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

@article{Plager1999ANA,
  title={A Novel and Highly Divergent Homolog of Human Eosinophil Granule Major Basic Protein*},
  author={Douglas A. Plager and David A. Loegering and Deborah A. Weiler and James L. Checkel and Jill M. Wagner and Nigel J. Clarke and Stephen Naylor and Scott M. Page and Larry L. Thomas and Ingrid E. Akerblom and Ben Cocks and Susan G. Stuart and Gerald J. Gleich},
  journal={The Journal of Biological Chemistry},
  year={1999},
  volume={274},
  pages={14464 - 14473}
}
Eosinophils are important effector cells in defense against helminth infection and in allergic diseases. To identify novel eosinophil proteins, large scale sequencing of a cDNA library prepared from interleukin-5-stimulated umbilical cord precursor cells was performed, and the major genes expressed by maturing eosinophils were determined. This resulted in the identification of a cDNA with 64% identity to human prepro-major basic protein (hprepro-MBP). This cDNA was designated hprepro-MBP… 

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References

SHOWING 1-10 OF 59 REFERENCES

The identification and cloning of a murine major basic protein gene expressed in eosinophils.

Genomic Southern blots using the mMBP gene at reduced stringency reveal the potential existence of a second, more divergent MBP-like sequence in the mouse, which suggests that, as with guinea pigs, the mouse genome may also encode the eosinophil major basic protein from more than one gene.

Expression of eosinophil-granule major basic protein messenger ribonucleic acid in placental X cells.

The presence of MBP mRNA and MBP protein in placental X cells indicates that X cells synthesize this biologically active molecule.

Expression, purification, and characterization of the recombinant proform of eosinophil granule major basic protein.

It was shown that proMBP not only lacked the able to inhibit protein synthesis in K562 cells, but it also lacked the ability to stimulate basophil histamine release or generate neutrophil superoxide anion release.

Isolation of a complementary DNA clone encoding a precursor to human eosinophil major basic protein

Northern analysis of HL-60 cells suggests that MBP is constitutively expressed in HL- 60 cells and is highly transcribed from a single copy gene.

Localization of a molecule immunochemically similar to eosinophil major basic protein in human placenta

It is shown, by immunofluorescence, that placental tissue specifically binds antibody to MBP in and around the placental X cells and placental-site giant cells and, using thin plastic sections, that placenta has no infiltrating eosinophils.

Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease.

Results indicate that EDN and ECP are related proteins and suggest that they derived from genes associated with the RNase family.

Ribonuclease activity associated with human eosinophil-derived neurotoxin and eosinophil cationic protein.

Results indicate that EDN and ECP both possessRNase activity, the RNase activity of EDN or ECP is specific, and EDNand ECP have maintained not only structural but also functional homology to pancreatic RNase.

Eosinophil major basic protein induces degranulation and IL-8 production by human eosinophils.

MBP and EPO may act as autocrine mediators in the pathogenesis of eosinophil-associated diseases, such as bronchial asthma.

Comparative properties of the Charcot-Leyden crystal protein and the major basic protein from human eosinophils.

The results indicate that the human MBP and the CLC are distinct substances with properties such that one cannot be derived from the other.
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