title: Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes.
abstract: A strong induction of semicarbazide-sensitive amine oxidase (SSAO) has previously been reported during murine preadipocyte lineage differentiation but it remains unknown whether this emergence also occurs during adipogenesis in man. Our aim was to compare SSAO and monoamine oxidase (MAO) expression during in vitro differentiation of human preadipocytes and in adipose and stroma-vascular fractions of human fat depots. A human preadipocyte cell strain from a patient with Simpson-Golabi-Behmel syndrome was first used to follow amine oxidase expression during in vitro differentiation. Then, human preadipocytes isolated from subcutaneous adipose tissues were cultured under conditions promoting ex vivo adipose differentiation and tested for MAO and SSAO expression. Lastly, human adipose tissue was separated into mature adipocyte and stroma-vascular fractions for analyses of MAO and SSAO at mRNA, protein and activity levels. Both SSAO and MAO were increased from undifferentiated preadipocytes to lipid-laden cells in all the models: 3T3-F442A and 3T3-L1 murine lineages, human SGBS cell strain or human preadipocytes in primary culture. In human subcutaneous adipose tissue, the adipocyte-enriched fraction exhibited seven-fold higher amine oxidase activity and contained three- to seven-fold higher levels of mRNAs encoded by MAO-A, MAO-B, AOC3 and AOC2 genes than the stroma-vascular fraction. MAO-A and AOC3 genes accounted for the majority of their respective MAO and SSAO activities in human adipose tissue. Most of the SSAO and MAO found in adipose tissue originated from mature adipocytes. Although the mechanism and role of adipogenesis-related increase in amine oxidase expression remain to be established, the resulting elevated levels of amine oxidase activities found in human adipocytes may be of potential interest for therapeutic intervention in obesity.
authors.affiliation: U858 INSERM, I2MR, IFR 31, CHU Rangueil, BP 84225, 31432 Toulouse Cedex 4, France.
authors.forename: Sandy
authors.initials: S
authors.lastname: Bour
authors.forename: Danièle
authors.initials: D
authors.lastname: Daviaud
authors.forename: Sandra
authors.initials: S
authors.lastname: Gres
authors.forename: Corinne
authors.initials: C
authors.lastname: Lefort
authors.forename: Danielle
authors.initials: D
authors.lastname: Prévot
authors.forename: Antonio
authors.initials: A
authors.lastname: Zorzano
authors.forename: Martin
authors.initials: M
authors.lastname: Wabitsch
authors.forename: Jean-Sébastien
authors.initials: JS
authors.lastname: Saulnier-Blache
authors.forename: Philippe
authors.initials: P
authors.lastname: Valet
authors.forename: Christian
authors.initials: C
authors.lastname: Carpéné
mesh_terms: D016475:3T3 Cells; D041721:3T3-L1 Cells; D017667:Adipocytes / Q000201:enzymology* / Q000378:metabolism; D050156:Adipogenesis; D000328:Adult; D006631:Amine Oxidase (Copper-Containing) / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D002454:Cell Differentiation / Q000235:genetics; D019070:Cell Lineage; D005260:Female; D006801:Humans; D007223:Infant; D051379:Mice; D008875:Middle Aged; D008995:Monoamine Oxidase / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism
chemical_list: D012333:RNA, Messenger; D006631:Amine Oxidase (Copper-Containing); D008995:Monoamine Oxidase