Weight measurement using image-based pose analysis

Image-based gait analysis as a means of biometric identification has attracted much research attention. Most of the existing methods focus on human identification, posture analysis and movement tracking. There have been few investigations on measuring the carried load based on the carrier＇s gait characteristics by automatic image processing. Nevertheless, this measurement is very useful in a number of applications, such as the study of the carried load on the postural development of children and adolescence. In this paper, we investigate how to automatically estimate the carried weight from a sequence of images. We present a method to extract human gait silhouette based on an observation that humans tend to minimize the energy during motion. We compute several angles of body leaning and determine the relationship of the carried weight, the leaning angles and the centroid location according to a human kinetic study. Our weight determination method has been verified successfully by experiments.     

Mutation of the matrix metalloproteinase 2 gene (MMP2) causes a multicentric osteolysis and arthritis syndrome.

The inherited osteolyses or 'vanishing bone' syndromes are a group of rare disorders of unknown etiology characterized by destruction and resorption of affected bones. The multicentric osteolyses are notable for interphalangeal joint erosions that mimic severe juvenile rheumatoid arthritis (OMIMs 166300, 259600, 259610 and 277950). We recently described an autosomal recessive form of multicentric osteolysis with carpal and tarsal resorption, crippling arthritic changes, marked osteoporosis, palmar and plantar subcutaneous nodules and distinctive facies in a number of consanguineous Saudi Arabian families. We localized the disease gene to 16q12-21 by using members of these families for a genome-wide search for homozygous-by-descent microsatellite markers. Haplotype analysis narrowed the critical region to a 1.2-cM region that spans the gene encoding MMP-2 (gelatinase A, collagenase type IV; (ref. 3). We detected no MMP2 enzymatic activity in the serum or fibroblasts of affected family members. We identified two family-specific homoallelic MMP2 mutations: R101H and Y244X. The nonsense mutation effects a deletion of the substrate-binding and catalytic sites and the fibronectin type II-like and hemopexin/TIMP2 binding domains. Based on molecular modeling, the missense mutation disrupts hydrogen bond formation within the highly conserved prodomain adjacent to the catalytic zinc ion.