Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
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Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
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Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
Hypoxia / reoxygenation induced the expression of CyPA and its cell surface receptor CD 147 on cardiac myocytes in vitro . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
We recently identified CD 147 as the main signaling receptor for cyclophilin A . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
However , other functions of emmprin , including as an activator of T cells , a chaperone for monocarboxylate transporters , a receptor for cyclophilin A and a neural recognition molecule , are also being identified in physiological and pathological conditions . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
Bsg is also involved in inflammatory processes and is proposed to be a receptor of cyclophilin A ; it is also likely to participate in HIV infection . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
CD 147 facilitates HIV 1 infection by interacting with virus associated cyclophilin A . ^^^ Our preliminary studies implicated CD 147 as a receptor for extracellular CyPA . ^^^ Here , we demonstrate a role for CyPA CD 147 interaction during the early steps of HIV 1 infection . ^^^ However , susceptibility to infection by viruses lacking CyPA ( simian immunodeficiency virus or HIV 1 produced in the presence of cyclosporin A ) was unaffected by CD 147 . ^^^ Virus associated CyPA coimmunoprecipitated with CD 147 from infected cells . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
We recently identified CD 147 as a cell surface receptor for CyPA and demonstrated that CD 147 is an essential component in the CyPA initiated signaling cascade that culminates in ERK activation and chemotaxis . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
Active site residues of cyclophilin A are crucial for its signaling activity via CD 147 . ^^^ Here , we identified CD 147 as a cell surface receptor for CyPA and demonstrated that CD 147 is an essential component in the CyPA initiated signaling cascade that culminates in ERK activation . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
A limited inhibition of attachment was observed when interfering with putative interactions with cellular heparan sulfate , whereas no effect was observed for cellular CD 147 or nucleolin or for virion incorporated cyclophilin A . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
Solution binding experiments demonstrated that the transmembrane domain was both necessary and sufficient for CD 147 binding to cyclophilin A ( CypA ) . ^^^ Peptide binding studies demonstrated specific interaction between CypA and the proline containing peptide from the CD 147 transmembrane domain . ^^^ Mutation of this proline residue reduced binding of CD 147 derived peptides to CypA and also diminished transport of CD 147 to the plasma membrane without reducing the total level of CD 147 expression . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
The mRNA levels of 13 genes including CD 147 ( receptor for CypA ) , PDGF BB , endothelin 1 ( ET 1 ) , vascular endothelial growth factor receptor 1 ( VEGFR 1 ) , VEGFR 2 , VEGFR 3 , neuropilin 1 ( NRP 1 ) , NRP 2 , eNOS , iNOS , nNOS , ICAM 1 , and PECAM 1 were semiquantitatively determined by real time RT PCR as standardized with a house keeping gene beta actin . ^^^ Blocking CD 147 did not affect the mitogenic action of CypA . ^^^ In addition , CypA also significantly increased the mRNA expression of CD 147 by 43 % and VEGFR 2 by 65 % in HAoSMCs ( P < 0 . 05 , t test ) . ^^^ CD 147 may not mediate the action of CypA . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
This interaction with Cyp 60 involved proline 211 of CD 147 , which was shown previously to be critical for interaction between CD 147 and another cyclophilin , cyclophilin A , in solution . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
The potential role of CD 147 in cyclophilin A ( CyPA ) mediated cell migration was studied using a chemotaxis assay in vitro and it was found that the addition of anti CD 147 antibody or a CD 147 antagonistic peptide significantly decreased the chemotactic index of the mononuclear cells . ^^^ Our study demonstrates that the increased expression of CD 147 on monocytes / macrophages in RA may be responsible for elevated MMP secretion , cell invasion and CyPA mediated cell migration into the joints , all of which may contribute to the cartilage and bone destruction of RA . ^^^ These findings , together with a better understanding of CD 147 , CyPA and RA , will help in the development of innovative therapeutic interventions for RA . . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
BACKGROUND : We previously found that cyclophilin A ( CypA ) is overexpressed in human pancreatic cancer cells and stimulates cell proliferation through CD 147 . ^^^ The messenger RNA ( mRNA ) levels of CypA , CypB , CD 147 , neuropilins ( NRPs ) , vascular endothelial growth factor ( VEGF ) , and VEGF receptors upon the treatment of exogenous recombinant human CypA were determined by real time reverse transcription polymerase chain reaction . ^^^ RESULTS : Exogenous human recombinant CypA reduced the mRNA levels of NRP 1 and VEGF , but not endogenous CypA , CypB , and CD 147 , in Panc 1 , MIA PaCa 2 , and BxPC 3 cells . ^^^ In contrast , HPDE cells showed a decrease of endogenous CypA and CD 147 mRNA , but not detectable changes of CypB , NRPs , and VEGF mRNA levels upon exogenous CypA treatment . ^^^
Interacting proteins: P35613 and P62937 Pubmed SVM Score :0.0
Cyclophilin A is overexpressed in human pancreatic cancer cells and stimulates cell proliferation through CD 147 . ^^^ In this study the expression of CypA and its receptor CD 147 on pancreatic cancer was determined as well as the effect of exogenous CypA on pancreatic cancer cell proliferation . ^^^ METHODS : The expression of CypA and CD 147 in human pancreatic cancer cell lines and tissues was determined with real time reverse transcriptase polymerase chain reaction ( RT PCR ) , Western blot , and immunostaining . ^^^ RESULTS : Pancreatic cancer cell lines expressed significantly higher levels of CypA and CD 147 than normal human pancreatic ductal epithelium ( HPDE ) cells . ^^^ Expression of CypA and CD 147 was also substantially higher in human pancreatic adenocarcinoma tissues than those in normal pancreatic tissues . ^^^