By the same authors

From the same journal

Multiple structural states of S100A12: A key to its functional diversity

Research output: Contribution to journalLiterature review

Published copy (DOI)

Author(s)

Department/unit(s)

Publication details

JournalMicroscopy research and technique
DatePublished - 15 Apr 2003
Issue number6
Volume60
Number of pages12
Pages (from-to)581-592
Original languageEnglish

Abstract

S100\A12 is a member of the S100 family of EF-hand calcium-binding proteins. Together with two other calgranulins, S100A8 and S100A9, it is mostly expressed in human granulocytes, although there is increasing evidence of expression in keratinocytes and psoriatic lesions. It is involved in host-parasite response, and linked to corneal autoimmune diseases connected with filarial parasite infestation. Interaction of S100A12 with a multiligand receptor for advanced glycation end products (RAGE) mediates inflammation. Human recombinant S100A12 was found to induce neuritogenesis of cultured hippocampal cells, similar to two other S100 proteins, S100B and S100A4. X-ray structure of S100A12 has been solved in two crystal forms: R3 and P2(1). In the R3 crystal form S100A12 is a dimer, and in the P2(1) crystal form the dimers are arranged as a hexamer. The hexameric form suggests its role in receptor oligomerisation. S100A12 binds copper at the predicted zinc/copper binding site, which is located close to the surface of the protein. We propose copper-mediated generation of reactive oxygen species by S100A12 as its function in host-parasite response. (C) 2003 Wiley-Liss, Inc.

    Research areas

  • S100 protein, calcium signalling, RAGE, granulocyte, copper, host-parasite response, GLYCATION END-PRODUCTS, CALCIUM-BINDING PROTEINS, CELL-SURFACE RECEPTOR, NF-KAPPA-B, CALGRANULIN-C, CRYSTAL-STRUCTURE, ZINC-BINDING, ENDOTHELIAL-CELLS, CORPORA-AMYLACEA, DEPENDENT SECRETION

Discover related content

Find related publications, people, projects, datasets and more using interactive charts.

View graph of relations