C. Gotting et al., XYLOSYLATION OF ALTERNATIVELY SPLICED ISOFORMS OF ALZHEIMER APP BY XYLOSYLTRANSFERASE, Journal of protein chemistry, 17(3), 1998, pp. 295-302
Acceptor affinities of UDP-D-xylose:proteoglycan core protein beta-D-x
ylosyltransferase (XT) recognition signals in synthetic L-APP and L-AP
LP2 homologous peptides were determined. The Michaelis-Menten constant
s (K-M) of the L-APP peptide TENEGSGLTNIK and the L-APLP2 peptide SENE
GSGMAEQK were 20.1 and 18.9 mu M, respectively. Therefore, the peptide
s proved to be as good accepters for XT as the bikunin aminoterminus h
omologous peptide (K-M = 22 mu M). 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 activ
ity of 0.75 mU/L was determined. Furthermore, XT activity was investig
ated in 21 different human cell lines. In 7 cell lines an enzyme activ
ity was not detected in either extracellular space or cytoplasma. Our
findings indicate that XT is not ubiquitously expressed in human cell
types.