Eintrag weiter verarbeiten
BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase
Gespeichert in:
| Zeitschriftentitel: | The Journal of Immunology |
|---|---|
| Personen und Körperschaften: | , , , , , , , |
| In: | The Journal of Immunology, 168, 2002, 6, S. 2712-2719 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The American Association of Immunologists
|
| Schlagwörter: |
| author_facet |
Tumang, Joseph R. Negm, Robert S. Solt, Laura A. Schneider, Thomas J. Colarusso, Thomas P. Hastings, William D. Woodland, Robert T. Rothstein, Thomas L. Tumang, Joseph R. Negm, Robert S. Solt, Laura A. Schneider, Thomas J. Colarusso, Thomas P. Hastings, William D. Woodland, Robert T. Rothstein, Thomas L. |
|---|---|
| author |
Tumang, Joseph R. Negm, Robert S. Solt, Laura A. Schneider, Thomas J. Colarusso, Thomas P. Hastings, William D. Woodland, Robert T. Rothstein, Thomas L. |
| spellingShingle |
Tumang, Joseph R. Negm, Robert S. Solt, Laura A. Schneider, Thomas J. Colarusso, Thomas P. Hastings, William D. Woodland, Robert T. Rothstein, Thomas L. The Journal of Immunology BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase Immunology Immunology and Allergy |
| author_sort |
tumang, joseph r. |
| spelling |
Tumang, Joseph R. Negm, Robert S. Solt, Laura A. Schneider, Thomas J. Colarusso, Thomas P. Hastings, William D. Woodland, Robert T. Rothstein, Thomas L. 0022-1767 1550-6606 The American Association of Immunologists Immunology Immunology and Allergy http://dx.doi.org/10.4049/jimmunol.168.6.2712 <jats:title>Abstract</jats:title><jats:p>B cell susceptibility to Fas-mediated apoptosis is regulated in a receptor-specific fashion. CD40 engagement produces marked sensitivity to Fas killing, whereas surface Ig (sIg) engagement blocks Fas signaling for cell death in otherwise sensitive, CD40-stimulated B cell targets, and thus, induces a state of Fas resistance. The signaling mediator, Bruton’s tyrosine kinase (Btk), is required for certain sIg-triggered responses, and Btk is reported to directly bind Fas and block Fas-mediated apoptosis. For these reasons, the role of Btk as a mediator of sIg-induced Fas resistance was examined. Dysfunction of Btk through mutation, and absence of Btk through deletion did not interfere with induction of Fas resistance by anti-Ig. This may be due, at least in part, to induction of Btk-dependent Bcl-2 family members by anti-Ig after CD40 ligand treatment. However, the susceptibility to Fas-mediated apoptosis of B cell targets stimulated by CD40 ligand alone was increased in the absence of Btk. These results indicate that Fas resistance produced by sIg triggering does not require Btk, but suggests that in certain situations Btk modulates B cell susceptibility to Fas killing.</jats:p> BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase The Journal of Immunology |
| doi_str_mv |
10.4049/jimmunol.168.6.2712 |
| facet_avail |
Online Free |
| finc_class_facet |
Medizin |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuNDA0OS9qaW1tdW5vbC4xNjguNi4yNzEy |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuNDA0OS9qaW1tdW5vbC4xNjguNi4yNzEy |
| institution |
DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 |
| imprint |
The American Association of Immunologists, 2002 |
| imprint_str_mv |
The American Association of Immunologists, 2002 |
| issn |
0022-1767 1550-6606 |
| issn_str_mv |
0022-1767 1550-6606 |
| language |
English |
| mega_collection |
The American Association of Immunologists (CrossRef) |
| match_str |
tumang2002bcrengagementinducesfasresistanceinprimarybcellsintheabsenceoffunctionalbrutonstyrosinekinase |
| publishDateSort |
2002 |
| publisher |
The American Association of Immunologists |
| recordtype |
ai |
| record_format |
ai |
| series |
The Journal of Immunology |
| source_id |
49 |
| title |
BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_unstemmed |
BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_full |
BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_fullStr |
BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_full_unstemmed |
BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_short |
BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_sort |
bcr engagement induces fas resistance in primary b cells in the absence of functional bruton’s tyrosine kinase |
| topic |
Immunology Immunology and Allergy |
| url |
http://dx.doi.org/10.4049/jimmunol.168.6.2712 |
| publishDate |
2002 |
| physical |
2712-2719 |
| description |
<jats:title>Abstract</jats:title><jats:p>B cell susceptibility to Fas-mediated apoptosis is regulated in a receptor-specific fashion. CD40 engagement produces marked sensitivity to Fas killing, whereas surface Ig (sIg) engagement blocks Fas signaling for cell death in otherwise sensitive, CD40-stimulated B cell targets, and thus, induces a state of Fas resistance. The signaling mediator, Bruton’s tyrosine kinase (Btk), is required for certain sIg-triggered responses, and Btk is reported to directly bind Fas and block Fas-mediated apoptosis. For these reasons, the role of Btk as a mediator of sIg-induced Fas resistance was examined. Dysfunction of Btk through mutation, and absence of Btk through deletion did not interfere with induction of Fas resistance by anti-Ig. This may be due, at least in part, to induction of Btk-dependent Bcl-2 family members by anti-Ig after CD40 ligand treatment. However, the susceptibility to Fas-mediated apoptosis of B cell targets stimulated by CD40 ligand alone was increased in the absence of Btk. These results indicate that Fas resistance produced by sIg triggering does not require Btk, but suggests that in certain situations Btk modulates B cell susceptibility to Fas killing.</jats:p> |
