Guinea pig eosinophil major basic protein as a potent histamine releaser. (II) Structure-activity relationships of GMBP1 and GMBP2

1992 ◽  
Vol 36 (S2) ◽  
pp. C246-C249 ◽  
Author(s):  
K. Tasaka ◽  
M. Mio ◽  
S. Nakai ◽  
I. Aoki
Keyword(s):  
Guinea Pig ◽  
Basic Protein ◽  
Major Basic Protein ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Eosinophil Major Basic Protein

Measurement of guinea pig eosinophil major basic protein by radioimmunoassay

1979 ◽  
Vol 16 (9) ◽  
pp. 711-719 ◽  
Author(s):  
Donald L. Wassom ◽  
David A. Loegering ◽  
Gerald J. Gleich
Keyword(s):  
Guinea Pig ◽  
Basic Protein ◽  
Major Basic Protein ◽  
Eosinophil Major Basic Protein

Sequencing and cloning of the cDNA of guinea pig eosinophil major basic protein

FEBS Letters ◽  
1991 ◽  
Vol 279 (2) ◽  
pp. 330-334 ◽  
Author(s):  
Ikuo Aoki ◽  
Yutaka Shindoh ◽  
Tsutomu Nishida ◽  
Satoru Nakai ◽  
Yeong-Man Hong ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Basic Protein ◽  
Major Basic Protein ◽  
Eosinophil Major Basic Protein

scholarly journals Localization of the guinea pig eosinophil major basic protein to the core of the granule

1978 ◽  
Vol 77 (3) ◽  
pp. 702-713 ◽  
Author(s):  
DM Lewis ◽  
JC Lewis ◽  
DA Loegering ◽  
GJ Gleich
Keyword(s):  
Guinea Pig ◽  
Basic Protein ◽  
Core Protein ◽  
Sodium Dodecyl ◽  
Rabbit Antiserum ◽  
Staining Procedure ◽  
Normal Rabbit Serum ◽  
Major Basic Protein ◽  
The Core ◽  
Eosinophil Major Basic Protein

The localization of the guinea pig eosinophil major basic protein (MBP) within the cell was investigated by the use of immunoelectron microscopy and by isolation of the granule crystalloids. First, by immunoperoxidase electron microscopy, we found that the MBP of eosinophil granules is contained within the crystalloid core of the granule. Specific staining of cores was present when rabbit antiserum to MBP was used as the first stage antibody in a double antibody staining procedure, whereas staining was not seen when normal rabbit serum was used as the first stage antibody. Second, crystalloids were isolated from eosinophil granules by disruption in 0.1% Triton X-100 and centrifugation through a cushion of 50% sucrose. Highly purified core preparations yielded essentially a single band when analyzed by electrophoresis on polyacrylamide gels containing 1% sodium dodecyl sulfate (SDS). The E1%1cm of the core protein was 26.8 +/- 1.0 (X +/- SEM); the E1%1cm for the MBP was 26.3. The core protein could not be distinguished from the MBP by radioimmunoassay (RIA) and essentially all of the protein in the core preparations could be accounted for as MBP. The results indicate that the MBP is contained in the core of the guinea pig eosinophil granule and that it is probably the only protein present in the core.

Prostaglandin secretion by guinea pig tracheal epithelial cells caused by eosinophil major basic protein

1993 ◽  
Vol 265 (3) ◽  
pp. L234-L242 ◽  
Author(s):  
S. R. White ◽  
K. S. Sigrist ◽  
S. M. Spaethe
Keyword(s):  
Epithelial Cells ◽  
Guinea Pig ◽  
Basic Protein ◽  
Primary Cultures ◽  
Thromboxane B2 ◽  
Major Basic Protein ◽  
Tracheal Epithelial Cells ◽  
Subsequent Response ◽  
Tracheal Epithelial ◽  
Eosinophil Major Basic Protein

We examined the effect of eosinophil major basic protein (MBP) on prostaglandin (PG) secretion from guinea pig tracheal epithelial (GPTE) cells. Primary cultures of GPTE cells were incubated with 10(-6) M MBP for up to 6 h and then stimulated with 10(-6) M bradykinin (BK). PGE2, 6-ketoprostaglandin F1 alpha (PGF1 alpha), PGF2 alpha, and thromboxane B2 (TxB2) concentrations in media were determined by enzyme-linked immunoabsorbent assay (EIA). Incubation with MBP for 6 h caused secretion of both PGE2 (17,614 +/- 4,416 vs. 1,426 +/- 555 pg/10(6) cells at baseline, P < 0.001, n = 7) and PGF2 alpha (20,303 +/- 5,724 vs. 3,790 +/- 1.075 pg/10(6) cells at baseline, P < 0.002, n = 7). Secretion of PGE2 and PGF2 alpha stimulated by MBP required at least 2 h. Incubation with MBP for 6 h also augmented the subsequent response to BK: PGE2 secretion was 29,215 +/- 6,853 vs. 3,445 +/- 1,041 pg/10(6) cells for BK alone (P < 0.0001), and PGF2 alpha secretion was 25,407 +/- 6,237 vs. 5,213 +/- 1,535 pg/10(6) cells for BK alone (P < 0.0001). MBP did not change 6-keto-PGF1 alpha and TxB2 secretion. Incubation of GPTE cells from seven animals with polylysine, a protein with mass and ion charge similar to MBP, for 2 h, both caused secretion of PGE2 (8,579 +/- 3,244 vs. 788 +/- 419 pg/10(6) cells at baseline, P < 0.01) and augmented the response to BK (12,732 +/- 4,788 vs. 1,653 +/- 680 pg/10(6) cells after BK alone, P < 0.005).(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Isolation of antibacterial peptides from guinea pig eosinophil major basic protein.

Ensho ◽  
1992 ◽  
Vol 12 (5) ◽  
pp. 441-445
Author(s):  
Yuichi Hashimoto ◽  
Isao Nagaoka ◽  
Akimasa Someya ◽  
Kazuhisa Iwabuchi ◽  
Shin Yomogida ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Basic Protein ◽  
Antibacterial Peptides ◽  
Major Basic Protein ◽  
Eosinophil Major Basic Protein

scholarly journals cDNA cloning of guinea pig eosinophil major basic protein.

1991 ◽  
Vol 55 ◽  
pp. 168
Author(s):  
Ikuo Aoki ◽  
Satoru Nakai ◽  
Mitsunobu Mio ◽  
Tadayuki Saito ◽  
Kenji Tasaka
Keyword(s):  
Guinea Pig ◽  
Cdna Cloning ◽  
Basic Protein ◽  
Major Basic Protein ◽  
Eosinophil Major Basic Protein
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