PMID- 10191275
OWN - NLM
STAT- MEDLINE
DCOM- 19990623
LR  - 20181113
IS  - 0264-6021 (Print)
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 339 ( Pt 2)
IP  - Pt 2
DP  - 1999 Apr 15
TI  - Calcium-binding protein S100A7 and epidermal-type fatty acid-binding protein are 
      associated in the cytosol of human keratinocytes.
PG  - 419-27
AB  - Expression of epidermal-type fatty acid-binding protein (E-FABP) and S100A7 has 
      previously been shown to be elevated in psoriatic skin, a disease characterized 
      by abnormal keratinocyte differentiation. However, no causal relationship between 
      the up-regulation of these proteins and the disease has been shown. E-FABP is 
      thought to be involved in cytosolic fatty acid (FA) transport, whereas the role 
      of S100A7 is still unknown. In this report, we show by overlay assays that 
      E-FABP, immobilized on nitrocellulose, is able to capture S100A7 from cytosolic 
      psoriatic protein extracts and vice versa, suggesting the formation of a complex 
      between the two proteins. Using purified E-FABP and S100A7, the complex can be 
      reconstituted only in presence of EDTA. Moreover, we show that increased EDTA 
      concentrations in psoriatic cytosolic protein extracts enhance complex formation. 
      Partial complex disruption was obtained by the addition of physiological 
      concentrations of Zn2+ (0.1 mM), whereas Ca2+ at 5 mM and Mg2+ at 30 mM had no 
      effect. On the other hand, high Ca2+ concentrations (30 mM) resulted in partial 
      complex disruption. Oleic acid-binding properties were observed for free E-FABP 
      and the complex E-FABP-S100A7, but not for free S100A7. By using confocal 
      microscopy we show that S100A7 and E-FABP are co-localized in the cytoplasm of 
      differentiating keratinocytes from lesional psoriatic skin. These data indicate 
      that formation of the E-FABP-S100A7 complex and its FA-binding function might be 
      regulated at least by bivalent cations.
FAU - Hagens, G
AU  - Hagens G
AD  - Clinique de Dermatologie and DHURDV, Hopital Universitaire, CH-1211 Geneve, 
      Switzerland.
FAU - Masouye, I
AU  - Masouye I
FAU - Augsburger, E
AU  - Augsburger E
FAU - Hotz, R
AU  - Hotz R
FAU - Saurat, J H
AU  - Saurat JH
FAU - Siegenthaler, G
AU  - Siegenthaler G
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (FABP5 protein, human)
RN  - 0 (FABP7 protein, human)
RN  - 0 (Fatty Acid-Binding Protein 7)
RN  - 0 (Fatty Acid-Binding Proteins)
RN  - 0 (Myelin P2 Protein)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (S100 Calcium Binding Protein A7)
RN  - 0 (S100 Proteins)
RN  - 0 (S100A7 protein, human)
RN  - 0 (Tumor Suppressor Proteins)
RN  - 2UMI9U37CP (Oleic Acid)
SB  - IM
MH  - Calcium-Binding Proteins/isolation & purification/*metabolism
MH  - Carrier Proteins/isolation & purification/*metabolism
MH  - Cells, Cultured
MH  - Chromatography, Gel
MH  - Cytosol/metabolism
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Epidermis/*metabolism
MH  - Fatty Acid-Binding Protein 7
MH  - Fatty Acid-Binding Proteins
MH  - Humans
MH  - Isoelectric Point
MH  - Keratinocytes/*metabolism
MH  - Myelin P2 Protein/isolation & purification/*metabolism
MH  - *Neoplasm Proteins
MH  - Oleic Acid/metabolism
MH  - Protein Binding
MH  - Psoriasis/metabolism
MH  - S100 Calcium Binding Protein A7
MH  - S100 Proteins
MH  - *Tumor Suppressor Proteins
PMC - PMC1220173
EDAT- 1999/04/07 00:00
MHDA- 1999/04/07 00:01
PMCR- 1999/10/15
CRDT- 1999/04/07 00:00
PHST- 1999/04/07 00:00 [pubmed]
PHST- 1999/04/07 00:01 [medline]
PHST- 1999/04/07 00:00 [entrez]
PHST- 1999/10/15 00:00 [pmc-release]
PST - ppublish
SO  - Biochem J. 1999 Apr 15;339 ( Pt 2)(Pt 2):419-27.