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

McGrogan, Michael; Simonsen, Christian C.; Scott, Randy W.; Griffith, J E; Ellis, Nathan A.; Kennedy, Jackie; Campanelli, David; Nathan, Carl; Gabay, Joëlle E.

doi:10.1084/jem.168.6.2295

Cited by 51 publications

(38 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…ECP mRNA was not present in HL-60 cells induced toward neutrophilic (DMSO) differentiation, nor was it present in peripheral blood neutrophils. In support of these findings, induction of HL-60 cells with DMSO leads to a diminution of other eosinophil-specific characteristics, including a decrease in Biebrich scarlet staining (63,64), and reduced mRNA transcription for (65) and biosynthesis of MBP (63).…”

Section: Resultsmentioning

confidence: 52%

Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity.

Rosenberg

Ackerman

Tenen

1989

The Journal of Experimental Medicine

143

View full text Add to dashboard Cite

The eosinophil cationic protein (ECP)' is one of several small, distinct argininerich proteins that have been isolated from the eosinophil's large specific granule. The molecular mass of human ECP has been estimated at 18-21 kD (1-3), depending on the degree of glycosylation (3). ECP has been shown to possess a wide variety of biological activities, including the ability to stimulate factor XII-dependent coagulation pathways (4), to neutralize the anticoagulant effects of heparin (5), and to inhibit lymphocyte proliferation induced by PHA or mixed lymphocyte reactions (6) . ECP is a potent cytotoxin; ECP-containing supernatants of activated eosinophils have been shown to be toxic to isolated myocardial cells in vitro (7), and both ECP and the eosinophil granule major basic protein (MBP) were found in the endothelial and endomyocardial lesions characteristic of the hypereosinophilic syndrome (8). Furthermore, ECP is also a potent helminthotoxin; destruction of schistosomula of Schistosoma mansont was reported at concentrations as low as 10' M (8-10-fold more active than MBP) (9, 10) . ECP has also been shown to kill trypomastigote and amastigote stages of Trypanosoma cruzi (11) . Both ECP and the related granule protein, eosinophil-derived neurotoxin (EDN), induce the neurotoxic effect known as the Gordon phenomenon (12)

show abstract

Section: Resultsmentioning

confidence: 52%

Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity.

Rosenberg

Ackerman

Tenen

1989

The Journal of Experimental Medicine

143

View full text Add to dashboard Cite

show abstract

“…Furthermore, in eosinophil proMBP (McGrogan et al, 1988;Barker et al, 1988), the strongly acidic, 90-residue pro sequence has been hypothesized to mask the toxic effects of the highly cationic, mature MBP, thereby protecting the cell from membrane damage during processing. While the p l of bactenecins has been calculated to be higher than 13 (see the amino acid sequence in Frank et al, 1990), both probactenecins have a pZ around 8, implying that their pro sequence is also acidic.…”

Section: Discussionmentioning

confidence: 99%

Proteolytic cleavage by neutrophil elastase converts inactive storage proforms to antibacterial bactenecins

Scocchi

Skerlavaj

Romeo

et al. 1992

European Journal of Biochemistry

145

107

View full text Add to dashboard Cite

Bac5 and Bac7, antibiotics of the bactenecin (proline/arginine‐rich peptide) family, are stored as proforms in the large granules of bovine neutrophils [Zanetti, M., Litteri, L., Gennaro, R., Horstmann, H. and Romeo, D. (1990) J. Cell Biol. 111, 1363–1371]. These proforms have been purified to homogeneity from granule extracts by immunoaffinity and reverse‐phase chromatography. While mature bactenecins efficiently kill Escherichia coli, Klebsiella pneumoniae and Salmonella typhimurium with minimal inhibitory concentrations of 6–12 μg/ml, proBac5 and proBac7 do not affect the growth of the same microorganisms, even at 500 μg/ml. Previous investigations have suggested that the conversion of probactenecins into mature antimicrobial peptides is catalyzed by a neutral serine protease stored in the azurophil granules. Purified proBac5 and proBac7 were thus treated with elastase, cathepsin G or proteinase 3, which constitute the pool of neutral serine proteases of the azurophils, and the reaction products were identified by Western blot analysis, mass spectrometry, and N‐terminal sequence analysis. Of the three proteases, only elastase is able to catalyze the stepwise cleavage of probactenecins into the corresponding mature peptides, which have the same mass, N‐terminal sequence and antibiotic activity of authentic Bac5 and Bac7. These results point to the importance of cooperation between azurophils and large granules in mounting a defense reaction.

show abstract

“…Each of these proteins have been cloned and their biochemical and functional properties are well-established [81][82][83][84][85][86][87][88]. The most abundant cationic eosinophil granule protein is MBP.…”

Section: Preformed Granular Constituentsmentioning

confidence: 99%

“…The most abundant cationic eosinophil granule protein is MBP. It is an arginine residue rich 14 kDa protein [82,83,85] devoid of any enzymatic activity, but highly toxic to helminthic parasites, tumour cells, and other mammalian cells and tissues. As will be outlined below, MBP has toxic properties independent of oxygen metabolism.…”

Section: Preformed Granular Constituentsmentioning

confidence: 99%

Pulmonary immune cells in health and disease: the eosinophil leucocyte (Part I)

Kroegel¹,

Virchow²,

Luttmann³

et al. 1994

Eur Respir J

129

View full text Add to dashboard Cite

P Pu ul lm mo on na ar ry y i im mm mu un ne e c ce el ll ls s i in n h he ea al lt th h a an nd d d di is se ea as se e: : t th he e e eo os si in no op ph hi il l l le eu uc co oc cy yt te e ( (P Pa ar rt t I I) ) ABSTRACT: Increasing evidence has accumulated to suggest that eosinophils play a key role in the pathogenesis of asthma and other pulmonary diseases by damaging infiltrated bronchial tissue and lung parenchyma. The first part of this review on eosinophils describes the cellular characteristics and properties of the cell, which help in understanding its role in disease. The article focuses on origin, maturation and differentiation of the eosinophil, its morphological and phenotypical properties, as well as its preformed and newly generated mediators of inflammation. The cause and putative significance of eosinophil heterogeneity in respect to function and density will also be discussed. In addition, the naturally occurring mediators through which eosinophils are activated and communicate with other inflammatory cells are outlined.The first part closes with new aspects of eosinophil recruitment from the circulation into perivascular tissue, including nonselective and putative selective adhesion mechanisms and chemotaxis.

show abstract

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

Cited by 51 publications

References 42 publications

Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity.

Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity.

Proteolytic cleavage by neutrophil elastase converts inactive storage proforms to antibacterial bactenecins

Pulmonary immune cells in health and disease: the eosinophil leucocyte (Part I)

Contact Info

Product

Resources

About