Abstract
The ultrastructural localization of Charcot-Leyden crystal (CLC) protein during f-Met-peptide-induced degranulation of human basophils was analyzed at multiple times after stimulation. In this secretion model, piecemeal and anaphylactic degranulation occurred sequentially in stimulated cells and were followed by reconstitution of granule contents. This analysis showed that granule number and alteration and location of gold-labeled, formed CLCs changed over time. CLCs were extruded from granules and remained attached to plasma membranes early after stimulation. At later times, similar structures reappeared in granules in quantity. Smooth-membrane-bound vesicles, analyzed by number, by visible particle contents (or lack of contents) and by gold labeling for CLC protein, showed that empty vesicles increased at the earliest time sampled (0 time) and plunged thereafter in actively extruding and completely degranulated cells. Vesicles containing granule particles were elevated initially at 10 s and at later times. Gold-labeled CLC-protein-containing vesicles were of either empty or particle-filled varieties, and both types were involved with CLC protein transport out of cells at early times and into cells at later times as basophils recovered. Thus, vesicle transport of CLC protein is a mechanism for producing piecemeal degranulation and endocytotic recovery of released CLC protein from human basophils. This vesicular shuttle may be an effector mechanism for widespread piecemeal losses from granules in basophils in inflammatory sites in vivo in human disease.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 465-477 |
| Number of pages | 13 |
| Journal | International Archives of Allergy and Immunology |
| Volume | 113 |
| Issue number | 4 |
| State | Published - Aug 1997 |
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Keywords
- Anaphylactic degranulation
- Eosinophil
- Mast cell
- Piecemeal degranulation
- Secretion
- Vesicular transport
ASJC Scopus subject areas
- Immunology and Allergy
- Immunology
Cite this
Vesicular transport of Charcot-Leyden crystal protein in f-Met peptide-stimulated human basophils. / Dvorak, Ann M.; Macglashan, Donald; Warner, Jane A.; Letourneau, Linda; Morgan, Ellen S.; Lichtenstein, Lawrence M.; Ackerman, Steven J.
In: International Archives of Allergy and Immunology, Vol. 113, No. 4, 08.1997, p. 465-477.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Vesicular transport of Charcot-Leyden crystal protein in f-Met peptide-stimulated human basophils
AU - Dvorak, Ann M.
AU - Macglashan, Donald
AU - Warner, Jane A.
AU - Letourneau, Linda
AU - Morgan, Ellen S.
AU - Lichtenstein, Lawrence M.
AU - Ackerman, Steven J.
PY - 1997/8
Y1 - 1997/8
N2 - The ultrastructural localization of Charcot-Leyden crystal (CLC) protein during f-Met-peptide-induced degranulation of human basophils was analyzed at multiple times after stimulation. In this secretion model, piecemeal and anaphylactic degranulation occurred sequentially in stimulated cells and were followed by reconstitution of granule contents. This analysis showed that granule number and alteration and location of gold-labeled, formed CLCs changed over time. CLCs were extruded from granules and remained attached to plasma membranes early after stimulation. At later times, similar structures reappeared in granules in quantity. Smooth-membrane-bound vesicles, analyzed by number, by visible particle contents (or lack of contents) and by gold labeling for CLC protein, showed that empty vesicles increased at the earliest time sampled (0 time) and plunged thereafter in actively extruding and completely degranulated cells. Vesicles containing granule particles were elevated initially at 10 s and at later times. Gold-labeled CLC-protein-containing vesicles were of either empty or particle-filled varieties, and both types were involved with CLC protein transport out of cells at early times and into cells at later times as basophils recovered. Thus, vesicle transport of CLC protein is a mechanism for producing piecemeal degranulation and endocytotic recovery of released CLC protein from human basophils. This vesicular shuttle may be an effector mechanism for widespread piecemeal losses from granules in basophils in inflammatory sites in vivo in human disease.
AB - The ultrastructural localization of Charcot-Leyden crystal (CLC) protein during f-Met-peptide-induced degranulation of human basophils was analyzed at multiple times after stimulation. In this secretion model, piecemeal and anaphylactic degranulation occurred sequentially in stimulated cells and were followed by reconstitution of granule contents. This analysis showed that granule number and alteration and location of gold-labeled, formed CLCs changed over time. CLCs were extruded from granules and remained attached to plasma membranes early after stimulation. At later times, similar structures reappeared in granules in quantity. Smooth-membrane-bound vesicles, analyzed by number, by visible particle contents (or lack of contents) and by gold labeling for CLC protein, showed that empty vesicles increased at the earliest time sampled (0 time) and plunged thereafter in actively extruding and completely degranulated cells. Vesicles containing granule particles were elevated initially at 10 s and at later times. Gold-labeled CLC-protein-containing vesicles were of either empty or particle-filled varieties, and both types were involved with CLC protein transport out of cells at early times and into cells at later times as basophils recovered. Thus, vesicle transport of CLC protein is a mechanism for producing piecemeal degranulation and endocytotic recovery of released CLC protein from human basophils. This vesicular shuttle may be an effector mechanism for widespread piecemeal losses from granules in basophils in inflammatory sites in vivo in human disease.
KW - Anaphylactic degranulation
KW - Eosinophil
KW - Mast cell
KW - Piecemeal degranulation
KW - Secretion
KW - Vesicular transport
UR - http://www.scopus.com/inward/record.url?scp=0030835971&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030835971&partnerID=8YFLogxK
M3 - Article
C2 - 9250593
AN - SCOPUS:0030835971
VL - 113
SP - 465
EP - 477
JO - International Archives of Allergy and Immunology
JF - International Archives of Allergy and Immunology
SN - 1018-2438
IS - 4
ER -