Treatment of Post-biopsy Arteriovenous Fistula of a Renal Graft by Selective Embolization.

The development of an arteriovenous fistula (AVF) after renal graft biopsy is a rare complication, it is associated in most cases with spontaneous resolution. However, interventional therapies are required in some cases, to prevent graft loss. Selective embolization has been described as an alternative treatment. In the present study, we describes our experience on AVF after biopsy in kidney transplant patients, which was managed with selective embolization. From 2005 to 2015, a total of 452 kidney transplant biopsies were performed, 12 had an AVF requiring embolization. In 92% of cases, this was successful. Beforehand, mean serum creatinine levels were 2.45 mg/dL, after the procedure, that increased to 3.05, however, 3 months later, mean creatinine levels dropped to 1.85 mg/dL. Graft survival after 2 follow-up years was 72%. Our experience demonstrates that selective embolization of the AVF after kidney transplant biopsy is a safe procedure, and that transplant function can be maintained in patients with this complication.

The Murcia Twin Registry: a population-based registry of adult multiples in Spain.

The Murcia Twin Registry (MTR) was created in 2006, under the auspices of the University of Murcia and the regional Health Authority, aiming to develop a research resource in Spain intended to stimulate current research and new investigation on the analysis of genetic factors related to health and health-related behaviors. The MTR development strategy was designed as a step-by-step process. Initially, it was focused on women's health but nowadays it includes males and opposite-sex twins. The database comprises 2,281 participants born between 1940 and 1966 in the region of Murcia, in Spain. There have been three waves of data collection and today the MTR databases include questionnaire and anthropometric data as well as biological samples. The current main areas of research interest are health and health-related behaviors, including lifestyle, health promotion, and quality of life. Future short-term development points to the completion of the biobank and continuing the collection of longitudinal data.

Production in Escherichia coli of a recombinant C-terminal truncated precursor of surfactant protein B (rproSP-B Delta C). Structure and interaction with lipid interfaces.

SP-B, a protein absolutely required to maintain the lungs open after birth, is synthesized in the pneumocytes as a precursor containing C-terminal and N-terminal domains flanking the mature sequence. These flanking-domains are cleaved to produce mature SP-B, coupled with its assembly into pulmonary surfactant lipid-protein complexes. In the present work we have optimized over-expression in Escherichia coli and purification of rproSP-B(DeltaC), a recombinant form of human proSP-B lacking the C-terminal flanking peptide, which is still competent to restore SP-B function in vivo. rProSP-B(DeltaC) has been solubilized, purified and refolded from bacterial inclusion bodies in amounts of about 4 mg per L of culture. Electrophoretic mobility, immunoreactivity, N-terminal sequencing and peptide fingerprinting all confirmed that the purified protein had the expected mass and sequence. Once refolded, the protein was soluble in aqueous buffers. Circular dichroism and fluorescence emission spectra of bacterial rproSP-B(DeltaC) indicated that the protein is properly folded, showing around 32% alpha-helix and a mainly hydrophobic environment of its tryptophan residues. Presence of zwitterionic or anionic phospholipids vesicles caused changes in the fluorescence emission properties of rproSP-B(DeltaC) that were indicative of lipid-protein interaction. The association of this SP-B precursor with membranes suggests an intrinsic amphipathic character of the protein, which spontaneously adsorbs at air-liquid interfaces either in the absence or in the presence of phospholipids. The analysis of the structure and properties of recombinant proSP-B(DeltaC) in surfactant-relevant environments will open new perspectives on the investigation of the mechanisms of lipid and protein assembly in surfactant complexes.