SELF-AGGREGATION OF THE TRANSMEMBRANE GLYCOPROTEIN CD38 PURIFIED FROMHUMAN ERYTHROCYTES

Citation
L. Franco et al., SELF-AGGREGATION OF THE TRANSMEMBRANE GLYCOPROTEIN CD38 PURIFIED FROMHUMAN ERYTHROCYTES, Biochemical and biophysical research communications, 202(3), 1994, pp. 1710-1715
Citations number
19
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006291X
Volume
202
Issue
3
Year of publication
1994
Pages
1710 - 1715
Database
ISI
SICI code
0006-291X(1994)202:3<1710:SOTTGC>2.0.ZU;2-B
Abstract
The 46 kDa human transmembrane glycoprotein CD38 is a multicatalytic e nzyme exhibiting ADPribosyl cyclase, cyclic ADPribose hydrolase and NA D(+)-glycohydrolase activities at its extracellular domain. When CD38, purified to homogeneity from human erythrocyte membranes, was incubat ed with NAD(+) or beta-mercaptoethanol, extensive aggregation took pla ce. Addition of both compounds to CD38 led to the formation of still l arger aggregates (over 300 nm), which were resistant to TCA precipitat ion. Extensive and stable CD38 self-aggregation was shown by, i) SDS-P AGE and autoradiography of the [P-32]NAD(+)-incubated CD38, ii) SDS-PA GE followed by immunochemical detection of CD38 on the transblots, iii ) direct electron microscopy on negatively stained CD38 samples. Self- aggregation of CD38 might be correlated with its putative function as a transducer of activation and proliferation signals in a number of he matopoietic cells. (C) 1994 Academic Press, Inc.