| pubmed-article:1378326 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1378326 | lifeskim:mentions | umls-concept:C0134835 | lld:lifeskim |
| pubmed-article:1378326 | lifeskim:mentions | umls-concept:C1335809 | lld:lifeskim |
| pubmed-article:1378326 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:1378326 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:1378326 | lifeskim:mentions | umls-concept:C1159366 | lld:lifeskim |
| pubmed-article:1378326 | lifeskim:mentions | umls-concept:C1549781 | lld:lifeskim |
| pubmed-article:1378326 | lifeskim:mentions | umls-concept:C1947906 | lld:lifeskim |
| pubmed-article:1378326 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1378326 | pubmed:dateCreated | 1992-8-20 | lld:pubmed |
| pubmed-article:1378326 | pubmed:abstractText | P-selectin (CD62), formerly called GMP-140 or PADGEM, is a membrane protein located in secretory storage granules of platelets and endothelial cells. To study the mechanisms responsible for the targeting of P-selectin to storage granules, we transfected its cDNA into COS-7 and CHO-K1 cells, which lack a regulated exocytic pathway, or into AtT20 cells, which are capable of regulated secretion. P-selectin was expressed on the plasma membrane of COS-7 and CHO-K1 cells but was concentrated in storage granules of AtT20 cells. Immunogold electron microscopy indicated that the electron-dense granules containing P-selectin in AtT20 cells also stored the endogenous soluble hormone ACTH. Activation of AtT20 cells with 8-Br-cAMP increased the surface expression of P-selectin, consistent with agonist-induced fusion of granule membranes with the plasma membrane. Deletion of the last 23 amino acids of the 35-residue cytoplasmic domain resulted in delivery of P-selectin to the plasma membrane of AtT20 cells. Replacement of the cytoplasmic tail of tissue factor, a plasma membrane protein, with the cytoplasmic domain of P-selectin redirected the chimeric molecule to granules. We conclude that the cytoplasmic domain of P-selectin is both necessary and sufficient for sorting of membrane proteins into the regulated pathway of secretion. | lld:pubmed |
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| pubmed-article:1378326 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1378326 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1378326 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1378326 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1378326 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:1378326 | pubmed:author | pubmed-author:BaintonD FDF | lld:pubmed |
| pubmed-article:1378326 | pubmed:author | pubmed-author:FugateR DRD | lld:pubmed |
| pubmed-article:1378326 | pubmed:author | pubmed-author:MorrisseyJ... | lld:pubmed |
| pubmed-article:1378326 | pubmed:author | pubmed-author:McEverR PRP | lld:pubmed |
| pubmed-article:1378326 | pubmed:author | pubmed-author:DisdierMM | lld:pubmed |
| pubmed-article:1378326 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1378326 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:1378326 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1378326 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1378326 | pubmed:pagination | 309-21 | lld:pubmed |
| pubmed-article:1378326 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1378326 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1378326 | pubmed:articleTitle | Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway. | lld:pubmed |
| pubmed-article:1378326 | pubmed:affiliation | Department of Medicine, St. Francis Medical Research Institute, University of Oklahoma Health Sciences Center, Oklahoma City. | lld:pubmed |
| pubmed-article:1378326 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1378326 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1378326 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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