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

K. A. Larson, M. A. Horton, B. J. Madden, G. J. Gleich, Nancy A Lee, J. J. Lee

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

The existence of a murine homologue of the major basic protein (MBP) found in human eosinophil granules was initially hypothesized from structural similarities at the electron microscopic level. The results presented in this study have extended these observations by describing the identification/purification of a mouse MBP (mMBP) and the cloning of the gene encoding this eosinophil granule protein. Using protein purification methodologies with extravascular eosinophils, an mMBP homologue has been identified on the basis of strong (64%) N-terminal sequence homology with the mature human MBP (hMBP). Since hMBP results from a proteolytic cleavage of a precursor molecule, this sequence conservation suggests that the mouse granule protein is processed by a similar mechanism. The gene encoding mMBP was isolated using a hMBP cDNA clone as a heterologous probe in low criteria screens of mouse genomic and cDNA libraries. The genomic structure and nucleotide sequence of the mMBP exons are well conserved with the human gene, although homology alignments of the encoded proteins show that extensive sequence conservation occurs only in the mature portion of the MBP molecules. Expression data demonstrate that this gene is transcriptionally active in tissues containing eosinophil progenitor cells, such as femoral bone marrow. 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. This suggests that, as with guinea pigs, the mouse genome may also encode the eosinophil major basic protein from more than one gene.

Original languageEnglish (US)
Pages (from-to)3002-3012
Number of pages11
JournalJournal of Immunology
Volume155
Issue number6
StatePublished - 1995

Fingerprint

Eosinophils
Organism Cloning
Proteins
Genes
Eosinophil Granule Proteins
Eosinophil Major Basic Protein
Genomic Library
Sequence Homology
Southern Blotting
Thigh
Gene Library
Exons
Guinea Pigs
Stem Cells
Complementary DNA
Clone Cells
Bone Marrow
Genome
Electrons

ASJC Scopus subject areas

  • Immunology

Cite this

Larson, K. A., Horton, M. A., Madden, B. J., Gleich, G. J., Lee, N. A., & Lee, J. J. (1995). The identification and cloning of a murine major basic protein gene expressed in eosinophils. Journal of Immunology, 155(6), 3002-3012.

The identification and cloning of a murine major basic protein gene expressed in eosinophils. / Larson, K. A.; Horton, M. A.; Madden, B. J.; Gleich, G. J.; Lee, Nancy A; Lee, J. J.

In: Journal of Immunology, Vol. 155, No. 6, 1995, p. 3002-3012.

Research output: Contribution to journalArticle

Larson, KA, Horton, MA, Madden, BJ, Gleich, GJ, Lee, NA & Lee, JJ 1995, 'The identification and cloning of a murine major basic protein gene expressed in eosinophils', Journal of Immunology, vol. 155, no. 6, pp. 3002-3012.
Larson, K. A. ; Horton, M. A. ; Madden, B. J. ; Gleich, G. J. ; Lee, Nancy A ; Lee, J. J. / The identification and cloning of a murine major basic protein gene expressed in eosinophils. In: Journal of Immunology. 1995 ; Vol. 155, No. 6. pp. 3002-3012.
@article{1d4669a105f34c5cb9285ed861d4ad9e,
title = "The identification and cloning of a murine major basic protein gene expressed in eosinophils",
abstract = "The existence of a murine homologue of the major basic protein (MBP) found in human eosinophil granules was initially hypothesized from structural similarities at the electron microscopic level. The results presented in this study have extended these observations by describing the identification/purification of a mouse MBP (mMBP) and the cloning of the gene encoding this eosinophil granule protein. Using protein purification methodologies with extravascular eosinophils, an mMBP homologue has been identified on the basis of strong (64{\%}) N-terminal sequence homology with the mature human MBP (hMBP). Since hMBP results from a proteolytic cleavage of a precursor molecule, this sequence conservation suggests that the mouse granule protein is processed by a similar mechanism. The gene encoding mMBP was isolated using a hMBP cDNA clone as a heterologous probe in low criteria screens of mouse genomic and cDNA libraries. The genomic structure and nucleotide sequence of the mMBP exons are well conserved with the human gene, although homology alignments of the encoded proteins show that extensive sequence conservation occurs only in the mature portion of the MBP molecules. Expression data demonstrate that this gene is transcriptionally active in tissues containing eosinophil progenitor cells, such as femoral bone marrow. 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. This suggests that, as with guinea pigs, the mouse genome may also encode the eosinophil major basic protein from more than one gene.",
author = "Larson, {K. A.} and Horton, {M. A.} and Madden, {B. J.} and Gleich, {G. J.} and Lee, {Nancy A} and Lee, {J. J.}",
year = "1995",
language = "English (US)",
volume = "155",
pages = "3002--3012",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "6",

