| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| Using Western ligand blotting and SDS PAGE analysis of fragmentation patterns of 125I labelled IGFBP 3 and 125 labelled IGFBP 1 , we have examined conditioned media from cultured human cell lines for the presence of proteolytic activity and compared this with the action of circulating proteases and with characterized enzymes including cathepsin D , kallikrein , plasmin and tissue plasminogen activator . 125I Labelled IGFBP 3 was incubated with serum from pregnant women , patients following heart surgery and patients with cancer of the breast , lung or head / neck . ^^^ |
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| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| The cell derived IGFBP 3 protease was identified as the aspartic proteinase cathepsin D , based on acidic pH optimum , inhibition by pepstatin , distinctive proteolytic fragment pattern , and immunoreactivity with cathepsin D antisera . ^^^ Furthermore , immuno depletion of cathepsin D effectively attenuated acid activated IGFBP 3 proteolysis . ^^^ These data suggest a role for cathepsin D in the regulation of cellular IGF action by virtue of its potential to alter the structure / function of IGFBP 3 . . ^^^ |
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| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| In this study , we have measured PSA , IGF 1 , IGF 2 , IGFBP 1 and IGFBP 3 in tumour tissue cytosols from 200 women with primary breast cancer , and have examined relationships between IGFs or IGFBPs and PSA along with other markers , including p 53 protein , steroid hormone receptors ( oestrogen and progesterone ) , cathepsin D , epidermal growth factor receptor , Her 2 / neu protein , S phase fraction and DNA ploidy . ^^^ |
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| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| Additionally , purified cathepsin D yielded a digestion pattern identical to that produced by prostatic cell CM and seminal plasma , following acidic incubation with IGFBP 3 . ^^^ |
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| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| In this study , we report on the in vitro degradation of IGFs and IGFBPs by the purified acidic aspartylprotease cathepsin D that has been shown to proteolyze IGFBP 3 . ^^^ By N terminal sequence analysis of nonglycosylated IGFBP 3 fragments produced by cathepsin D , at least four different cleavage sites were identified . ^^^ The IGFBP 3 and 4 cleavage sites produced by cathepsin D are located in the nonconserved central region . ^^^ |
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| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| Thus , a role of cathepsin D for the regulation of IGFBP 3 bioavailability via endocytosis in acidic prelysosomal compartments was suggested . ^^^ |
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| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| Fibroblasts derived from double mutant mice missort the lysosomal protease cathepsin D , and are able to degrade endocytosed ( 125I ) IGFBP 3 intracellularly , however , with lower efficiency than in control cells . ^^^ |
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| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| Expression levels of IGFBP 3 , an IGF 2 carrier protein , metalloproteinase 2 and cathepsin D were also increased to 200 , 340 , and 310 % of control levels , respectively . ^^^ |
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| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P07339 and P17936 |
Pubmed |
SVM Score :0.0 |
| NA |
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