The place of human γ-trace (cystatin C) amongst the cysteine proteinase inhibitors
Abstract
Native gamma-trace, a small basic protein present in high concentration in cerebrospinal fluid, semen and neuroendocrine cells, but of unknown biological function, is shown to be a potent inhibitor of the cysteine proteinases papain, ficin, and human cathepsins B, H and L. It proves to be the tightest -binding protein inhibitor of cathepsin B so far discovered. The name cystatin C is proposed for gamma-trace to reflect the many similarities in activity and structure to chicken egg-white cystatin and mammalian cystatins A and B. The inhibition constants of cystatin C, taken together with its widespread distribution in human tissues and extracellular fluids, suggest that a physiological function could well be the regulation of cysteine proteinase activity.
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CyC is biologically active as a potent cysteine protease inhibitor.
“CyC is biologically active as a potent cysteine protease inhibitor,74”
From Cystatin C is glucocorticoid responsive, directs recruitment of Trem2+ macrophages, and predicts failure of cancer immunotherapy (2023) · cites this paper as [74]
CyC levels are highest in cerebrospinal and seminal fluid.
“CyC levels are highest in cerebrospinal and seminal fluid,74”
From Cystatin C is glucocorticoid responsive, directs recruitment of Trem2+ macrophages, and predicts failure of cancer immunotherapy (2023) · cites this paper as [74]
CyC is a known potent inhibitor of cysteine proteases, such as those involved in antigen presentation.
“CyC is a known potent inhibitor of cysteine proteases,74 such as those involved in antigen presentation,75”
From Cystatin C is glucocorticoid responsive, directs recruitment of Trem2+ macrophages, and predicts failure of cancer immunotherapy (2023) · cites this paper as [74]
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- Authors
- Barrett, A. J., Davies, M. E., & Grubb, A.
- Affiliations
- University of Cambridge (GB)
- Lund University (SE)
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 1984-04
- Volume
- 120
- Issue
- 2
- Pages
- 631-636
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W1984079474
- Cited by
- 294
- References
- 28
- Citations by year
- 2025: 3 · 2024: 7 · 2023: 4 · 2022: 1 · 2021: 5 · 2020: 1 · 2019: 4 · 2018: 3 · 2017: 4 · 2016: 4 · 2015: 8 · 2014: 9 · 2013: 12 · 2012: 2
- FWCI
- 8.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- cystatin C, cysteine protease inhibitors, papain, ficin, cathepsin B, cathepsin H, cathepsin L, tight-binding inhibition, cerebrospinal fluid, cystatin A, cystatin B
- MeSH terms
- Epitopes, Cathepsins, Drug Stability, Ficain, Humans, Kinetics, Papain, Protease Inhibitors, Proteins, Cystatins, Cystatin C
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