| pubmed-article:1921761 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0035366 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0344315 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0021080 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0017278 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0021079 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0596873 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C1422036 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0127400 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:1921761 | lifeskim:mentions | umls-concept:C0597551 | lld:lifeskim |
| pubmed-article:1921761 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:1921761 | pubmed:dateCreated | 1991-11-14 | lld:pubmed |
| pubmed-article:1921761 | pubmed:abstractText | CKS-17, an immunosuppressive peptide homologous to certain retroviral transmembrane envelope protein, has been shown to inhibit lymphocyte proliferation in response to mitogens or alloantigens when covalently attached to bovine serum albumin (CKS-17-BSA). To define its site of action, we determined if CKS-17 conjugated to human serum albumin (CKS-17-HSA) could block the direct activation of lymphocytes by phorbol-12-myristate-13-acetate (PMA) or by a synthetic diacylglycerol, dioctanoylglycerol (DiC8). CKS-17-HSA inhibited lymphocyte proliferation in response to PMA and ionomycin in a dose-dependent manner with up to 88% inhibition occurring with 15 microM CKS-17-HSA. The conjugated peptide also inhibited the proliferation of lymphocytes in response to DiC8 and ionomycin by up to 57% at 15 microM CKS-17-HSA. Based on these findings we investigated the effect of CKS-17-HSA on the activity of protein kinase C (PKC), an enzyme directly activated by PMA and DiC8. PKC was isolated chromatographically from the cytosol of human neutrophils or the human lymphoblastoid cell line Jurkat. CKS-17-HSA caused a dose-dependent enzyme inhibition with a concentration giving half-maximal inhibition (IC50) of ca.3 microM and greater than 95% inhibition at 15 microM CKS-17-HSA. Inhibition of PKC by the conjugated peptide was not reversed by increasing concentrations of Ca2+, Mg2+, phosphatidylserine, diolein, or adenosine triphosphate (ATP), indicating that the conjugated peptide did not function as a chelator or competitive inhibitor. In contrast to its effects on PKC, CKS-17-HSA did not inhibit the activity of adenosine 3':5'-cyclic monophosphate (cyclic AMP)-dependent protein kinase (PK-A) nor the calcium and phospholipid-independent form of PKC (PK-M). Moreover the peptide inhibited in vivo PKC activity in cytosol of intact cells and in membrane of PMA-stimulated cells. These results suggest that the inhibition of lymphocyte proliferation by CKS-17-HSA may be due to the direct inactivation of PKC. | lld:pubmed |
| pubmed-article:1921761 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1921761 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1921761 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1921761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1921761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1921761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1921761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1921761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1921761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1921761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1921761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1921761 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1921761 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1921761 | pubmed:issn | 0385-5600 | lld:pubmed |
| pubmed-article:1921761 | pubmed:author | pubmed-author:SnydermanRR | lld:pubmed |
| pubmed-article:1921761 | pubmed:author | pubmed-author:CiancioloG... | lld:pubmed |
| pubmed-article:1921761 | pubmed:author | pubmed-author:KadotaJJ | lld:pubmed |
| pubmed-article:1921761 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1921761 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:1921761 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1921761 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1921761 | pubmed:pagination | 443-59 | lld:pubmed |
| pubmed-article:1921761 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:meshHeading | pubmed-meshheading:1921761-... | lld:pubmed |
| pubmed-article:1921761 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1921761 | pubmed:articleTitle | A synthetic peptide homologous to retroviral transmembrane envelope proteins depresses protein kinase C mediated lymphocyte proliferation and directly inactivated protein kinase C: a potential mechanism for immunosuppression. | lld:pubmed |
| pubmed-article:1921761 | pubmed:affiliation | Second Department of Internal Medicine, Nagasaki University School of Medicine. | lld:pubmed |
| pubmed-article:1921761 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1921761 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1921761 | lld:pubmed |
