|
|
 Previous Article | Table of Contents | Next Article 
Regulation and Processing of a Precursor Form of Eosinophil Granule
Major Basic Protein (ProMBP) in Differentiating Eosinophils
Pamela Popken-Harris,
James Checkel,
David Loegering,
Benjamin Madden,
Margaret Springett,
Gail Kephart, and
Gerald J. Gleich
From the Departments of Immunology, Internal Medicine, and
Biochemistry and Molecular Biology, Mayo Clinic and Mayo Foundation,
Rochester, MN.
The cDNA for eosinophil granule major basic protein (MBP) encodes a
prepromolecule with a total length of 222 amino acids (preproMBP).
PreproMBP includes a secretory leader of 15 amino acids, an acidic
propiece of 90 amino acids, and a basic MBP portion of 117 amino acids.
The function of the propiece, which has a predicted pI of 3.9, is
unknown, but it gives proMBP an overall acidic charge. Because proMBP
is not found in mature eosinophils, we analyzed eosinophil
differentiation in interleukin-5 (IL-5)-stimulated umbilical cord stem
cells cultured for 24 days. By immunofluorescence, proMBP appeared by
day 6 and peaked on day 18, whereas MBP was prominent at days 12 to 24. By day 6, Western blots detected heterogeneous glycosylated 33-kD
proMBP; its peak expression occurred on day 12. Western blots showed
sequential processing of 33-kD proMBP to an 18-kD intermediate form and
finally to 14-kD MBP. By dual label immunoelectron microscopy, proMBP
was localized primarily to large uncondensed eosinophil granules,
whereas MBP was localized to granules containing a condensed central
area. Thus, proMBP is likely expressed and processed as the granule
condenses in a multistep process to 14-kD MBP in differentiating
eosinophils.
Blood, Vol. 92 No. 2 (July 15), 1998:
pp. 623-631
© 1998 by the American Society of Hematology.
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
M. Ulrich, A. Petre, N. Youhnovski, F. Promm, M. Schirle, M. Schumm, R. S. Pero, A. Doyle, J. Checkel, H. Kita, et al.
Post-translational Tyrosine Nitration of Eosinophil Granule Toxins Mediated by Eosinophil Peroxidase
J. Biol. Chem.,
October 17, 2008;
283(42):
28629 - 28640.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Wehling-Henricks, S. Sokolow, J. J. Lee, K. H. Myung, S. A. Villalta, and J. G. Tidball
Major basic protein-1 promotes fibrosis of dystrophic muscle and attenuates the cellular immune response in muscular dystrophy
Hum. Mol. Genet.,
August 1, 2008;
17(15):
2280 - 2292.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Glerup, S. Kloverpris, and C. Oxvig
The Proform of the Eosinophil Major Basic Protein Binds the Cell Surface through a Site Distinct from Its C-type Lectin Ligand-binding Region
J. Biol. Chem.,
October 20, 2006;
281(42):
31509 - 31516.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Glerup, H. B. Boldt, M. T. Overgaard, L. Sottrup-Jensen, L. C. Giudice, and C. Oxvig
Proteinase Inhibition by Proform of Eosinophil Major Basic Protein (pro-MBP) Is a Multistep Process of Intra- and Intermolecular Disulfide Rearrangements
J. Biol. Chem.,
March 18, 2005;
280(11):
9823 - 9832.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. T. Overgaard, E. S. Sorensen, D. Stachowiak, H. B. Boldt, L. Kristensen, L. Sottrup-Jensen, and C. Oxvig
Complex of Pregnancy-associated Plasma Protein-A and the Proform of Eosinophil Major Basic Protein. DISULFIDE STRUCTURE AND CARBOHYDRATE ATTACHMENT SITES
J. Biol. Chem.,
January 17, 2003;
278(4):
2106 - 2117.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
T. Nakajima, K. Matsumoto, H. Suto, K. Tanaka, M. Ebisawa, H. Tomita, K. Yuki, T. Katsunuma, A. Akasawa, R. Hashida, et al.
Gene expression screening of human mast cells and eosinophils using high-density oligonucleotide probe arrays: abundant expression of major basic protein in mast cells
Blood,
August 15, 2001;
98(4):
1127 - 1134.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Christiansen, I. Jaliashvili, M. T. Overgaard, C. Ensinger, P. Obrist, and C. Oxvig
Quantification and Characterization of Pregnancy-associated Complexes of Angiotensinogen and the Proform of Eosinophil Major Basic Protein in Serum and Amniotic Fluid
Clin. Chem.,
August 1, 2000;
46(8):
1099 - 1105.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
L. Cameron, P. Christodoulopoulos, F. Lavigne, Y. Nakamura, D. Eidelman, A. McEuen, A. Walls, J. Tavernier, E. Minshall, R. Moqbel, et al.
Evidence for Local Eosinophil Differentiation Within Allergic Nasal Mucosa: Inhibition with Soluble IL-5 Receptor
J. Immunol.,
February 1, 2000;
164(3):
1538 - 1545.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. T. Overgaard, C. Oxvig, M. Christiansen, J. B. Lawrence, C. A. Conover, G. J. Gleich, L. Sottrup-Jensen, and J. Haaning
Messenger Ribonucleic Acid Levels of Pregnancy-Associated Plasma Protein-A and the Proform of Eosinophil Major Basic Protein: Expression in Human Reproductive and Nonreproductive Tissues
Biol Reprod,
October 1, 1999;
61(4):
1083 - 1089.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
M. A. Giembycz and M. A. Lindsay
Pharmacology of the Eosinophil
Pharmacol. Rev.,
June 1, 1999;
51(2):
213 - 340.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
J. Ohmori, Y. Nawa, D.-H. Yang, S. Tsuyama, and F. Murata
Keratan Sulfate Glycosaminoglycans in Murine Eosinophil-specific Granules
J. Histochem. Cytochem.,
April 1, 1999;
47(4):
481 - 488.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
M. T. Overgaard, J. Haaning, H. B. Boldt, I. M. Olsen, L. S. Laursen, M. Christiansen, G. J. Gleich, L. Sottrup-Jensen, C. A. Conover, and C. Oxvig
Expression of Recombinant Human Pregnancy-associated Plasma Protein-A and Identification of the Proform of Eosinophil Major Basic Protein as Its Physiological Inhibitor
J. Biol. Chem.,
September 29, 2000;
275(40):
31128 - 31133.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
G. J. Swaminathan, A. J. Weaver, D. A. Loegering, J. L. Checkel, D. D. Leonidas, G. J. Gleich, and K. R. Acharya
Crystal Structure of the Eosinophil Major Basic Protein at 1.8 A. AN ATYPICAL LECTIN WITH A PARADIGM SHIFT IN SPECIFICITY
J. Biol. Chem.,
July 6, 2001;
276(28):
26197 - 26203.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