}

TY - JOUR

T1 - The identification and cloning of a murine major basic protein gene expressed in eosinophils

AU - Larson, K. A.

AU - Horton, M. A.

AU - Madden, B. J.

AU - Gleich, G. J.

AU - Lee, Nancy A

AU - Lee, J. J.

PY - 1995

Y1 - 1995

N2 - The existence of a murine homologue of the major basic protein (MBP) found in human eosinophil granules was initially hypothesized from structural similarities at the electron microscopic level. The results presented in this study have extended these observations by describing the identification/purification of a mouse MBP (mMBP) and the cloning of the gene encoding this eosinophil granule protein. Using protein purification methodologies with extravascular eosinophils, an mMBP homologue has been identified on the basis of strong (64%) N-terminal sequence homology with the mature human MBP (hMBP). Since hMBP results from a proteolytic cleavage of a precursor molecule, this sequence conservation suggests that the mouse granule protein is processed by a similar mechanism. The gene encoding mMBP was isolated using a hMBP cDNA clone as a heterologous probe in low criteria screens of mouse genomic and cDNA libraries. The genomic structure and nucleotide sequence of the mMBP exons are well conserved with the human gene, although homology alignments of the encoded proteins show that extensive sequence conservation occurs only in the mature portion of the MBP molecules. Expression data demonstrate that this gene is transcriptionally active in tissues containing eosinophil progenitor cells, such as femoral bone marrow. 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. This suggests that, as with guinea pigs, the mouse genome may also encode the eosinophil major basic protein from more than one gene.

AB - The existence of a murine homologue of the major basic protein (MBP) found in human eosinophil granules was initially hypothesized from structural similarities at the electron microscopic level. The results presented in this study have extended these observations by describing the identification/purification of a mouse MBP (mMBP) and the cloning of the gene encoding this eosinophil granule protein. Using protein purification methodologies with extravascular eosinophils, an mMBP homologue has been identified on the basis of strong (64%) N-terminal sequence homology with the mature human MBP (hMBP). Since hMBP results from a proteolytic cleavage of a precursor molecule, this sequence conservation suggests that the mouse granule protein is processed by a similar mechanism. The gene encoding mMBP was isolated using a hMBP cDNA clone as a heterologous probe in low criteria screens of mouse genomic and cDNA libraries. The genomic structure and nucleotide sequence of the mMBP exons are well conserved with the human gene, although homology alignments of the encoded proteins show that extensive sequence conservation occurs only in the mature portion of the MBP molecules. Expression data demonstrate that this gene is transcriptionally active in tissues containing eosinophil progenitor cells, such as femoral bone marrow. 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. This suggests that, as with guinea pigs, the mouse genome may also encode the eosinophil major basic protein from more than one gene.

UR - http://www.scopus.com/inward/record.url?scp=0029056336&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029056336&partnerID=8YFLogxK

M3 - Article

C2 - 7673718

AN - SCOPUS:0029056336

VL - 155

SP - 3002

EP - 3012

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 6

ER -