Initial validation of a virtual blood draw exposure paradigm for fear of blood and needles.

Fear of blood, injections, and needles commonly prevents or delays individuals' receipt of health care, such as vaccines or blood draws. Innovative methods are needed to overcome these fears and reduce anxiety related to activities of this nature. The present study describes initial testing of an arm illusion paradigm that may prove useful during early phases of graded exposure for people with blood and needle fear. Seventy-four undergraduate students aged 18-29 years were tested. In line with study aims, results indicated that the virtual blood draw paradigm promoted strong perceptions of arm ownership and elicited significant changes in physiological indices (blood pressure, heart rate, electrodermal activity, respiratory rate) in response to key procedure elements (e.g., needle insertion). Further, bivariate correlations indicated that individual differences in self-reported blood and needle fear collected prior to the illusion paradigm were significantly associated with presyncopal symptoms reported following the procedure. In regression analyses, self-reported measures of blood and needle fear explained unique variance in presyncopal symptoms even after controlling for general state anxiety. These findings provide initial support for the virtual blood draw paradigm as a promising tool to help provide graded exposure to medical procedures involving needles and blood draw.

Single amino acid substitutions can convert the uncleaved signal-anchor of sucrase-isomaltase to a cleaved signal sequence.

A hydrophobic segment near the amino terminus (positions 12-32) of rabbit sucrase-isomaltase functions both as a membrane anchor and as a signal sequence for translocation into the endoplasmic reticulum. Unlike most signal sequences, that of sucrase-isomaltase is not cleaved by signal peptidase. Using in vitro transcription and translation systems, we have found that substitution of a single proline, at position 28 or 29, converted the signal-anchor to a cleaved signal sequence, with cleavage occurring after alanine 26 and the introduced proline thereby occupying position +2 or +3 relative to the cleavage site. Two deletions that shorten the transmembrane domain by 8 amino acids were also effective, whereas various other changes upstream and downstream of this domain were without effect. We conclude that susceptibility to mammalian signal peptidase is influenced both by the length of the hydrophobic region and by the secondary structure downstream of the cleavage site.

Isolation and characterization of a Saccharomyces cerevisiae mutant disrupted for the succinate dehydrogenase flavoprotein subunit.

A partial genomic clone of the flavoprotein subunit of the mitochondrial enzyme, succinate dehydrogenase (EC 1.3.99.1) from Saccharomyces cerevisiae has been isolated. The partial clone was used to construct, by targeted gene disruption, a yeast mutant with a defective flavoprotein subunit gene. Submitochondrial membranes from the mutant are defective in activities requiring a functional succinate dehydrogenase but not in other respiratory chain activities. In addition, the mutant contains significantly lower levels of covalently attached flavin adenine dinucleotide cofactor than does the wild type. Disruption of the flavoprotein subunit gene results in the simultaneous loss of both the iron-sulfur and the flavoprotein subunits from mitochondrial membranes.