CABP2 IS A RAT HOMOLOG OF ERP72 WITH PROTEINDISULFIDE ISOMERASE ACTIVITY

被引:45
作者
VAN, PN [1 ]
RUPP, K [1 ]
LAMPEN, A [1 ]
SOLING, HD [1 ]
机构
[1] UNIV GOTTINGEN, ZENTRUM INNERE MED, KLIN BIOCHEM ABT, ROBERT KOCH STR 40, W-3400 GOTTINGEN, GERMANY
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1993年 / 213卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1993.tb17821.x
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
Ca-binding protein 2 (CaBP2) has been described previously as an intracisternal calcium-binding microsomal glycoprotein [1]. We report now the primary sequence of this protein as deduced from the corresponding cDNA. The protein possesses a C-terminal -KEEL retention sequence and three repeats of the thioredoxin-like motive -EFYAPNCGHCK-, and represents the rat homolog of ERp72 [2]. In contrast to earlier reports on ERp72, CaBP2 possesses significant proteindisulfide isomerase activity. Furthermore, in contrast to ERp72, CaBP2 is a glycoporotein containing O-linked glycans. The amount of CaBP2 in H-35 Reuber hepatoma cells increases in parallel with that of immunoglobin heavy-chain-binding protein under conditions which lead to impaired glycosylation, while the amount of calreticulin, another KDEL-containing glycoprotein, remains almost unchanged.
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页码:789 / 795
页数:7
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