Xylosylation of alternatively spliced isoforms of Alzheimer APP by xylosyltransferase

J Protein Chem. 1998 Apr;17(3):295-302. doi: 10.1023/a:1022549121672.

Abstract

Acceptor affinities of UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase (XT) recognition signals in synthetic L-APP and L-APLP2 homologous peptides were determined. The Michaelis-Menten constants (KM) of the L-APP peptide TENEGSGLTNIK and the L-APLP2 peptide SENEGSGMAEQK were 20.1 and 18.9 microM, respectively. Therefore, the peptides proved to be as good acceptors for XT as the bikunin aminoterminus homologous peptide (KM = 22 microM). Due to the occurrence of L-APP and L-APLP2 transcripts in human brain tissue, XT activity was measured in human liquor cerebrospinalis. Mean values were calculated as 0.22 mU/L in males and 0.47 mU/L in females without disturbance of blood brain barrier. In addition, in homogenized rat brain tissue a mean XT activity of 0.75 mU/L was determined. Furthermore, XT activity was investigated in 21 different human cell lines. In 7 cell lines an enzyme activity was not detected in either extracellular space or cytoplasma. Our findings indicate that XT is not ubiquitously expressed in human cell types.

MeSH terms

  • Alternative Splicing
  • Alzheimer Disease*
  • Amyloid beta-Protein Precursor / genetics
  • Amyloid beta-Protein Precursor / metabolism*
  • Animals
  • Brain / enzymology*
  • Cell Line
  • Female
  • Humans
  • Male
  • Pentosyltransferases / blood
  • Pentosyltransferases / metabolism*
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / chemistry*
  • Rats
  • Rats, Inbred Lew
  • UDP Xylose-Protein Xylosyltransferase

Substances

  • Amyloid beta-Protein Precursor
  • Peptide Fragments
  • Pentosyltransferases