Fibromyalgia in primary antiphospholipid (Hughes) syndrome.

Fibromyalgia (FM) is a syndrome that can be associated with several rheumatic diseases. However, no study has evaluated its frequency in patients with primary antiphospholipid syndrome (PAPS). The objective of this study was to analyze the frequency of FM in PAPS patients compared with healthy controls, to determine the possible associations between FM and PAPS features, and also to evaluate quality of life and depression in these patients. This case-control study included 30 PAPS patients (by the Sapporo criteria) and 40 healthy subjects. Demographic and clinical data, drug use, and antiphospholipid antibodies were analyzed. FM was diagnosed based on international criteria (ACR). Questionnaires on quality of life, including the Short Form 36 Health Survey (SF-36), Beck Depression Inventory (BDI), Fibromyalgia Impact Questionnaire (FIQ), and Visual Analog Scale (VAS), were also applied. PAPS patients and controls were similar in mean age as well as in distributions of gender and Caucasian race. Mean disease duration was 5.4 ± 4.2 years. A diagnosis of fibromyalgia was made in five (16.7%) PAPS patients and no controls (p = 0.012). PAPS patients had more diffuse pain (53% vs. 0%, respectively, p < 0.0001), ≥11 tender points (23% vs. 5%, respectively, p = 0.032), and a greater total number (175 vs. 57, respectively, p < 0.0001) as well as median number of tender points per patient than controls (5 [0-18] vs. 0 [0-11], respectively, p < 0.0001). PAPS patients had lower values in all dimensions of the SF-36, as well as higher FIQ scores, higher BDI scores, more depression diagnoses according to BDI results, and increased VAS in comparison with controls. Analysis of PAPS patients with FM compared with those subjects without FM revealed no significant differences regarding demographic features or thrombotic or clinical events; however, PAPS patients who also had FM had lower values in SF-36 dimensions as well as higher FIQ (82.6 ± 9.6 vs. 33.6 ± 29.8, respectively, p < 0.0001) and VAS scores (6.6 ± 2.97 vs. 3.25 ± 3.11, respectively, p = 0.03). BDI scores, in contrast, were similar in both groups. In conclusion, one-fifth of PAPS patients had fibromyalgia and a low quality of life when compared with healthy subjects.

Sucking and swallowing in infants and diagnostic tools.

Preterm infants often have difficulties in learning how to suckle from the breast or how to drink from a bottle. As yet, it is unclear whether this is part of their prematurity or whether it is caused by neurological problems. Is it possible to decide on the basis of how an infant learns to suckle or drink whether it needs help and if so, what kind of help? In addition, can any predictions be made regarding the relationship between these difficulties and later neurodevelopmental outcome? We searched the literature for recent insights into the development of sucking and the factors that play a role in acquiring this skill. Our aim was to find a diagnostic tool that focuses on the readiness for feeding or that provides guidelines for interventions. At the same time, we searched for studies on the relationship between early sucking behavior and developmental outcome. It appeared that there is a great need for a reliable, user-friendly and noninvasive diagnostic tool to study sucking in preterm and full-term infants.

Tetramer formation of a variant type human transthyretin (prealbumin) produced by Escherichia coli expression system.

A variant of human transthyretin(TTR, prealbumin) with methionine for valine substitution at position 30 is a major component of amyloid fibrils found in patients of familial amyloidotic polyneuropathy(FAP) type I, an autosomal dominant genetic disease. But the molecular nature of the variant TTR has been obscure, because most of plasma TTR from FAP patients is a mixture of variant and wild type TTR and no pure preparation of the variant has been available. For this reason, we constructed a system in which the variant type TTR was efficiently synthesized. In this system, the recombinant variant TTR was first synthesized as a fusion protein with E. coli outer membrane protein A (ompA) signal peptide, processed to eliminate the signal peptide and finally secreted to the culture medium. The final concentration of the recombinant variant TTR in the medium was about 5 mg/l. SDS polyacrylamide gel electrophoresis and gel filtration analysis suggested that the recombinant variant TTR can form tetramer as seen for native one. Purification of the protein was accomplished by only two steps of chromatography.