Abstract
Mastoparan-induced changes in the K+ permeability of rat peritoneal mast cells, human erythrocytes, Staphylococcus aureus and Escherichia coli were examined. Mastoparan did not efficiently increase the K+ permeability of cells except for S. aureus. The release of membrane phospholipids was also observed from S. aureus cells in the concentration range of the permeability enhancement. Mastoparan stimulated histamine release from mast cells, independently of a small efflux of K+. Mastoparan became markedly effective to E. coli cells whose outer membrane structure was chemically disrupted beforehand, showing that the peptide can enhance the permeability of the cytoplasmic membranes of both Gram-positive and -negative bacteria. In experiments using liposomes, mastoparan increased the permeability of the liposomes composed of egg phosphatidylethanolamine and egg phosphatidylglycerol, which are the lipid constituents of the cytoplasmic membrane of E. coli cells, while it showed a weak activity to the liposomes composed of egg phosphatidylcholine and cholesterol. The latter result related closely to the fact that this peptide acted weakly on erythrocytes and mast cells in which acidic lipids constitute a minor portion. Mastoparan decreased the phase transition temperature of dipalmitoylphosphatidylglycerol liposomes, but it did not affect that of dipalmitoylphosphatidylcholine liposomes. These results indicate that mastoparan penetrated into membranes mainly containing acidic phospholipids and disrupted the membrane structure to increase the permeability. The action of the wasp venom mastoparan was compared with that of a bee venom melittin.
| Original language | English |
|---|---|
| Pages (from-to) | 185-190 |
| Number of pages | 6 |
| Journal | BBA - Biomembranes |
| Volume | 1027 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Aug 24 1990 |
Fingerprint
Keywords
- Biologically active peptide
- Histamine release
- Mastoparan
- Melittin
- Membrane fluidity
- Membrane permeability
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
Cite this
Interaction of wasp venom mastoparan with biomembranes. / Katsu, Takashi; Kuroko, Masakazu; Morikawa, Takayo; Sanchika, Kozo; Yamanaka, Hiroyasu; Shinoda, Sumio; Fujita, Yuzaburo.
In: BBA - Biomembranes, Vol. 1027, No. 2, 24.08.1990, p. 185-190.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Interaction of wasp venom mastoparan with biomembranes
AU - Katsu, Takashi
AU - Kuroko, Masakazu
AU - Morikawa, Takayo
AU - Sanchika, Kozo
AU - Yamanaka, Hiroyasu
AU - Shinoda, Sumio
AU - Fujita, Yuzaburo
PY - 1990/8/24
Y1 - 1990/8/24
N2 - Mastoparan-induced changes in the K+ permeability of rat peritoneal mast cells, human erythrocytes, Staphylococcus aureus and Escherichia coli were examined. Mastoparan did not efficiently increase the K+ permeability of cells except for S. aureus. The release of membrane phospholipids was also observed from S. aureus cells in the concentration range of the permeability enhancement. Mastoparan stimulated histamine release from mast cells, independently of a small efflux of K+. Mastoparan became markedly effective to E. coli cells whose outer membrane structure was chemically disrupted beforehand, showing that the peptide can enhance the permeability of the cytoplasmic membranes of both Gram-positive and -negative bacteria. In experiments using liposomes, mastoparan increased the permeability of the liposomes composed of egg phosphatidylethanolamine and egg phosphatidylglycerol, which are the lipid constituents of the cytoplasmic membrane of E. coli cells, while it showed a weak activity to the liposomes composed of egg phosphatidylcholine and cholesterol. The latter result related closely to the fact that this peptide acted weakly on erythrocytes and mast cells in which acidic lipids constitute a minor portion. Mastoparan decreased the phase transition temperature of dipalmitoylphosphatidylglycerol liposomes, but it did not affect that of dipalmitoylphosphatidylcholine liposomes. These results indicate that mastoparan penetrated into membranes mainly containing acidic phospholipids and disrupted the membrane structure to increase the permeability. The action of the wasp venom mastoparan was compared with that of a bee venom melittin.
AB - Mastoparan-induced changes in the K+ permeability of rat peritoneal mast cells, human erythrocytes, Staphylococcus aureus and Escherichia coli were examined. Mastoparan did not efficiently increase the K+ permeability of cells except for S. aureus. The release of membrane phospholipids was also observed from S. aureus cells in the concentration range of the permeability enhancement. Mastoparan stimulated histamine release from mast cells, independently of a small efflux of K+. Mastoparan became markedly effective to E. coli cells whose outer membrane structure was chemically disrupted beforehand, showing that the peptide can enhance the permeability of the cytoplasmic membranes of both Gram-positive and -negative bacteria. In experiments using liposomes, mastoparan increased the permeability of the liposomes composed of egg phosphatidylethanolamine and egg phosphatidylglycerol, which are the lipid constituents of the cytoplasmic membrane of E. coli cells, while it showed a weak activity to the liposomes composed of egg phosphatidylcholine and cholesterol. The latter result related closely to the fact that this peptide acted weakly on erythrocytes and mast cells in which acidic lipids constitute a minor portion. Mastoparan decreased the phase transition temperature of dipalmitoylphosphatidylglycerol liposomes, but it did not affect that of dipalmitoylphosphatidylcholine liposomes. These results indicate that mastoparan penetrated into membranes mainly containing acidic phospholipids and disrupted the membrane structure to increase the permeability. The action of the wasp venom mastoparan was compared with that of a bee venom melittin.
KW - Biologically active peptide
KW - Histamine release
KW - Mastoparan
KW - Melittin
KW - Membrane fluidity
KW - Membrane permeability
UR - http://www.scopus.com/inward/record.url?scp=0025032776&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025032776&partnerID=8YFLogxK
U2 - 10.1016/0005-2736(90)90083-Z
DO - 10.1016/0005-2736(90)90083-Z
M3 - Article
C2 - 2204429
AN - SCOPUS:0025032776
VL - 1027
SP - 185
EP - 190
JO - Biochimica et Biophysica Acta - Biomembranes
JF - Biochimica et Biophysica Acta - Biomembranes
SN - 0005-2736
IS - 2
ER -