Proteolytic processing of chemokines: implications in physiological and pathological conditions

Wolf, Marlene; Albrecht, Stefan; Märki, Christa (2008). Proteolytic processing of chemokines: implications in physiological and pathological conditions. International journal of biochemistry & cell biology, 40(6-7), pp. 1185-98. Amsterdam: Elsevier 10.1016/j.biocel.2007.12.009

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Chemokines are small, secreted proteins that orchestrate the migration of cells, which are involved in immune defence, immune surveillance and haematopoiesis. However, chemokines are also implicated in the pathology of various inflammatory diseases, cancers and HIV. The chemokine system is considerably large and has a redundancy in the repertoire of its inflammatory mediators. Therefore, strict regulation of chemokine activity is crucial. Chemokines are the substrate for various proteases including the serine protease CD26/dipeptidyl-peptidase IV and matrix metalloproteinases. Regulation by proteolytic cleavage controls and fine-tunes chemokine function by either enhancing or reducing its chemotactic activity or receptor selectivity. Often chemokines and the proteases that regulate them are produced in the same microenvironment and expression of both may be simultaneously induced by a common stimulus enabling the rapid regulation of chemokine activity. The overall impact of cleaved chemokines in cellular responses is very complex. In this review, we will give an overview on chemokine modification and the respective chemokine modifying proteases. Furthermore, we will summarize the emerging literature describing the consequences in inflammation, haematopoiesis, cancer and HIV infection upon proteolytic chemokine processing.

Item Type:

Journal Article (Further Contribution)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Theodor Kocher Institute

UniBE Contributor:

Wolf, Marlene; Albrecht, Stefan and Märki, Christa

ISSN:

1357-2725

ISBN:

18243768

Publisher:

Elsevier

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:55

Last Modified:

04 May 2014 23:16

Publisher DOI:

10.1016/j.biocel.2007.12.009

PubMed ID:

18243768

Web of Science ID:

000256493300012

URI:

https://boris.unibe.ch/id/eprint/23663 (FactScience: 43340)

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