Characterization of TG2 and TG1-TG2 double knock-out mouse epidermis.

Transglutaminases (TGs) are a family of enzymes that catalyse the formation of isopeptide bonds between the γ-carboxamide groups of glutamine residues and the ε-amino groups of lysine residues leading to cross-linking reactions among proteins. Four members, TG1, TG2, TG3, and TG5, of the nine mammalian enzymes are expressed in the skin. TG1, TG3 and TG5 crosslinking properties are fundamental for cornified envelope assembly.

Attachment style predict compliance, quality of life and renal function in adult patients after kidney transplant: preliminary results.

Aim: Aim of this study was to evaluate the association between attachment style, compliance, quality of life and renal function in adult patients after kidney transplantation.

Methods: A total of 43 adult patients who received a kidney transplant more than 3 months before were enrolled and were asked to complete two Self-Report questionnaires: Attachment Style Questionnaire (ASQ-40) and Short Form Health Survey (SF-36). Also compliance was measured using appropriate questions.

Emotional self-efficacy and alexithymia may affect compliance, renal function and quality of life in kidney transplant recipients: results from a preliminary cross-sectional study.

Unlabelled: Recent studies show that alexithymia may influence compliance and quality of life in different clinical situations. The aim of this study was to evaluate the associations between alexithymia or emotional self-efficacy and compliance, quality of life (QoL) and renal function in renal transplant patients.

Methods: Forty-three patients were enrolled during a follow-up visit (>3 months post-transplant) and were asked to complete three self-report questionnaires (TAS-20, SF-36, RESE) to answer the following items: "In the past four weeks, how many times did you fail to take your prescribed dose?" and "How would you rate your adherence levels from 0 to 100?" (visual analogue scale).

Inactive and highly active, proteolytically processed transglutaminase-5 in epithelial cells.

Transglutaminases (TGs) are Ca(2+)-dependent enzymes capable of catalyzing transamidation of glutamine residues to form intermolecular isopeptide bonds. These enzymes are involved in various biological phenomena, including blood coagulation, wound healing, cell death, tissue repair, and terminal differentiation of keratinocytes. Among the TG-family members, TG5 is one of the latest identified enzymes and therefore the less characterized at the functional level.

Dominant and recessive COL6A1 mutations in Ullrich scleroatonic muscular dystrophy.

In this study, we characterized five Ullrich scleroatonic muscular dystrophy patients (two Italians, one Belgian, and two Turks) with a clinical phenotype showing different degrees of severity, all carrying mutations localized in COL6A1. We sequenced the three entire COL6 complementary DNA. Three of five patients have recessive mutations: two patients (P1and P3) have homozygous single-nucleotide deletions, one in exon 9 and one in exon 22; one patient (P2) has a homozygous single-nucleotide substitution leading to a premature termination codon in exon 31.

Transglutaminase 5 is regulated by guanine-adenine nucleotides.

Transglutaminases (TGases) are Ca2+-dependent enzymes capable of catalysing transamidation of glutamine residues to form intermolecular isopeptide bonds. Nine distinct TGases have been described in mammals, and two of them (types 2 and 3) are regulated by GTP/ATP. TGase2 hydrolyses GTP and is therefore a bifunctional enzyme.