scholarly journals Acidic precursor revealed in human eosinophil granule major basic protein cDNA.

1988 ◽  
Vol 168 (4) ◽  
pp. 1493-1498 ◽  
Author(s):  
R L Barker ◽  
G J Gleich ◽  
L R Pease
Keyword(s):  
Endoplasmic Reticulum ◽  
Nucleotide Sequence ◽  
Cdna Library ◽  
Basic Protein ◽  
Cell Types ◽  
Major Basic Protein ◽  
Human Eosinophil ◽  
Damage Cell ◽  
Eosinophil Granule ◽  
Single Polypeptide

Eosinophil granule major basic protein (MBP), a potent toxin for helminths and various cell types, is a 13.8-kD single polypeptide rich in arginine with a calculated isoelectric point (pI) of 10.9. A cDNA for human MBP was isolated from a gamma GT10 HL-60 cDNA library. The nucleotide sequence of the MBP cDNA indicates that MBP is translated as a 25.2-kD preproprotein. The 9.9-kD pro-portion of proMBP is rich in glutamic and aspartic acids and has a calculated pI of 3.9, while proMBP itself has a calculated pI of 6.2. We suggest that MBP is translated as a nontoxic precursor that protects the eosinophil from damage while the protein is processed through the endoplasmic reticulum to its sequestered site in the granule core toxic MBP, and we present results from the literature suggesting that other cationic toxins, which damage cell membranes, may also be processed from nontoxic precursors containing distinct anionic and cationic regions.

scholarly journals Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein.

1988 ◽  
Vol 263 (25) ◽  
pp. 12559-12563
Author(s):  
T L Wasmoen ◽  
M P Bell ◽  
D A Loegering ◽  
G J Gleich ◽  
F G Prendergast ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Basic Protein ◽  
Major Basic Protein ◽  
Amino Acid Sequence Analysis ◽  
Human Eosinophil ◽  
Eosinophil Granule

scholarly journals A Novel and Highly Divergent Homolog of Human Eosinophil Granule Major Basic Protein

1999 ◽  
Vol 274 (20) ◽  
pp. 14464-14473 ◽  
Author(s):  
Douglas A. Plager ◽  
David A. Loegering ◽  
Deborah A. Weiler ◽  
James L. Checkel ◽  
Jill M. Wagner ◽  
...  
Keyword(s):  
Basic Protein ◽  
Major Basic Protein ◽  
Human Eosinophil ◽  
Eosinophil Granule

The Effect of Human Eosinophil Granule Major Basic Protein on Airway Responsiveness in the RatIn Vivo: A Comparison with Polycations

1993 ◽  
Vol 147 (4) ◽  
pp. 982-988 ◽  
Author(s):  
Derek A. Uchida ◽  
Steven J. Ackerman ◽  
Anthony J. Coyle ◽  
Gary L. Larsen ◽  
Peter F. Weller ◽  
...  
Keyword(s):  
Basic Protein ◽  
Airway Responsiveness ◽  
Major Basic Protein ◽  
Human Eosinophil ◽  
Eosinophil Granule

Epithelial augmentation of trachealis contraction caused by major basic protein of eosinophils

1989 ◽  
Vol 66 (4) ◽  
pp. 1867-1873 ◽  
Author(s):  
J. D. Brofman ◽  
S. R. White ◽  
J. S. Blake ◽  
N. M. Munoz ◽  
G. J. Gleich ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Basic Protein ◽  
Tracheal Smooth Muscle ◽  
Active Tension ◽  
Major Basic Protein ◽  
Human Eosinophil ◽  
Control Segment ◽  
Eosinophil Granule

