1998
DOI: 10.1046/j.1432-1327.1998.2510472.x
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Abstract: Plasminogen contains a unique disulphide bond, Cys558 Cys566, responsible for the cyclic nature of the peptide sequence surrounding the activation site at Arg561-Val562. A recombinant [Ser558, Ser566]-Lys78-plasminogen variant was produced in which the two cysteine residues were replaced by serine residues. The variant was used to study the functional implications of removing the structural restrains imposed to the activation loop by this disulphide bond. Elimination of the Cys558 Cys566 bond attenuated activa… Show more

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Cited by 15 publications
(8 citation statements)
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“…Cys558-Cys566 stabilizes the activation loop ( Fig. 1B ) and it has been proposed that it has a role in its recognition by uPA, tPA and fibrin [ 72 ]. Furthermore, it has been proposed that the disulphide bond Cys558-Cys566 may be important for the enzymatic specificity of plasminogen [ 4 ].…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Cys558-Cys566 stabilizes the activation loop ( Fig. 1B ) and it has been proposed that it has a role in its recognition by uPA, tPA and fibrin [ 72 ]. Furthermore, it has been proposed that the disulphide bond Cys558-Cys566 may be important for the enzymatic specificity of plasminogen [ 4 ].…”
Section: Discussionmentioning
confidence: 99%
“…However, there are other Trp and Tyr residues in closer proximity to other disulphide bonds in the catalytic domain that could be more likely targets for photolysis ( Table 3 ). Furthermore, it has been proven that the activity of plasmin does not depend on the presence of the Cys558-Cys566 disulphide bond [ 72 ].…”
Section: Discussionmentioning
confidence: 99%
“…This cleavage site is located in a small disulfide‐bounded loop that must restrict the conformation around this bond. It has been shown, indeed, that this disulfide bond is of importance for the specificity of plasminogen activation 32. The sequence corresponding to this loop is comprised in the P 2 ‐P 17 / P′ 2 ‐P′ 23 sequence of plasminogen that is strictly preserved in apo(a); in contrast, the P 1 ‐P′ 1 peptide bond in apo(a) consist of Ser‐Ile instead of Arg‐Val,2 a substitution that may impair recognition by activators (Fig.…”
Section: Structural Basis For the Antifibrinolytic Activity Of Lp(a)mentioning
confidence: 99%
“…Plasminogen cleavage by plasminogen activators at residues Arg 561 -Val 562 produces plasmin, which has both proteolytic and fibrinolytic activities (13). The proteolytic activity controls activation of several important angiogenic modulators such as transforming growth factor ␤ and matrix metalloproteinase (MMP) (14,15).…”
mentioning
confidence: 99%