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Characterisation of two endogenous mammalian cysteine proteinase inhibitors, bovine cystatin C and human cystatin A

Olsson, Sigrid-Lisa (1999). Characterisation of two endogenous mammalian cysteine proteinase inhibitors, bovine cystatin C and human cystatin A. Diss. (sammanfattning/summary) Sveriges lantbruksuniv., Acta Universitatis Agriculturae Sueciae. Veterinaria, 1401-6257
ISBN 91-576-5423-9
[Doctoral thesis]

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The binding of human cystatin A to papain-like proteinases was quantified with a recombinant inhibitor, expressed in E.coli. The interaction with papain and cathepsin L was strong, with K, values of 10'n-10'13 M, and rapid, with values of 3-5106 M’1*1. The binding to papain was consistent with a one-step reaction, occurring without detectable conformational changes ofeitherproteinase orinhibitor.Hie cDNA sequence of bovine cystatin C and analyses of the inhibitor isolated from cerebrospinal fluid showed that bovine cystatin C is synthesised as a preprotein with a signal peptide of 30 residues preceding the mature protein with 118 residues. In particular, the inhibitor has an N-terminal region similar to that of other family II cystatins.Recombinant bovine cystatin C with a complete N-terminal region was characterised. The general properties, as well as the affinity and kinetics of inhibition of papain and cathepsins B, H and L, were comparable with those of human cystatin C. However, some differences between the bovine and human inhibitors were observed. Most importantly, bovine cystatin C bound to cathepsin L with a four-fold higher association rate constant than the human inhibitor. The full-length bovine cystatin C bound appreciably more tightly to proteinases than the shorter forms characterised previously. Digestion with elastase indicated that these forms had arisen by cleavage of a full-length inhibitor.In-situ hybridisation with digoxigenin-labelled cRNA probes demonstrated that bovine cystatin C mRNA was heavily concentrated in the epithelial cells ofthe choroid plexus, in single cells speckled in lymphoid tissue and in Sertoli cells. Cystatin C mRNA was also present in occasional neurons and glial cells throughout the cerebrum and the cerebellum. In the submandibular gland, specific mRNA was found mainly in striated intralobular and interlobular ducts. The expression of cystatin C in brain tissue is of particular interest, as the inhibitor is involved in certain neurological diseases.

Authors/Creators:Olsson, Sigrid-Lisa
Title:Characterisation of two endogenous mammalian cysteine proteinase inhibitors, bovine cystatin C and human cystatin A
Series Name/Journal:Acta Universitatis Agriculturae Sueciae. Veterinaria
Year of publishing :1999
Number of Pages:52
Publisher:Swedish University of Agricultural Sciences
ISBN for printed version:91-576-5423-9
Publication Type:Doctoral thesis
Article category:Other scientific
Version:Published version
Full Text Status:Public
Subjects:(A) Swedish standard research categories 2011 > 3 Medical and Health Sciences > 301 Basic Medicine > Medicinal Chemistry
(A) Swedish standard research categories 2011 > 4 Agricultural Sciences > 403 Veterinary Science > Pathobiology
Keywords:cysteine proteinase, cysteine proteinase inhibitor, cystatins, bovine, cerebrospinal fluid, in-situ hybridisation, enzyme kinetics, papain, cathepsins
Permanent URL:
ID Code:28329
Faculty:VH - Faculty of Veterinary Medicine and Animal Science
Department:(VH) > Department of Veterinary Medical Chemistry
Deposited By: SLUpub Connector
Deposited On:14 Jun 2022 14:25
Metadata Last Modified:14 Jun 2022 14:37

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