Measurement of Shoulder Range of Motion in Patients with Adhesive Capsulitis Using a Kinect

Range of motion (ROM) measurements are essential for the evaluation for and diagnosis of adhesive capsulitis of the shoulder (AC). However, taking these measurements using a goniometer is inconvenient and sometimes unreliable. The Kinect (Microsoft, Seattle, WA, USA) is gaining attention as a new motion detecting device that is nonintrusive and easy to implement. This study aimed to apply Kinect to measure shoulder ROM in AC; we evaluated its validity by calculating the agreement of the measurements obtained using Kinect with those obtained using goniometer and assessed its utility for the diagnosis of AC. Both shoulders of 15 healthy volunteers and affected shoulders of 12 patients with AC were included in the study. The passive and active ROM of each were measured with a goniometer for flexion, abduction, and external rotation. Their active shoulder motions for each direction were again captured using Kinect and the ROM values were calculated. The agreement between the two measurements was tested with the intraclass correlation coefficient (ICC). Diagnostic performance using the Kinect ROM was evaluated with Cohen’s kappa value. The cutoff values of the limited ROM were determined in the following ways: the same as passive ROM values, reflecting the mean difference, and based on receiver operating characteristic curves. The ICC for flexion/abduction/external rotation between goniometric passive ROM and the Kinect ROM were 0.906/0.942/0.911, while those between active ROMs and the Kinect ROMs were 0.864/0.932/0.925. Cohen’s kappa values were 0.88, 0.88, and 1.0 with the cutoff values in the order above. Measurements of the shoulder ROM using Kinect show excellent agreement with those taken using a goniometer. These results indicate that the Kinect can be used to measure shoulder ROM and to diagnose AC as an alternative to goniometer.     

Isolation of cDNA for bovine stomach 155 kDa protein exhibiting myosin light chain kinase activity.

Two proteins with myosin light chain kinase activity and electrophoretic molecular weights of 155,000 and 130,000 were each isolated from bovine stomach smooth muscle [Kuwayama, H., Suzuki, M., Koga, R., & Ebashi, S. (1988) J. Biochem. 104, 862-866]. The 155 kDa component showed a much higher superprecipitation-inducing activity than the 130 kDa component, when compared on the basis of equivalent myosin light chain kinase activity. In this study, we isolated a cDNA for the entire coding region of the 155 kDa protein. The deduced amino acid sequence revealed a high degree of similarity to those of chicken and rabbit smooth muscle myosin light chain kinases. Multiple motifs, such as three repeats of an immunoglobulin C2-like domain, a fibronectin type III domain, and unusual 20 repeats of 12 amino acids were detected in the sequence. Part of the amino-terminal sequence was similar to that of the actin- and calmodulin-binding domain of smooth muscle caldesmon. These observations suggest that the 155 kDa protein has additional functions other than its enzymatic activity. Two mRNAs of 6.0 and 2.6 kb in length in the bovine stomach smooth muscle RNAs were hybridized with cDNA probes. The 2.6-kb RNA probably encodes telokin, which is the carboxyl terminus of smooth muscle myosin light chain kinase. mRNAs with identical lengths were also detected in bovine aorta.     

Degranulation and histamine release from murine mast cells sensitized with dengue virus-immune sera

Mice were immunized with dengue type 2 virus (DEN 2) under a schedule favoring the production of IgE antibody. The antibody obtained could sensitize peritoneal resident mast cells both in vitro and in vivo so that the sensitized cells were degranulated and released histamine on challenge with the DEN 2 antigen. It was also demonstrated that the antibody was cytophilic and heat-labile. The above observations suggest that the present experimental system can be used to detect anti-DEN 2 IgE antibody in mice.     

Purification and characterization of yolk protein-2 from the fall webworm,Hyphantria cunea drury

Yolk proteins (YP1, YP2, and YP3) of the fall webworm, Hyphantria cunea, are of relatively low molecular weight. Yolk protein-2 (YP2) was purified from gel slices and by KBr density gradient ultracentrifugation followed by ion exchange chromatography. YP2 is composed of one subunit with a molecular weight of 35.5 kDa. YP2 contains neutral lipids (diacylglycerol and triacylglycerol) and phospholipids (phosphatidylcholine and phosphatidylethanolamine). The neutral lipids are largely composed of lauric acid and palmitoleic acid. YP2 contains relatively large amounts of glutamic acid and aspartic acid but small amounts of tyrosine, phenylalanine, and methionine. YP2 is a vitellin (Vn) synthesized by the fat body. Vitellogenin-2 (Vg2), the precursor of YP2, is present in very small amounts in the hemolymph. Lipophorin and storage protein also are found in the ovary of H. cunea, and these proteins do not immunologically cross-react with YP2. YP2 is detected in first instar larvae but completely disappears during the second instar, indicating that YP2 is intensively utilized during postembryonic development. Anti-YP2 antibodies cross-react with ovarial extracts of Bombyx mori but not with those of insects from other orders such as Cletus schmidti (Hemiptera), Lucilia illustris (Diptera), Anechura japonica (Dermaptera), Periplaneta americana (Dictyoptera), and Ducetia japonica (Orthoptera). © 1995 Wiley-Liss, Inc.