Enhancement of transport-dependent decarboxylation of phosphatidylserine by S100B protein in permeabilized Chinese hamster ovary cells

Citation
O. Kuge et al., Enhancement of transport-dependent decarboxylation of phosphatidylserine by S100B protein in permeabilized Chinese hamster ovary cells, J BIOL CHEM, 276(26), 2001, pp. 23700-23706
Citations number
28
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
00219258 → ACNP
Volume
276
Issue
26
Year of publication
2001
Pages
23700 - 23706
Database
ISI
SICI code
0021-9258(20010629)276:26<23700:EOTDOP>2.0.ZU;2-A
Abstract
Phosphatidylethanolamine synthesis through the phosphatidylserine (PtdSer) decarboxylation pathway requires PtdSer transport from the endoplasmic reti culum or mitochondrial-associated membrane to the mitochondrial inner membr ane in mammalian cells. The transport-dependent PtdSer decarboxylation in p ermeabilized Chinese hamster ovary (CHO) cells was enhanced by cytosolic fa ctors from bovine brain. A cytosolic protein factor exhibiting this enhanci ng activity was purified, and its amino acid sequence was partially determi ned. The sequence was identical to part of the amino acid sequence of an EF -hand type calcium-binding protein, S100B. A His(6)-tagged recombinant CHO S100B protein was able to remarkably enhance the transport-dependent PtdSer decarboxylation in permeabilized CHO cells. Under the standard assay condi tions for PtdSer decarboxylase, the recombinant S100B protein did not stimu late PtdSer decarboxylase activity and exhibited no PtdSer decarboxylase ac tivity. These results implicated the S100B protein in the transport of PtdS er to the mitochondrial inner membrane.