Cholesterol and steroid synthesizing smooth endoplasmic reticulum of adrenocortical cells contains high levels of translocation apparatus proteins Journal Article
| Authors: | Black, V. H.; Sanjay, A.; Van Leyen, K.; Möeller, I.; Lauring, B.; Kreibich, G. |
| Article Title: | Cholesterol and steroid synthesizing smooth endoplasmic reticulum of adrenocortical cells contains high levels of translocation apparatus proteins |
| Abstract: | Steroid-secreting cells possess abundant smooth endoplasmic reticulum whose membranes contain many enzymes involved in sterol and steroid synthesis. In this. study we demonstrate that adrenal smooth microsomal subfractions enriched in these membranes also possess high levels of proteins belonging to the translocation apparatus, proteins previously assumed to be confined to morphologically identifiable rough endoplasmic reticulum (RER). We further demonstrate that these smooth microsomal subfractions are capable of effecting the functions of these protein complexes: co-translational translocation, signal peptide cleavage and N-glycosylation of newly synthesized polypeptides. We hypothesize that these elements participate in regulating the levels of ER-targeted membrane proteins involved in cholesterol and steroid metabolism in a sterol-dependent and hormonally-regulated manner. |
| Keywords: | controlled study; carrier protein; nonhuman; conference paper; protein function; animals; animal tissue; protein degradation; cell protein; membrane proteins; steroid; endoplasmic reticulum; protein synthesis; dogs; signal peptide; rat; glycosylation; translocation, genetic; cholesterol; rats; cell level; adrenal cortex cell; transferases; steroids; steroidogenesis; rough endoplasmic reticulum; guinea pigs; cholesterol synthesis; microsome; smooth endoplasmic reticulum; adrenal cortex; microsomes; priority journal; hexosyltransferases |
| Journal Title: | Endocrine Research |
| Volume: | 28 |
| Issue: | 4 |
| ISSN: | 0743-5800 |
| Publisher: | Informa Healthcare |
| Date Published: | 2002-01-01 |
| Start Page: | 425 |
| End Page: | 430 |
| Language: | English |
| DOI: | 10.1081/erc-120016818 |
| PUBMED: | 12530645 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 14 November 2014 -- Source: Scopus |
