In:
Journal of Histochemistry & Cytochemistry, SAGE Publications, Vol. 60, No. 3 ( 2012-03), p. 205-218
Abstract:
CDC50 proteins are β-subunits for P4 ATPases, which upon heterodimerization form a functional phospholipid translocation complex. Emerging evidence in mouse models and men links mutations in P4 ATPase genes with human disease. This study analyzed the tissue distribution and cellular localization of CDC50A, the most abundant and ubiquitously expressed CDC50 homologue in the mouse. The authors have raised antibodies that detect mouse and human CDC50A and studied CDC50A localization and glycosylation status in mouse liver cells. CDC50A is a terminal-glycosylated glycoprotein and is expressed in hepatocytes and liver sinusoidal endothelial cells, where it resides in detergent-resistant membranes. In pancreas and stomach, CDC50A localized to secretory vesicles, whereas in the kidney, CDC50A localized to the apical region of proximal convoluted tubules of the cortex. In WIF-B9 cells, CDC50A partially costains with the trans-Golgi network. Data suggest that CDC50A is present as a fully glycosylated protein in vivo, which presumes interaction with distinct P4 ATPases.
Type of Medium:
Online Resource
ISSN:
0022-1554
,
1551-5044
DOI:
10.1369/0022155411435705
Language:
English
Publisher:
SAGE Publications
Publication Date:
2012
detail.hit.zdb_id:
1421306-0
SSG:
12