Impact of muscle activation on ranges of motion during active elbow movement in children with spastic hemiplegic cerebral palsy

Background Children with spastic hemiplegic cerebral palsy are restricted in their daily activities due to limited active ranges of motion of their involved upper limb, specifically at the elbow. Their impaired muscles are frequently targeted by anti-spastic treatments that reduce muscle tone. But these treatments do not necessarily improve the limb function. There is a lack of comprehensive knowledge of the quantitative relations between muscle activation and joint active ranges of motion. Consequently, the objective of this study is to quantify the impact of muscle activation on the elbow active ranges of motion. Methods During voluntary elbow pronation/supination and extension/flexion movements, kinematic and electromyographic measurements were collected from the involved upper limb of 15 children with spastic hemiplegic cerebral palsy (mean age = 8.7 years, standard deviation = 2.2) and the dominant upper limb of 15 age-matched children who are typically developing. Representative indicators of the muscle activation, such as the muscle co-activation, were extracted from the electromyographic measurements. Findings Muscle co-activation in the involved upper limb accounted for 78% and 59% of the explained variance of the supination and extension limited active ranges of motion respectively. The agonist and antagonist muscle activations were both longer in the involved upper limb. Interpretations This study succeeded in quantifying the impact of longer antagonist muscle activation on decreased elbow active ranges of motion in children with spastic hemiplegic cerebral palsy. Longer agonist muscle activation suggests that strengthening agonist muscles could increase the extension and supination ranges of motion, which constitutes a perspective of future clinical studies

Association of leptin, 25-hydroxyvitamin D, and parathyroid hormone in women.

Vitamin D deficiency and adipocytokines have been implicated in the etiology of aging-related diseases such as cancer, osteoporosis, and diseases of the cardiovascular system. The association between elevated parathyroid hormone (PTH) and low 25-hydroxyvitamin D (25-OH-VitD) in plasma is used to define vitamin D deficiency, yet their associated mechanistic pathways are unclear. Utilizing plasma samples from women in a previous intervention study, we measured plasma 25-OH-VitD, leptin, adiponectin, PTH, and lipid levels. We observed strong positive associations for leptin with PTH, gamma -tocopherol, and body mass index (BMI) and inverse associations with 25-OH-VitD and adiponectin. Although commonly accepted that vitamin D deficiency causes hyperparathyroidism, we observed this association primarily in individuals with elevated leptin levels, suggesting that leptin may be an important modifier of this effect consistent with 25-OH-VitD-mediated inhibition of leptin. Leptin was highly correlated with the BMI/25-OH-VitD ratio (r = 0.80; P < 0.0001), consistent with a model in which BMI (adiposity) and 25-OH-VitD are the primary determinants of circulating leptin and PTH levels. This model may explain the failure of some studies to observe elevated PTH in vitamin D deficient adolescents and provides important insight into epidemiological studies exploring the associations of these individual biomarkers with chronic disease risk and mortality

Differential Expression of PRAMEL1, a Cancer/Testis Antigen, during Spermatogenesis in the Mouse

PRAME belongs to a group of cancer/testis antigens (CTAs) that are characterized by their restricted expression in normal gametogenic tissues and a variety of tumors. The PRAME family is one of the most amplified gene families in the mouse and other mammalian genomes. Members of the PRAME gene family encode leucine-rich repeat (LRR) proteins functioning as transcription regulators in cancer cells. However, the role of PRAME in normal gonads is unknown. The objective of this study is to characterize the temporal and spatial expression of the mouse Pramel1 gene, and to determine the cellular localization of the PRAMEL1 protein during the mouse spermatogenesis. Our results indicated that the mouse Pramel1 was expressed in testis only. The mRNA and protein expression level was low in the newborn testes, and gradually increased from 1- to 3-week-old testes, and then remained constant after three weeks of age. Immunofluorescent staining on testis sections with the mouse PRAMEL1 antibody revealed that PRAMEL1 was localized in the cytoplasm of spermatocytes and the acrosomal region of round, elongating and elongated spermatids. Further analyses on the testis squash preparation and spermatozoa at a subcellular level indicated that the protein localization patterns of PRAMEL1 were coordinated with morphological alterations during acrosome formation in spermatids, and were significantly different in connecting piece, middle piece and principal piece of the flagellum between testicular and epididymal spermatozoa. Collectively, our results suggest that PRAMEL1 may play a role in acrosome biogenesis and sperm motility