Zinc as a modulator of transglutaminase activity - Laboratory and pathophysiological aspects
(2021) In Journal of Translational Autoimmunity 4.- Abstract
For a whole century, citrate has been used as an in vitro anticoagulant via chelation of calcium. Later, also EDTA was introduced as an anticoagulant. An often overlooked fact is that zinc is bound to citrate and EDTA with affinities much greater than that for calcium, imposing problems in biomedical research. In vivo, proteins of the S100 family are released from leukocytes and known to bind calcium. Some of them, e.g., calprotectin, also chelate zinc. Thus, at an inflamed site, the ratio between Ca2+ and Zn2+ is changed. This mechanism is of importance for the modulation of the activation of a fascinating family of post-translationally acting calcium-dependent thiol enzymes, the transglutaminases, which are inhibited by zinc. This... (More)
For a whole century, citrate has been used as an in vitro anticoagulant via chelation of calcium. Later, also EDTA was introduced as an anticoagulant. An often overlooked fact is that zinc is bound to citrate and EDTA with affinities much greater than that for calcium, imposing problems in biomedical research. In vivo, proteins of the S100 family are released from leukocytes and known to bind calcium. Some of them, e.g., calprotectin, also chelate zinc. Thus, at an inflamed site, the ratio between Ca2+ and Zn2+ is changed. This mechanism is of importance for the modulation of the activation of a fascinating family of post-translationally acting calcium-dependent thiol enzymes, the transglutaminases, which are inhibited by zinc. This presentation illustrates the complexity of in vitro studies with zinc. Moreover, it exemplifies the role of Zn2+ in pathophysiological situations such as celiac disease and neurodegeneration.
(Less)
- author
- Stenberg, Pål LU ; Roth, Bodil LU and Ohlsson, Bodil LU
- organization
- publishing date
- 2021
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Translational Autoimmunity
- volume
- 4
- article number
- 100110
- publisher
- Elsevier
- external identifiers
-
- scopus:85109109217
- pmid:34195588
- ISSN
- 2589-9090
- DOI
- 10.1016/j.jtauto.2021.100110
- language
- English
- LU publication?
- yes
- id
- 8f5edabb-8bc4-44ad-a563-5d8b4dcd05d2
- date added to LUP
- 2021-08-11 09:51:59
- date last changed
- 2024-03-23 07:23:29
@article{8f5edabb-8bc4-44ad-a563-5d8b4dcd05d2,
abstract = {{<p>For a whole century, citrate has been used as an in vitro anticoagulant via chelation of calcium. Later, also EDTA was introduced as an anticoagulant. An often overlooked fact is that zinc is bound to citrate and EDTA with affinities much greater than that for calcium, imposing problems in biomedical research. In vivo, proteins of the S100 family are released from leukocytes and known to bind calcium. Some of them, e.g., calprotectin, also chelate zinc. Thus, at an inflamed site, the ratio between Ca2+ and Zn2+ is changed. This mechanism is of importance for the modulation of the activation of a fascinating family of post-translationally acting calcium-dependent thiol enzymes, the transglutaminases, which are inhibited by zinc. This presentation illustrates the complexity of in vitro studies with zinc. Moreover, it exemplifies the role of Zn2+ in pathophysiological situations such as celiac disease and neurodegeneration.</p>}},
author = {{Stenberg, Pål and Roth, Bodil and Ohlsson, Bodil}},
issn = {{2589-9090}},
language = {{eng}},
publisher = {{Elsevier}},
series = {{Journal of Translational Autoimmunity}},
title = {{Zinc as a modulator of transglutaminase activity - Laboratory and pathophysiological aspects}},
url = {{http://dx.doi.org/10.1016/j.jtauto.2021.100110}},
doi = {{10.1016/j.jtauto.2021.100110}},
volume = {{4}},
year = {{2021}},
}