Accession Number : ADA456044


Title :   Role of Conserved Oligomeric Golgi Complex in the Abnormalities of Glycoprotein Processing in Breast Cancer Cells


Descriptive Note : Annual summary rept. 1 May 2003-30 Apr 2006


Corporate Author : ARKANSAS UNIV AT LITTLE ROCK


Personal Author(s) : Zolov, Sergey N


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a456044.pdf


Report Date : May 2006


Pagination or Media Count : 52


Abstract : The conserved oligomeric Golgi (COG) complex consists of eight subunits that are thought to be involved in vesicle tethering. Available mutants with the mutations in COG complex subunits exhibit defects in basic Golgi functions: protein glycosylation and its sorting. For analysis of COG complex function we utilized RNA interference assay to knockdown COG3p subunit of COG complex in normal and breast cancer cells and other tumor cell lines. Acute knockdown of the COG3 was accompanied by reduction in Cogi 2 and 4 protein levels rapid Golgi fragmentation and accumulation of COG complex dependent (CCD) vesicles. Constantly cycling medial-Golgi enzymes are transported from distal compartments in CCD vesicles. Dysfunction of COG complex leads to separation of glycosyltransferases from anterograde cargo molecules passing along secretory pathway thus affecting normal protein glycosylation. Altered level of COG3p (or COG complex) expression could be a common feature of cancer cells defective in protein trafficking and Golgi modifications. The importance of the COG complex for both function and architecture of the Golgi apparatus does not depend on cell type. Partial malfunction of the COG complex may play a role in establishing of cancer phenotype.


Descriptors :   *GLYCOPROTEINS , *OLIGOMERS , NEOPLASMS , MUTATIONS , GLYCOSIDES , BREAST CANCER , CELL STRUCTURE , CELLS(BIOLOGY) , RIBONUCLEIC ACIDS


Subject Categories : Medicine and Medical Research


Distribution Statement : APPROVED FOR PUBLIC RELEASE