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Background Prescription drug abuse in the United States and elsewhere in the world is increasing at an alarming rate with non-medical opioid use, in particular, increasing to epidemic proportions over the past two decades. It is imperative to identify those most likely to develop opioid abuse or dependence to inform large-scale, targeted prevention efforts. Methods The present investigation utilized a large commercial insurance claims database to identify demographic, mental health, physical health, and healthcare service utilization variables that differentiate persons who receive an opioid abuse or dependence diagnosis within two years of filling an opioid prescription (OUDs) from those who do not receive such a diagnosis within the same time frame (non-OUDs). Results When compared to non-OUDs, OUDs were more likely to: 1) be male (59.9% vs. 44.2% for non-OUDs) and younger (M=37.9 vs. 47.7); 2) have a prescription history of more opioids (1.7 vs. 1.2), and more days supply of opioids (M=272.5, vs. M=33.2; 3) have prescriptions filled at more pharmacies (M=3.3 per year vs. M=1.3); 4) have greater rates of psychiatric disorders; 5) utilize more medical and psychiatric services; and 6) be prescribed more concomitant medications. A predictive model incorporating these findings was 79.5% concordant with actual OUDs in the data set. Conclusions Understanding correlates of OUD development can help to predict risk and inform prevention efforts.

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Saccharomyces cerevssiae strain FH4C carries a single invertase structural gene, SUC2, but produces distinct invertase mRNAs'and polypeptides for the secreted and cytoplasmic forms ofthe enzyme. The two major invertase cell-free translation products are polypeptides of 60,000 daltons (p60) and 62,000 daltons (p62) and correspond to the nonglycosylated cytoplasmic form of invertase and the precursor of glycosylated secreted invertase, respectively. This paper describes amino acid sequence and peptide map analyses of invertase polypeptides. The peptide maps demonstrate that p62, p60, and the in vivo secreted polypeptide have significant structural homology. Sequence analysis, however, revealed differences between p62 and p60 at their amino termini. p62 contains an amino-terminal signal sequence of 19 amino acid residues that is specifically cleaved during secretion in a cell-free system to generate the secreted 87,000-dalton invertase glycopeptide gp87. This signal sequence is not present in p60. p60 synthesis begins with a methionine which can be aligned with a methionine at residue 21 in p62. During translation, the p60 initiator methionine is removed and the newly generated amino terminus is acetylated. Based on peptide map similarities, partial amino-terminal sequence data, and common genetic origin, it is suggested that p60 and p62 have identical amino acid sequences carboxy-terminal to the p60 initiator methionine (residue 21 of p62). The reciprocal correlations ofsignal sequence with secretion and absence of signal sequence with cytoplasmic localization provide proof of the signal hypothesis for secreted proteins. Two mechanisms are proposed for the derivation ofp60 and p62 from a single structural gene: alternative promoter sites, and differential processing of a single primary transcript.Sucrose-fermenting yeast strains carrying one or more SUC genes synthesize two forms ofthe enzyme invertase, a secreted glycoprotein and a cytoplasmic form containing no carbohydrate (1). The polypeptide portions of these two forms are encoded by a single structural gene but are synthesized from distinct mRNAs (2). These invertase mRNA species direct the synthesis of three polypeptides: 63,000 daltons (p63), 62,000 daltons (p62), and 60,000 daltons (p60). When synthesized in cell-free systems containing microsomal membranes, the major product, p62, is glycosylated to yield an 87,000-dalton glycopeptide (gp87) and is rendered insensitive to exogenous proteolytic degradation (membrane-sequestered). The structure of the core carbohydrate and size of the polypeptide moiety, 60,000 daltons, of this glycopeptide are similar to those of the in vivo secreted enzyme (2,3). In contrast, the p60 invertase polypeptide is not membrane-sequestered or glycosylated when cell-free synthesis is conducted in the presence of microsomal membranes. These findings indicate that p62 represents a precursor of secreted invertase whereas p60 corresponds to cytoplasmic invertase (2).Although differing in size and capacity for membrane proces...