The place of human gamma-trace (cystatin C) amongst the cysteine proteinase inhibitors
Barrett, Alan ; Davies, ME and Grubb, Anders LU
(1984)
In Biochemical and Biophysical Research Communications
120.
p.631-636
- Abstract
- Native γ-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 γ-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... (More)
- Native γ-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 γ-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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/eea63c10-2875-47cd-b3b6-674a23f142b4
- author
- Barrett, Alan
; Davies, ME
and Grubb, Anders
LU
- organization
- publishing date
- 1984
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemical and Biophysical Research Communications
- volume
- 120
- pages
- 631 - 636
- publisher
- Elsevier
- external identifiers
-
- scopus:0021236724
- ISSN
- 1090-2104
- DOI
- 10.1016/0006-291X(84)91302-0
- language
- English
- LU publication?
- yes
- id
- eea63c10-2875-47cd-b3b6-674a23f142b4
- date added to LUP
- 2018-11-16 16:31:30
- date last changed
- 2023-03-15 09:53:53
@article{eea63c10-2875-47cd-b3b6-674a23f142b4,
abstract = {{Native γ-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 γ-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.}},
author = {{Barrett, Alan and Davies, ME and Grubb, Anders}},
issn = {{1090-2104}},
language = {{eng}},
pages = {{631--636}},
publisher = {{Elsevier}},
series = {{Biochemical and Biophysical Research Communications}},
title = {{The place of human gamma-trace (cystatin C) amongst the cysteine proteinase inhibitors}},
url = {{http://dx.doi.org/10.1016/0006-291X(84)91302-0}},
doi = {{10.1016/0006-291X(84)91302-0}},
volume = {{120}},
year = {{1984}},
}