In:
The Journal of Immunology, The American Association of Immunologists, Vol. 119, No. 5 ( 1977-11-01), p. 1744-1750
Abstract:
Human eosinophils, obtained in greater than 90% purity from patients with idiopathic hypereosinophilia, were found to adhere to serum-treated Sepharose beads and to release granule-associated enzymes. The release of aryl-sulfatase, an eosinophil-specific enzyme, was found to occur during a 60-min time period and to be dependent upon the presence of serum or a component of serum coating the Sepharose beads. IgG was examined as a possible opsonic factor and no significant role was evident. The factor in serum responsible for inducing eosinophil adherence and enzyme release was heat-labile and was not generated in C3-deficient serum, but was formed upon reconstitution of C3-deficient serum with purified human C3. The activation of the Sepharose particles by normal human serum was found to be dependent upon the presence of magnesium but not calcium, and to occur normally in C2, C4, C5, and C6-deficient sera, suggesting a requirement for the activation of C by the alternative pathway. With 125I anti-C3b/c, serum-exposed Sepharose was shown to exhibit C3b/c on its surface. Furthermore, human RBC were observed to adhere to serumtreated Sepharose consistent with the presence of C3b on the bead surface. Although the opsonic factor has not been directly identified, the concordance appreciated between the loss of immune adherence and the capacity of serum-treated Sepharose to generate aryl-sulfatase release after heating in 2 M salt as well as after trypsin treatment suggests that both phenomena may be related. Thus, eosinophils encountering a noningestible surface capable of activating the alternative C pathway may adhere to that surface and release granule-associated enzymes.
Type of Medium:
Online Resource
ISSN:
0022-1767
,
1550-6606
DOI:
10.4049/jimmunol.119.5.1744
Language:
English
Publisher:
The American Association of Immunologists
Publication Date:
1977
detail.hit.zdb_id:
1475085-5
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