We studied the effect of epithelial removal and intraepithelial administration of human eosinophil granule major basic protein (MBP) on the contraction of underlying canine tracheal smooth muscle in 23 dogs in vivo. A dual in situ tracheal preparation was utilized that allowed sharp excision of epithelium. The response to intra-arterial acetylcholine (ACh) was augmented substantially in five dogs receiving 200 micrograms MBP by intraepithelial instillation. Active tension elicited by 10(-8) mol intra-arterial ACh was 34.0 +/- 2.2 g/cm before and 46.1 +/- 2.6 g/cm 30 min after MBP (P less than 0.002). There was no change in active tension in the control segment in the same dogs after intraepithelial instillation of vehicle only (34.7 +/- 3.2 vs. 34.4 +/- 2.3 g/cm; P = NS). Instillation of MBP directly into the subepithelial tracheal smooth muscle did not alter contraction. To assess whether this augmentation was caused by inhibition of an epithelial-derived relaxant factor, additional studies were performed in nine other dogs in which the epithelium was excised discretely from one of the two tracheal segments. No significant differences in contractile response to ACh or relaxation response to isoproterenol were observed at 2, 15, 30, or 60 min after epithelial excision. We demonstrate that intraepithelial administration of MBP augments the contraction of underlying canine tracheal smooth muscle elicited by ACh. This augmentation is a direct effect of MBP and does not require antagonism of epithelial inhibition.

Human eosinophil granule major basic protein and its novel homolog

Allergy ◽  
1998 ◽  
Vol 53 ◽  
pp. 33-40 ◽  
Author(s):  
D. A. Plager ◽  
S. Stuad ◽  
G.J. Gleich
Keyword(s):  
Basic Protein ◽  
Major Basic Protein ◽  
Human Eosinophil ◽  
Eosinophil Granule

scholarly journals Vesicle-mediated secretion of human eosinophil granule-derived major basic protein

2009 ◽  
Vol 89 (7) ◽  
pp. 769-781 ◽  
Author(s):  
Rossana C N Melo ◽  
Lisa A Spencer ◽  
Sandra A C Perez ◽  
Josiane S Neves ◽  
Staci P Bafford ◽  
...  
Keyword(s):  
Basic Protein ◽  
Major Basic Protein ◽  
Human Eosinophil ◽  
Eosinophil Granule

scholarly journals Acidic polyamino acids inhibit human eosinophil granule major basic protein toxicity. Evidence of a functional role for ProMBP.

1991 ◽  
Vol 88 (3) ◽  
pp. 798-805 ◽  
Author(s):  
R L Barker ◽  
R H Gundel ◽  
G J Gleich ◽  
J L Checkel ◽  
D A Loegering ◽  
...  
Keyword(s):  
Functional Role ◽  
Basic Protein ◽  
Major Basic Protein ◽  
Human Eosinophil ◽  
Eosinophil Granule ◽  
Protein Toxicity

scholarly journals Activation of basophil and mast cell histamine release by eosinophil granule major basic protein.

1983 ◽  
Vol 157 (6) ◽  
pp. 1981-1991 ◽  
Author(s):  
M C O'Donnell ◽  
S J Ackerman ◽  
G J Gleich ◽  
L L Thomas
Keyword(s):  
Mast Cell ◽  
Histamine Release ◽  
Basic Protein ◽  
Major Basic Protein ◽  
Histamine Secretion ◽  
Human Eosinophil ◽  
Peritoneal Mast Cells ◽  
Eosinophil Granule ◽  
Kinetics Of ◽  
Human Basophils

Major basic protein (MBP) is a primary constituent of eosinophil granules. In this report, we demonstrate that MBP from human eosinophil granules initiates a nonlytic histamine release from human leukocytes. A direct effect of MBP on basophils was confirmed using purified human basophils. The kinetics of release were similar to those reported for poly-L-arginine, although MBP was less potent than poly-L-arginine of similar molecular weight. Reduction and alkylation of MBP diminished both the potency and efficacy of the molecule. Native MBP also stimulated histamine secretion from purified rat peritoneal mast cells in a manner characteristic of other polycations. These results emphasize the bidirectional nature of the basophil/mast cell-eosinophil regulatory axis.

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