| pubmed-article:8725720 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8725720 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8725720 | lifeskim:mentions | umls-concept:C0229304 | lld:lifeskim |
| pubmed-article:8725720 | lifeskim:mentions | umls-concept:C0072348 | lld:lifeskim |
| pubmed-article:8725720 | lifeskim:mentions | umls-concept:C1148608 | lld:lifeskim |
| pubmed-article:8725720 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8725720 | pubmed:dateCreated | 1997-1-21 | lld:pubmed |
| pubmed-article:8725720 | pubmed:abstractText | Interactions between proteins and heparin(-like) structures involve electrostatic forces and structural features. Based on charge distributions in the linear sequence of protein C inhibitor (PCI), two positively charged regions of PCI were proposed as possible candidates for this interaction. The first region, the A+ helix, is located at the N-terminus (residues 1-11), whereas the second region, the H helix, is positioned between residues 264 and 280 of PCI. Competition experiments with synthetic peptides based on the sequence of these regions demonstrated that the H helix has the highest affinity for heparin. In contrast to previous observations we found that the A+ helix peptide competed for the interaction of PCI with heparin, but its affinity was much lower than that of the H helix peptide. Recombinant PCI was also used to investigate the role of the A+ helix in heparin binding. Full-length (wild-type) rPCI as well as an A+ helix deletion mutant of PCI (rPCI-delta 2-11) were expressed in baby hamster kidney cells and both had normal inhibition activity with activated protein C and thrombin. The interaction of the recombinant PCIs with heparin was investigated and compared to plasma PCI. The A+ helix deletion mutant showed a decreased affinity for heparin in inhibition reactions with activated protein C and thrombin, but had similar association constants compared to wild-type rPCI. The synthetic A+ helix peptide competed with rPCI-delta w-11 for binding to heparin. This indicated that the interaction between PCI and heparin is fairly non-specific and that the interaction is primarily based on electrostatic interactions. In summary, our data suggest that the H helix of PCI is the main heparin binding region of PCI, but the A+ helix increases the overall affinity for the PCI-heparin interaction by contributing a second positively charged region to the surface of PCI. | lld:pubmed |
| pubmed-article:8725720 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8725720 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8725720 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8725720 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8725720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8725720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8725720 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8725720 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8725720 | pubmed:month | May | lld:pubmed |
| pubmed-article:8725720 | pubmed:issn | 0340-6245 | lld:pubmed |
| pubmed-article:8725720 | pubmed:author | pubmed-author:BoumaB NBN | lld:pubmed |
| pubmed-article:8725720 | pubmed:author | pubmed-author:ChurchF CFC | lld:pubmed |
| pubmed-article:8725720 | pubmed:author | pubmed-author:MeijersJ CJC | lld:pubmed |
| pubmed-article:8725720 | pubmed:author | pubmed-author:ElisenM GMG | lld:pubmed |
| pubmed-article:8725720 | pubmed:author | pubmed-author:MaselandM HMH | lld:pubmed |
| pubmed-article:8725720 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8725720 | pubmed:volume | 75 | lld:pubmed |
| pubmed-article:8725720 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8725720 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8725720 | pubmed:pagination | 760-6 | lld:pubmed |
| pubmed-article:8725720 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8725720 | pubmed:meshHeading | pubmed-meshheading:8725720-... | lld:pubmed |
| pubmed-article:8725720 | pubmed:meshHeading | pubmed-meshheading:8725720-... | lld:pubmed |
| pubmed-article:8725720 | pubmed:meshHeading | pubmed-meshheading:8725720-... | lld:pubmed |
| pubmed-article:8725720 | pubmed:meshHeading | pubmed-meshheading:8725720-... | lld:pubmed |
| pubmed-article:8725720 | pubmed:meshHeading | pubmed-meshheading:8725720-... | lld:pubmed |
| pubmed-article:8725720 | pubmed:meshHeading | pubmed-meshheading:8725720-... | lld:pubmed |
| pubmed-article:8725720 | pubmed:meshHeading | pubmed-meshheading:8725720-... | lld:pubmed |
| pubmed-article:8725720 | pubmed:meshHeading | pubmed-meshheading:8725720-... | lld:pubmed |
| pubmed-article:8725720 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8725720 | pubmed:articleTitle | Role of the A+ helix in heparin binding to protein C inhibitor. | lld:pubmed |
| pubmed-article:8725720 | pubmed:affiliation | Department of Haematology, University Hospital, Utrecht, The Netherlands. | lld:pubmed |
| pubmed-article:8725720 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8725720 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8725720 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8725720 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8725720 | lld:pubmed |
