Cystatin A, a mammalian cysteine proteinase inhibitor
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Cystatin A, a mammalian cysteine proteinase inhibitor mechanism of inhibition of target proteinases by recombinant cystatin A variants by Sergio Estrada

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Published by Sveriges Lantbruksuniversitet in Uppsala .
Written in English

Subjects:

  • Cysteine proteinases.,
  • Proteinase.,
  • Recombinant proteins.

Book details:

Edition Notes

Series of papers combined to form a doctoral thesis for the Swedish University of Agricultural Sciences, Uppsala.

StatementSergio Estrada.
SeriesActa Universitatis Agriculturae Sueciae -- 39
ContributionsSveriges Lantbruksuniversitet.
The Physical Object
Paginationvarious pagings :
ID Numbers
Open LibraryOL22415766M
ISBN 109157654484

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Cystatins are the thiol Proteinase inhibitors, present ubiquitously in mammalian body. They prevent unwanted proteolysis and play important role in several diseases. Regulation of cysteine Proteinase and their inhibitors is of utmost importance in neurodegenerative diseases like Alzheimer, amyloid a Cited by: 1. The cystatins are a family of cysteine protease inhibitors which share a sequence homology and a common tertiary structure of an alpha helix lying on top of an anti-parallel beta sheet. The family is subdivided as described below. Cystatins show similarity to fetuins, kininogens, histidine-rich glycoproteins and cystatin-related proteins. Cystatins mainly inhibit peptidase enzymes (another InterPro: IPR Cystatins belong to a large superfamily of cysteine protease inhibitors. They generally contain – amino acids, and their fold is composed of a five-stranded β sheet and an α helix that is packed orthogonally onto the β strands. 42 The substrate binding sites of cystatins are highly conserved and located in β hairpin loops that connect strands 2 and 3 (site I) and 4 and 5 (site II. The cystatin superfamily of proteins, derived from a common ancestor, is comprised of a diverse group of potent cysteine proteinase inhibitors and antibacterial/viral agents grouped into several families.

Cystatin A (acid cysteine proteinase inhibitor; ACPI) is a natural inhibitor of cysteine proteinases. It has been suggested that an inverse correlation exists between cystatin A and malignant progression. We wanted to assess the biological and clinical significance of cystatin A in infiltrative breast carcinoma by immunohistochemical staining. Formalin-fixed paraffin-embedded material from Cystatin protease inhibitors and immune functions Article Literature Review (PDF Available) in Frontiers in Bioscience 13(12) February with Reads How we measure 'reads'. Cystatin S: a cysteine proteinase inhibitor of human saliva. Isemura S, Saitoh E, Ito S, Isemura M, Sanada K. An acidic protein of human saliva, which we named SAP-1 previously, is now shown to be an inhibitor of several cysteine proteinases. The protein inhibited papain and ficin strongly, and stem bromelain and bovine cathepsin C partially. Cystatin A (acid cysteine proteinase inhibitor; ACPI) is a natural inhibitor of cysteine proteinases. It has been suggested that an inverse correlation exists between cystatin A and malignant progression. We wanted to assess the biological and clinical significance of cystatin A in infiltrative breast carcinoma by immunohistochemical staining. For.

Cystatin-C is a small protein ( aminoacid, kDa), a cysteine proteinase inhibitor, product of a “housekeeping” gene expressed in all nuclear cells. 6 Cystatine-C has many characteristics of an ideal marker of renal function, it has constant rate of production and is freely filtrated by the glomerulus. 6,7 Although it is not secreted by. In mammalian cells cystatin M may target any of the lysosomal cathepsins B, L, H, and S or an unidentified cysteine proteinase with papain-like activity. Unlike serine proteases, cystatins do not bind covalently to target proteinases but rather block their active site and display a broad specificity. Cysteine proteinase inhibitor Cystatin A in breast cancer Article (PDF Available) in Cancer Research 58(3) March with 65 Reads How we measure 'reads'. At least for lysosomal cathepsins of mammalian cells, there are indications that their activity is regulated by endogenous cysteine protease inhibitors from the cystatin superfamily (Rawlings and Barrett, ). For example, cystatin C regulates cell surface expression of MHC class II molecules in dendritic cells (Pierre and Mellman, ).