Reporting the Reliability of Accelerometer Data with and without Missing Values

Objectives

Participants with complete accelerometer data often represent a low proportion of the total sample and, in some cases, may be distinguishable from participants with incomplete data. Because traditional reliability methods characterize the consistency of complete data, little is known about reliability properties for an entire sample. This study employed Generalizability theory to report an index of reliability characterizing complete (7 days) and observable (1 to 7 days) accelerometer data.

Design

Cross-sectional.

Methods

Accelerometer data from the Study of Early Child Care and Youth Development were analyzed in this study. Missing value analyses were conducted to describe the pattern and mechanism of missing data. Generalizability coefficients were derived from variance components to report reliability parameters for complete data and also for the entire observable sample. Analyses were conducted separately by age (9, 11, 12, and 15 yrs) and daily wear time criteria (6, 8, 10, and 12 hrs).

Results

Participants with complete data were limited (<34%) and, most often, data were not considered to be missing completely at random. Across conditions, reliability coefficients for complete data were between 0.74 and 0.87. Relatively lower reliability properties were found across all observable data, ranging from 0.52 to 0.67. Sample variability increased with longer wear time criteria, but decreased with advanced age.

Conclusions

A reliability coefficient that includes all participants, not just those with complete data, provides a global perspective of reliability that could be used to further understand group level associations between activity and health outcomes.     

Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation

Acidic noncaspase proteases-like cathepsins have been introduced as novel mediators of apoptosis. A clear role for these proteases and the acidic endolysosomal compartment in apoptotic signalling is not yet defined. To understand the role and significance of noncaspases in promoting and mediating cell death, it is important to determine whether an intersection of these proteases and the caspase pathway exists. We recently identified the endolysosomal aspartate protease cathepsin D (CTSD) as a target for the proapoptotic lipid ceramide. Here, we show that tumor necrosis factor (TNF)-induced CTSD activation depends on functional acid sphingomyelinase (A-SMase) expression. Ectopic expression of CTSD in CTSD-deficient fibroblasts results in an enhanced TNF-mediated apoptotic response. Intracellular colocalization of CTSD with the proapoptotic bcl-2 protein family member Bid in HeLa cells, and the ability of CTSD to cleave directly Bid in vitro as well as the lack of Bid activation in cathepsin-deficient fibroblasts indicate that Bid represents a direct downstream target of CTSD. Costaining of CTSD and Bid with Rab5 suggests that the endosomal compartments are the common 'meeting point'. Caspase-9 and -3 activation also was in part dependent on A-SMase and CTSD expression as revealed in the respective deficiency models. Our results link as novel endosomal intermediates the A-SMase and the acid aspartate protease CTSD to the mitochondrial apoptotic TNF pathway.