Membrane Interactions of S100A12 (Calgranulin C)

Author(s)

Garcia, Assuero F. ^{[1, 2]} ; Lopes, Jose L. S. ^{[1, 3]} ; Costa-Filho, Antonio J. ^{[1, 2]} ; Wallace, Bonnie A. ^[3] ; Araujo, Ana P. U. ^[1]

Affiliation

^[1] Univ Sao Paulo, Inst Fis Sao Carlos, Sao Carlos, SP - Brazil

^[2] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Fis, Ribeirao Preto, SP - Brazil

^[3] Univ London, Inst Struct & Mol Biol, Birkbeck Coll, London - England

• Document type: Journal article
• Source: PLoS One; v. 8, n. 12 DEC 18 2013.
• Web of Science Citations: 3

Abstract

S100A12 (Calgranulin C) is a small acidic calcium-binding peripheral membrane protein with two EF-hand structural motifs. It is expressed in macrophages and lymphocytes and highly up-regulated in several human inflammatory diseases. In pigs, S100A12 is abundant in the cytosol of granulocytes, where it is believed to be involved in signal modulation of inflammatory process. In this study, we investigated the interaction of the porcine S100A12 with phospholipid bilayers and the effect that ions (Ca2+, Zn2+ or both together) have in modifying protein-lipid interactions. More specifically, we intended to address issues such as: (1) is the protein-membrane interaction modulated by the presence of ions? (2) is the protein overall structure affected by the presence of the ions and membrane models simultaneously? (3) what are the specific conformational changes taking place when ions and membranes are both present? (4) does the protein have any kind of molecular preferences for a specific lipid component? To provide insight into membrane interactions and answer those questions, synchrotron radiation circular dichroism spectroscopy, fluorescence spectroscopy, and surface plasmon resonance were used. The use of these combined techniques demonstrated that this protein was capable of interacting both with lipids and with ions in solution, and enabled examination of changes that occur at different levels of structure organization. The presence of both Ca2+ and Zn2+ ions modify the binding, conformation and thermal stability of the protein in the presence of lipids. Hence, these studies examining molecular interactions of porcine S100A12 in solution complement the previously determined crystal structure information on this family of proteins, enhancing our understanding of its dynamics of interaction with membranes. (AU)

• FAPESP's process: 10/17662-8 - Electron magnetic resonance in studies of structure, function and interactions of biologically-relevant molecules
• Grantee: Antonio José da Costa Filho
• Support Opportunities: Regular Research Grants
• FAPESP's process: 12/20367-3 - Structural and functional studies of the Golgi Re-Assembly and Stacking Protein (GRASP) from Cryptococcus neoformans
• Grantee: Antonio José da Costa Filho
• Support Opportunities: Regular Research Grants