PMID- 8011635
OWN - NLM
STAT- MEDLINE
DCOM- 19940727
LR  - 20190613
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 33
IP  - 24
DP  - 1994 Jun 21
TI  - Regulation of membrane cholesterol domains by sterol carrier protein-2.
PG  - 7682-90
AB  - Sterols are not randomly distributed in membranes but appear to be localized in 
      multiple kinetic domains. Factors that regulate these sterol domains are not 
      well-understood. A recently developed fluorescence polarization assay that 
      measures molecular sterol transfer [Butko, P., Hapala, I., Nemecz, G., of 
      Schroeder, F. (1992) J. Biochem. Biophys. Methods 24, 15-37] was used to examine 
      the mechanism whereby anionic phospholipids and liver sterol carrier protein-2 
      (SCP2) enhance sterol transfer. Two exchangeable and one very slowly or 
      nonexchangeable sterol domain were resolved in phosphatidylcholine (POPC)/sterol 
      small unilamellar vesicles (SUV). Inclusion of 10 mol % anionic phospholipids 
      enhanced sterol exchange primarily by redistribution of sterol domain sizes 
      rather than by alteration of half-times of exchange. This effect was dependent 
      primarily on the percent content rather than the net charge per anionic 
      phospholipid. In contrast, SCP2 simultaneously altered both the distribution of 
      sterol molecules between kinetic domains and the exchange half-times of 
      exchangeable sterol domains. The effects of SCP2 were much more pronounced when 
      10% acidic phospholipid was incorporated in the SUV. Compared to spontaneous 
      sterol exchange, in the presence of 1.5 microM SCP2, the rapidly exchanging pool 
      was increased by 36 to 330%, depending on the SUV phospholipid composition. 
      Concomitantly, exchange half-times for rapidly and slowly exchangeable sterol 
      were reduced by 60 to 98% for 1t1/2 and 14 to 85% for 2t1/2, respectively. The 
      stimulatory effect of SCP2 was saturable and dependent both on protein 
      concentration and on content of acidic phospholipids in membranes.(ABSTRACT 
      TRUNCATED AT 250 WORDS)
FAU - Hapala, I
AU  - Hapala I
AD  - Institute of Animal Biochemistry and Genetics, Slovak Academy of Science, Ivanka 
      Pri Dunaji.
FAU - Kavecansky, J
AU  - Kavecansky J
FAU - Butko, P
AU  - Butko P
FAU - Scallen, T J
AU  - Scallen TJ
FAU - Joiner, C H
AU  - Joiner CH
FAU - Schroeder, F
AU  - Schroeder F
LA  - eng
GR  - DK41402/DK/NIDDK NIH HHS/United States
GR  - GM31651/GM/NIGMS NIH HHS/United States
GR  - HL37515/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Anions)
RN  - 0 (Carrier Proteins)
RN  - 0 (Fatty Acid-Binding Proteins)
RN  - 0 (Liposomes)
RN  - 0 (Membrane Lipids)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Phosphatidylcholines)
RN  - 0 (Phosphatidylserines)
RN  - 0 (Phospholipids)
RN  - 0 (Plant Proteins)
RN  - 0 (sterol carrier proteins)
RN  - 660YQ98I10 (Potassium Chloride)
RN  - 97C5T2UQ7J (Cholesterol)
SB  - IM
MH  - Anions
MH  - Carrier Proteins/administration & dosage/*pharmacology
MH  - Cholesterol/*metabolism
MH  - Dose-Response Relationship, Drug
MH  - Drug Synergism
MH  - Electrochemistry
MH  - Fatty Acid-Binding Proteins
MH  - Fluorescence Polarization
MH  - Hydrogen-Ion Concentration
MH  - Kinetics
MH  - Liposomes/chemistry/*metabolism
MH  - Membrane Lipids/analysis/*metabolism
MH  - *Neoplasm Proteins
MH  - Phosphatidylcholines/analysis
MH  - Phosphatidylserines/analysis
MH  - Phospholipids/analysis/pharmacology
MH  - *Plant Proteins
MH  - Potassium Chloride/pharmacology
EDAT- 1994/06/21 00:00
MHDA- 1994/06/21 00:01
CRDT- 1994/06/21 00:00
PHST- 1994/06/21 00:00 [pubmed]
PHST- 1994/06/21 00:01 [medline]
PHST- 1994/06/21 00:00 [entrez]
AID - 10.1021/bi00190a023 [doi]
PST - ppublish
SO  - Biochemistry. 1994 Jun 21;33(24):7682-90. doi: 10.1021/bi00190a023.