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CTSH  -  cathepsin H

Bos taurus

 
 
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High impact information on CTSH

  • Activities of cathepsin B and L, but not cathepsin H, increase during bovine myogenic differentiation [1].
  • Reaction with 2,2'-dipyridyl disulphide in acidic media, which is known to provide a rapid spectrophotometric active centre titration for many cysteine proteinases, is applicable to cathepsin H [2].
  • The considerable differences in catalytic site characteristics detected by this two-protonic-state reactivity probe between cathepsin B, cathepsin H, papain (EC 3.4.22.2) and actinidin (EC 3.4.22.14) are discussed [2].
  • Cathepsin H appeared to prefer cleaving at the NH2-terminal side of basic residues [3].
  • They could however be distinguished by the fact that cathepsin S reacted with Z-[125I]Tyr-Ala-CHN2 and hydrolyzed Z-Phe-Arg-NHMec whereas cathepsin H did not [4].
 

Biological context of CTSH

  • Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4 [2].
  • Neither of the recombinant variants inhibited bovine cathepsin B. Our data supply evidence indicating that the amino acid sequence of the first hairpin loop of the cystatin superfamily is important in the inhibition of papain, ficin, cathepsin C, cathepsin H, and cathepsin K [5].
  • The binding kinetics could only be evaluated for papain and cathepsin H and showed that the reduced affinities for these enzymes were predominantly due to increased dissociation rate constants [6].
 

Associations of CTSH with chemical compounds

  • Cathepsin H Arg-4-methyl-7-coumarylamide hydrolyzing activity was low and not significantly affected by cimaterol treatment [7].
 

Other interactions of CTSH

 

Analytical, diagnostic and therapeutic context of CTSH

  • This is useful because other active-centre titrations have proved unsuitable in view of the relatively low reactivity of the thiol group in cathepsin H [2].

References

  1. Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. Characterization of a cDNA encoding bovine cathepsin B. Béchet, D.M., Ferrara, M.J., Mordier, S.B., Roux, M.P., Deval, C.D., Obled, A. J. Biol. Chem. (1991) [Pubmed]
  2. Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4. Willenbrock, F., Brocklehurst, K. Biochem. J. (1985) [Pubmed]
  3. Distinct properties of prohormone thiol protease (PTP) compared to cathepsins B, L, and H: evidence for PTP as a novel cysteine protease. Azaryan, A.V., Hook, V.Y. Arch. Biochem. Biophys. (1994) [Pubmed]
  4. The specificity and elastinolytic activities of bovine cathepsins S and H. Xin, X.Q., Gunesekera, B., Mason, R.W. Arch. Biochem. Biophys. (1992) [Pubmed]
  5. Production and characterization of two variants of human cystatin SA encoded by two alleles at the CST2 locus of the type 2 cystatin gene family. Saitoh, E., Minaguchi, K., Ishibashi, O. Arch. Biochem. Biophys. (1998) [Pubmed]
  6. Contributions of individual residues in the N-terminal region of cystatin B (stefin B) to inhibition of cysteine proteinases. Pol, E., Björk, I. Biochim. Biophys. Acta (2003) [Pubmed]
  7. Cimaterol reduces cathepsin activities but has no anabolic effect in cultured myotubes. Béchet, D.M., Listrat, A., Deval, C., Ferrara, M., Quirke, J.F. Am. J. Physiol. (1990) [Pubmed]
  8. Human and bovine brain cathepsin L and cathepsin H: purification, physico-chemical properties, and specificity. Azaryan, A., Galoyan, A. Neurochem. Res. (1987) [Pubmed]
 
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