Prevalence of malnutrition & anemia in preschool children; a single center study.

BACKGROUND: Malnutrition including undernutrition, overnutrition, and micronutrient deficiencies are considerable problems worldwide, with variable burdens among different communities. Its complications include physical and cognitive impairment, with the probability of irreversible lifelong consequences. We aimed to assess the prevalence of undernutrition, overweight, obesity, and anemia in preschoolers, being a risk group for developmental adverse events. METHODS: We recruited 505 healthy preschool children, with a male: female ratio of 1.05:1. Children with chronic diseases were excluded. We used anthropometry and complete blood count to screen for malnutrition and anemia. RESULTS: The mean age of the study group was 3.8 ± 1.4 years (1.02-7). The screening results were average in 228 (45.1%) children, while 277 (54.9%) children had either abnormal anthropometry, anemia, or both. We observed undernutrition in 48 (9.5%) children; among them, 33 (6.6%) were underweight, 33 (6.6%) wasted, and 15 (3%) were stunted, with no significant difference between children aged below or above five. We identified overnutrition in 125 (24.8%); 43 (8.5%) were overweight, 12 (2.4%) were obese, and 70 (13.9%) had a high body mass index Z score, not qualifying the definition of overweight. Anemia was diagnosed in 141 (27.9%) children and was significantly more frequent among older children without gender discrimination. About 10% (50 children) had both anemia and abnormal anthropometry. The frequency of abnormal anthropometry was comparable between children with anemia and those with normal hemoglobin. CONCLUSION: Malnutrition and anemia in preschoolers are still a heavy burden affecting about half of our study group, with an upward trend towards the overnutrition side. Anemia is still a moderate public health problem in preschoolers.

In vivo characterization of mutant myotilins.

Myofibrillar myopathy (MFM) is a group of disorders that are pathologically defined by the disorganization of the myofibrillar alignment associated with the intracellular accumulation of Z-disk-associated proteins. MFM is caused by mutations in genes encoding Z-disk-associated proteins, including myotilin. Although a number of MFM mutations have been identified, it has been difficult to elucidate the precise roles of the mutant proteins. Here, we present a useful method for the characterization of mutant proteins associated with MFM. Expression of mutant myotilins in mouse tibialis anterior muscle by in vivo electroporation recapitulated both the pathological changes and the biochemical characteristics observed in patients with myotilinopathy. In mutant myotilin-expressing muscle fibers, myotilin aggregates and is costained with polyubiquitin, and Z-disk-associated proteins and myofibrillar disorganization were commonly seen. In addition, the expressed S60C mutant myotilin protein displayed marked detergent insolubility in electroporated mouse muscle, similar to that observed in human MFM muscle with the same mutation. Thus, in vivo electroporation can be a useful method for evaluating the pathogenicity of mutations identified in MFM.

Distal myopathy in multi-minicore disease.

A 52-year-old man noted distal dominant slowly progressive muscle weakness at age 36 years. On muscle CT, the red muscles of the soleus, anterior tibial and paraspinal muscles, where type 1 fiber is known to predominate, were almost totally replaced by fat tissue while quadriceps femoris, gastrocnemius and upper extremity muscles were relatively spared. Quadriceps muscle biopsy revealed multi-minicores in addition to occasional larger cores, in about 70% of the type 1 fibers. A novel heterozygous nucleotide change c.5869T > A (p.S1957T) was identified in RYR1. Although pathogenicity was not confirmed, this nucleotide change was absent in 100 control DNA. We did not find a mutation in either multi-minicore disease-associated gene, SEPN1, or major distal myopathy-related genes, including GNE, ZASP, MYOT, exons 32-36 of MYH7, and the last exon of TTN. This is probably a unique form of distal myopathy characterized by the presence of multi-minicores with preferential involvement of type 1 fibers.

Defective myotilin homodimerization caused by a novel mutation in MYOT exon 9 in the first Japanese limb girdle muscular dystrophy 1A patient.

Myotilin is a muscle-specific Z disk protein. Several missense mutations in the myotilin gene (MYOT) have been identified in limb girdle muscular dystrophy (LGMD), myofibrillar myopathy, and distal myopathy patients. All previously reported pathogenic MYOT mutations have been identified only in Exon 2. We sequenced MYOT in 138 patients diagnosed as having LGMD, myofibrillar myopathy, or distal myopathy, and identified a novel MYOT mutation in Exon 9 encoding the second immunoglobulin-like domain in 1 patient with clinically typical LGMD. By light microscopy, there were scattered fibers with rimmed vacuoles and myofibrillary disorganization in the patient's muscle biopsy; accumulation of Z disk proteins was observed by immunohistochemistry. Immunoblot analysis demonstrated that the amount of myotilin monomer was increased in the patient muscle, but that the myotilin homodimeric band was decreased. Functional analysis of the myotilin mutation using a yeast 2-hybrid system revealed defective homodimerization of the mutant myotilin and decreased interaction between mutant myotilin and alpha-actinin. The homodimerization defect was further demonstrated by immunoprecipitation. This is the first MYOT mutation outside of Exon 2 in an LGMD type 1A patient and the first MYOT mutation identified in the Japanese population. This mutation in the second immunoglobulin-like domain impairs myotilin dimerization and alters the binding between myotilin and alpha-actinin, which is known to be important for actin bundling.

Rigid spine syndrome caused by a novel mutation in four-and-a-half LIM domain 1 gene (FHL1).

Four-and-a-half LIM domain 1 gene (FHL1) has recently been identified as the causative gene for reducing body myopathy (RBM), X-linked scapuloperoneal myopathy (SPM) and X-linked myopathy with postural muscle atrophy (XMPMA). Rigid spine is a common clinical feature of the three diseases. We searched for FHL1 mutations in eighteen patients clinically diagnosed as rigid spine syndrome (RSS). We identified one RSS patient with FHL1 mutation. Reducing bodies were observed in few fibers of the patient's muscle sample. Amount of FHL1 protein was decreased on immunoblotting. In conclusion, FHL1 can be one of the causative genes for RSS.