ASU Scholarship Showcase

The current study examined heterogeneity in emerging adult children's routine and self-disclosure to parents using mixture modeling and explored predictors and outcomes associated with the patterns of disclosure. Participants consisted of 449 emerging adults (49% male, 68% European American, 65% college students, 33% single-parent families) who completed questionnaires every year across three waves (Mage at Time 1 = 18.4 years). Latent profile analyses suggested that large groups of emerging adults reported moderate levels of routine disclosure and low levels of self-disclosure to both mothers (79%) and fathers (36%), while other groups (20%) reported high levels of routine and self-disclosure to both parents. Profile membership was associated with predictors (parental autonomy granting, self-disclosure to friend, gender, family structure, college attendance) at Time 1 and outcomes (delinquency, depression, and prosocial behavior) at Time 3. Implications regarding the continued parent-child relationship and disclosure to parents in the third decade of life are discussed.

Background: Cysteine sulfenic acid (Cys-SOH) plays important roles in the redox regulation of numerous proteins. As a relatively unstable posttranslational protein modification it is difficult to quantify the degree to which any particular protein is modified by Cys-SOH within a complex biological environment. The goal of these studies was to move a step beyond detection and into the relative quantification of Cys-SOH within specific proteins found in a complex biological setting--namely, human plasma.

Results: This report describes the possibilities and limitations of performing such analyses based on the use of thionitrobenzoic acid and dimedone-based probes which are commonly employed to trap Cys-SOH. Results obtained by electrospray ionization-based mass spectrometric immunoassay reveal the optimal type of probe for such analyses as well as the reproducible relative quantification of Cys-SOH within albumin and transthyretin extracted from human plasma--the latter as a protein previously unknown to be modified by Cys-SOH.

Conclusions: The relative quantification of Cys-SOH within specific proteins in a complex biological setting can be accomplished, but several analytical precautions related to trapping, detecting, and quantifying Cys-SOH must be taken into account prior to pursuing its study in such matrices.