Xylosylation of alternatively spliced isoforms of Alzheimer APP by xylosyltransferase

被引:18
作者
Götting, C [1 ]
Kuhn, J [1 ]
Brinkmann, T [1 ]
Kleesiek, K [1 ]
机构
[1] Ruhr Univ Bochum, Univ Klin, Herz & Diabet Zentrum Nordrhein Westfalen, Inst Lab & Transfus Med, D-32545 Bad Oeynhausen, Germany
来源
JOURNAL OF PROTEIN CHEMISTRY | 1998年 / 17卷 / 03期
关键词
xylosyltransferase; beta A4-amyloid protein precursor; amyloid precursor-like protein 2; chondroitin sulfate glycosaminoglycan; proteoglycans;
D O I
10.1023/A:1022549121672
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 (K-M) of the L-APP peptide TENEGSGLTNIK and the L-APLP2 peptide SENEGSGMAEQK were 20.1 and 18.9 mu M, respectively. Therefore, the peptides proved to be as good accepters for XT as the bikunin aminoterminus homologous 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 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.
引用
收藏
页码:295 / 302
页数:8
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