title: Selective activation of N-acyl-D-glucosamine 2-epimerase expression in failing human heart ventricular myocytes.
abstract: BACKGROUND
  O-linked N-acyl-glycosylation may regulate protein function by competing with phosphorylation of serine residues. Availability of substrate for this process is regulated, in part, by N-Acyl-D-glucosamine 2-epimerase (NAGE), which interconverts N-acetyl-glucosamine (GlcNAc) and N-acetylmannosamine (ManNAc). NAGE is also a putative renin-binding protein. This study tested the hypothesis that NAGE is present in the human heart and that NAGE expression is increased in the failing human heart.
  
  
  RESULTS
  Ribonuclease protection assays (RPAs) demonstrated increased NAGE gene expression in failing hearts from subjects with idiopathic dilated and ischemic cardiomyopathies compared with nonfailing hearts. In situ reverse transcriptase-polymerase chain reaction, using primers designed to localize NAGE mRNA, demonstrated that, in nonfailing hearts, NAGE gene expression was restricted to endothelial cells and not detectable in cardiac myocytes. However, in failing human hearts NAGE gene expression was selectively activated in cardiac myocytes, but not endothelial cells. Immunohistochemistry confirmed that the pattern of NAGE protein expression corresponded to the pattern of gene expression.
  
  
  CONCLUSIONS
  NAGE gene and protein expression were selectively activated in left ventricular myocytes from end-stage failing human hearts.
authors.affiliation: The Heart Institute, Albany Medical College, Albany, New York 12208, USA.
authors.forename: Teresa
authors.initials: T
authors.lastname: Bohlmeyer
authors.forename: Anthony
authors.initials: A
authors.lastname: Ferdensi
authors.forename: Michael R
authors.initials: MR
authors.lastname: Bristow
authors.forename: Saori
authors.initials: S
authors.lastname: Takahashi
authors.forename: Lawrence S
authors.initials: LS
authors.lastname: Zisman
mesh_terms: D000293:Adolescent; D000328:Adult; D002238:Carbohydrate Epimerases / Q000096:biosynthesis* / Q000235:genetics; D002311:Cardiomyopathy, Dilated / Q000378:metabolism*; D002352:Carrier Proteins / Q000096:biosynthesis* / Q000235:genetics; D004789:Enzyme Activation / Q000502:physiology; D005260:Female; D015971:Gene Expression Regulation, Enzymologic / Q000235:genetics; D014644:Genetic Variation / Q000235:genetics; D006352:Heart Ventricles / Q000166:cytology / Q000378:metabolism; D006801:Humans; D017379:Hypertrophy, Left Ventricular / Q000378:metabolism; D007150:Immunohistochemistry; D008297:Male; D008875:Middle Aged; D017202:Myocardial Ischemia / Q000378:metabolism; D032383:Myocytes, Cardiac / Q000201:enzymology; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013223:Statistics as Topic; D018487:Ventricular Dysfunction, Left / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D012333:RNA, Messenger; D002238:Carbohydrate Epimerases; C024519:N-acyl-D-glucosamine 2-epimerase; C498259:RENBP protein, human