote area of the infarct (compared to normal myocytes), but there were no differences between the slopes of the activation and deactivation curves [56] .

It is obvious, from the examples cited above, that disease states can and do alter ion channel function. Observed changes in macroscopic currents can be the result of an acquired (versus genetic) change in structure and function of normally expressed channels, a change in the number of functional channels, or a combination of both.

A change in the number of functional channels can be determined at both the single channel and molecular levels. From a molecular standpoint, a change in the number of functional channels could be due to changes in the levels of expressed protein or to alterations in channel protein incorporation into the membrane.

A change in expression of functional channel proteins is most likely due to a change in gene transcription, translation, or post translational modification. Transcription, the initial step in protein expression, involves the production of an mRNA copy from a DNA template.

Recent studies suggest that transcription of different ion channel proteins is greatly affected by disease state. For instance, experimental myocardial hypertrophy, and treatments to prolong AP duration, result in a substantial increase in the K + channel Kv1.4 mRNA levels in cultured rat myocytes [60] (for review of nomenclature, see [61] ) . This gene regulation is reversed by normalization of hypertrophy [62] . There is no report yet, as to whether this enhanced transcription results in an enhancement of functional channel proteins in the hypertrophied cell. Tseng and her colleagues [32] have studied the effects of myocardial infarction (at 2–5 days post occlusion) on K + channel expression using RNase protection assays. In the course of so doing they found that while the molecular marker, d -glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mRNA levels are homogeneous in the normal ventricle, they are severely reduced in the infarcted canine ventricle making them unsuitable measures for internal controls. Therefore, using 28S rRNA as internal controls, they have recently reported on both the suppressed transcription and function of the native delayed rectifying K + currents in myocytes surviving in the infarcted heart. In particular, by 48 h post MI, mRNAs for dKvLQT1, dIsK and dERG are all reduced. By day 5, dKvLQT1 transcripts have recovered, but dIsK and dERG remain reduced [32] . These findings are consistent with loss in function of I Ks and I Kr in the 5-day border zone myocytes (see above). In the rat model by 3 days post MI there is a significant reduction in Kv4.2 channel protein levels in noninfarcted but regionally hypertrophied tissues with no changes in Kv2.1 or Kv1.5 levels [53] . By 3–4 weeks post MI in the same model, mRNAs of Kv1.4, Kv2.1 and Kv4.2 all appear to be significantly decreased, with no changes detected in either Kv1.2 or Kv1.5 levels [63] . Quantitative analysis of mRNA levels in normal and failing human ventricles (some post myocardial infarction) show that steady state mRNAs for Kv4.3 and HERG are decreased while no mRNA changes occur for Kv1.2,1.4,1.5,2.1 or I K1 proteins [64] .

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