XYLOSYLATION OF ALTERNATIVELY SPLICED ISOFORMS OF ALZHEIMER APP BY XYLOSYLTRANSFERASE

Citation
C. Gotting et al., XYLOSYLATION OF ALTERNATIVELY SPLICED ISOFORMS OF ALZHEIMER APP BY XYLOSYLTRANSFERASE, Journal of protein chemistry, 17(3), 1998, pp. 295-302
Citations number
33
Categorie Soggetti
Biology
ISSN journal
02778033
Volume
17
Issue
3
Year of publication
1998
Pages
295 - 302
Database
ISI
SICI code
0277-8033(1998)17:3<295:XOASIO>2.0.ZU;2-5
Abstract
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.