The relationship between the MAOA-uVNTR polymorphism, delinquent peer affiliation, and antisocial behavior with a consideration of sex differences

Psychiatr Q. 2018 Dec;89(4):841-853. doi: 10.1007/s11126-018-9582-7.

Abstract

With the advent of new and more readily usable gene sequencing techniques, researchers have been able to examine the interactions between genes and the environment (G X E) within a multitude of scientific perspectives. One area that G X E interactions have been implicated in is the development of antisocial behavior (ASB). Antisocial behavior consists of a wide range of maladaptive behaviors and has been at the forefront of public health and mental health concerns for decades. One genetic polymorphism that has been associated with ASB is MAOA-uVNTR. Meta-analytic studies have found the low-activity MAOA-uVNTR polymorphism to be associated with ASB from early childhood through adulthood. Recently, studies have begun to examine the independent and interactive G X E relationship between MAOA-uVNTR and deviant peer affiliation on ASB. Inconsistent with the broader literature, these findings suggest an interaction between high-activity MAOA-uVNTR and deviant peer affiliation on ASB in a mixed sex sample. The current study re-examines the relationship between MAOA-uVNTR, peer delinquency, and ASB with a consideration of sex differences in 291 college participants. Findings indicate an interaction between the low-activity allele of the MAOA-uVNTR and peer delinquency in predicting ASB. Results are also specific to differences between the sexes. Implications and future research are discussed.

Keywords: Antisocial behavior; G X E; MAOA; Peer delinquency; Sex differences.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Female
  • Gene-Environment Interaction*
  • Humans
  • Juvenile Delinquency*
  • Male
  • Minisatellite Repeats
  • Monoamine Oxidase / genetics*
  • Peer Group*
  • Sex Characteristics*
  • Social Behavior*
  • Young Adult

Substances

  • Monoamine Oxidase
  • monoamine oxidase A, human