Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase.

@article{Abrahamson1991HumanCC,
  title={Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase.},
  author={M. Abrahamson and R. Mason and H. Hansson and D. Buttle and A. Grubb and K. Ohlsson},
  journal={The Biochemical journal},
  year={1991},
  volume={273 ( Pt 3)},
  pages={
          621-6
        }
}
Leucocyte elastase in catalytic amounts was observed to rapidly cleave the Val-10-Gly-11 bond of the human cysteine-proteinase inhibitor cystatin C at neutral pH. The resulting modified inhibitor had size and amino acid composition consistent with a cystatin C molecule devoid of the N-terminal Ser-1-Val-10 decapeptide. Leucocyte-elastase-modified cystatin C had more than 240-fold lower affinity than native cystatin C for papain. Removal of the N-terminal decapeptide of human cystatin C also… Expand
Cathepsin L is capable of truncating cystatin C of 11 N‐terminal amino acids
TLDR
N‐terminal sequencing after separation by HPLC showed that cystatin C is cleaved by cathepsin L at the Gly11‐Gly12 bond, which may be explained by the cleavage of the scissile bond in an inappropriate complex. Expand
Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases
  • E. Pol, I. Björk
  • Chemistry, Medicine
  • Protein science : a publication of the Protein Society
  • 2001
TLDR
Cys 3 of both human and bovine cystatin B is of appreciable importance for inhibition of cysteine proteinases, in particular cathepsin B. Expand
The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C.
TLDR
The properties of recombinant, full-length bovine cystatin C having a complete N-terminal region are reported and the affinity and kinetics of inhibition of papain and cathepsins B, H and L by thebovine inhibitor were comparable with those of the human inhibitor, although certain differences were apparent. Expand
Contributions of individual residues in the N-terminal region of cystatin B (stefin B) to inhibition of cysteine proteinases.
TLDR
It is demonstrated that the N-terminal region of cystatin B contributes appreciably to proteinase inhibition, in contrast to previous proposals, and is responsible for 12-40% of the total binding energy of the inhibitor to the proteinases investigated. Expand
The role of the second binding loop of the cysteine protease inhibitor, cystatin A (stefin A), in stabilizing complexes with target proteases is exerted predominantly by Leu73.
TLDR
Results show that the second binding loop of cystatin A plays a major role in stabilizing the complexes with proteases by retarding their dissociation. Expand
Mechanism of action of mammalian cystatins Studies of inhibition of cysteine endo- and exopeptidases by cystatins A and C
Pavlova, A., 2003. Mechanism of action of mammalian cystatins. Studies of inhibition of cysteine endoand exopeptidases by cystatins A and C. Doctor's dissertation. ISSN 1401-6257, ISBN 91-576-6379-3.Expand
Molecular cloning and N-terminal analysis of bovine cystatin C. Identification of a full-length N-terminal region.
TLDR
Results show that bovine cystatin C has 118 residues, in contrast with 110-112 residues reported previously, and has an N-terminal region analogous to that of human cyStatin C, which presumably is of similar importance for tight binding of target proteinases as in the human inhibitor. Expand
Mechanism of action of mammalian cystatins
TLDR
The N-terminal region of a cystatin was concluded to promote occluding loop displacement by appropriately positioning the binding loops of the inhibitor entering the active-site cleft of cathepsin B. Expand
Human cystatin A is inactivated by engineered truncation. The NH2-terminal region of the cysteine proteinase inhibitor is essential for expression of its inhibitory activity.
TLDR
The amino-terminal region of cystatin A is essential for the expression of its inhibitory activity and was found to cause changes in the chemical shifts of Val47 and Val48, which locate on a first loop and consist of a conservative QVVAG sequence. Expand
Elongation on the amino-terminal part of stefin B decreases inhibition of cathepsin H.
TLDR
It is suggested that reduced binding of stefins with elongated amino termini is caused by the mini chain of cathepsin H which is probably in close proximity to the aminotermini in the complexes. Expand
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