ABSTRACT
The translationally controlled tumor-associated proteins (TCTPs) are a highly conserved and abundantly expressed family of eukaryotic proteins that are implicated in both cell growth and the human acute allergic response but whose intracellular biochemical function has remained elusive. We report here the solution structure of the TCTP from Schizosaccharomyces pombe, which, on the basis of sequence homology, defines the fold of the entire family. We show that TCTPs form a structural superfamily with the Mss4/Dss4 family of proteins, which bind to the GDP/GTP free form of Rab proteins (members of the Ras superfamily) and have been termed guanine nucleotide-free chaperones (GFCs). Mss4 also acts as a relatively inefficient guanine nucleotide exchange factor (GEF). We further show that the Rab protein binding site on Mss4 coincides with the region of highest sequence conservation in the TCTP family. This is the first link to any other family of proteins that has been established for the TCTP family and suggests the presence of a GFC/GEF at extremely high abundance in eukaryotic cells.
Subject(s)
Biomarkers, Tumor , Conserved Sequence , Lymphokines/chemistry , Molecular Chaperones/chemistry , Proteins/chemistry , Schizosaccharomyces/chemistry , Amino Acid Motifs , Amino Acid Sequence , Binding Sites , Fungal Proteins/chemistry , Guanine Nucleotide Exchange Factors/chemistry , Guanine Nucleotide Exchange Factors/metabolism , Guanosine Diphosphate/metabolism , Guanosine Triphosphate/metabolism , Humans , Models, Molecular , Molecular Chaperones/metabolism , Molecular Sequence Data , Nuclear Magnetic Resonance, Biomolecular , Protein Structure, Secondary , Proteins/metabolism , Sequence Alignment , Tumor Protein, Translationally-Controlled 1 , rab GTP-Binding Proteins/metabolismABSTRACT
Thousands of health care providers spend time, money, and energy each year taking the AHA-sponsored ACLS courses, and ACLS-certified health care providers are frequently given greater job responsibility than other health care providers in the same setting. The purpose of this study was to determine the effect of an ACLS course on the ability of health care providers to perform ACLS in a simulated situation. A nonequivalent control group design was used. The sample consisted of 76 health care providers whose job responsibilities included ACLS. The Mega-Code skill station from the ACLS course was used to evaluate ACLS performance. Chi-square analyses showed a significant (p less than 0.05) difference in the posttest pass/fail results of the two groups and a significant (p less than 0.05) difference in the changes from pretest to posttest of the two groups. The research hypotheses were supported, and the researches concluded that the course had a positive effect on the subjects' ACLS ability.
Subject(s)
Health Occupations/education , Heart Arrest/therapy , Life Support Care , Resuscitation , Clinical Competence , Education, Continuing , Female , Humans , Male , Teaching/methodsABSTRACT
The composition of serum seromucoid, the protein fraction of serum not precipitated by 0.6 M perchloric acid, has been shown to vary with the technique of preparation. Immunochemical examination revealed that 91.5% of the protein present in the seromucoid fraction of serum was alpha 1 acid glycoprotein, the remainder consisting of alpha 1 antitrypsin, alpha 1 antichymotrypsin, beta 2 glycoprotein, haemopexin, albumin, and pre-albumin. Serum alpha 1 acid glycoprotein concentration determined by radial immunodiffusion correlated well with serum seromucoid concentration although the former was usually 0.4 g/l lower. The determination of serum alpha 1 acid glycoprotein by an immunological method is more precise than the seromucoid method and is not subject to interference from other proteins.