| container_issue |
6 |
| container_start_page |
2712 |
| container_title |
The Journal of Immunology |
| container_volume |
168 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792333322125312003 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T14:10:55.356Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=BCR+Engagement+Induces+Fas+Resistance+in+Primary+B+Cells+in+the+Absence+of+Functional+Bruton%E2%80%99s+Tyrosine+Kinase&rft.date=2002-03-15&genre=article&issn=1550-6606&volume=168&issue=6&spage=2712&epage=2719&pages=2712-2719&jtitle=The+Journal+of+Immunology&atitle=BCR+Engagement+Induces+Fas+Resistance+in+Primary+B+Cells+in+the+Absence+of+Functional+Bruton%E2%80%99s+Tyrosine+Kinase&aulast=Rothstein&aufirst=Thomas+L.&rft_id=info%3Adoi%2F10.4049%2Fjimmunol.168.6.2712&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792333322125312003 |
| author | Tumang, Joseph R., Negm, Robert S., Solt, Laura A., Schneider, Thomas J., Colarusso, Thomas P., Hastings, William D., Woodland, Robert T., Rothstein, Thomas L. |
| author_facet | Tumang, Joseph R., Negm, Robert S., Solt, Laura A., Schneider, Thomas J., Colarusso, Thomas P., Hastings, William D., Woodland, Robert T., Rothstein, Thomas L., Tumang, Joseph R., Negm, Robert S., Solt, Laura A., Schneider, Thomas J., Colarusso, Thomas P., Hastings, William D., Woodland, Robert T., Rothstein, Thomas L. |
| author_sort | tumang, joseph r. |
| container_issue | 6 |
| container_start_page | 2712 |
| container_title | The Journal of Immunology |
| container_volume | 168 |
| description | <jats:title>Abstract</jats:title><jats:p>B cell susceptibility to Fas-mediated apoptosis is regulated in a receptor-specific fashion. CD40 engagement produces marked sensitivity to Fas killing, whereas surface Ig (sIg) engagement blocks Fas signaling for cell death in otherwise sensitive, CD40-stimulated B cell targets, and thus, induces a state of Fas resistance. The signaling mediator, Bruton’s tyrosine kinase (Btk), is required for certain sIg-triggered responses, and Btk is reported to directly bind Fas and block Fas-mediated apoptosis. For these reasons, the role of Btk as a mediator of sIg-induced Fas resistance was examined. Dysfunction of Btk through mutation, and absence of Btk through deletion did not interfere with induction of Fas resistance by anti-Ig. This may be due, at least in part, to induction of Btk-dependent Bcl-2 family members by anti-Ig after CD40 ligand treatment. However, the susceptibility to Fas-mediated apoptosis of B cell targets stimulated by CD40 ligand alone was increased in the absence of Btk. These results indicate that Fas resistance produced by sIg triggering does not require Btk, but suggests that in certain situations Btk modulates B cell susceptibility to Fas killing.</jats:p> |
| doi_str_mv | 10.4049/jimmunol.168.6.2712 |
| facet_avail | Online, Free |
| finc_class_facet | Medizin |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuNDA0OS9qaW1tdW5vbC4xNjguNi4yNzEy |
| imprint | The American Association of Immunologists, 2002 |
| imprint_str_mv | The American Association of Immunologists, 2002 |
| institution | DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1 |
| issn | 0022-1767, 1550-6606 |
| issn_str_mv | 0022-1767, 1550-6606 |
| language | English |
| last_indexed | 2024-03-01T14:10:55.356Z |
| match_str | tumang2002bcrengagementinducesfasresistanceinprimarybcellsintheabsenceoffunctionalbrutonstyrosinekinase |
| mega_collection | The American Association of Immunologists (CrossRef) |
| physical | 2712-2719 |
| publishDate | 2002 |
| publishDateSort | 2002 |
| publisher | The American Association of Immunologists |
| record_format | ai |
| recordtype | ai |
| series | The Journal of Immunology |
| source_id | 49 |
| spelling | Tumang, Joseph R. Negm, Robert S. Solt, Laura A. Schneider, Thomas J. Colarusso, Thomas P. Hastings, William D. Woodland, Robert T. Rothstein, Thomas L. 0022-1767 1550-6606 The American Association of Immunologists Immunology Immunology and Allergy http://dx.doi.org/10.4049/jimmunol.168.6.2712 <jats:title>Abstract</jats:title><jats:p>B cell susceptibility to Fas-mediated apoptosis is regulated in a receptor-specific fashion. CD40 engagement produces marked sensitivity to Fas killing, whereas surface Ig (sIg) engagement blocks Fas signaling for cell death in otherwise sensitive, CD40-stimulated B cell targets, and thus, induces a state of Fas resistance. The signaling mediator, Bruton’s tyrosine kinase (Btk), is required for certain sIg-triggered responses, and Btk is reported to directly bind Fas and block Fas-mediated apoptosis. For these reasons, the role of Btk as a mediator of sIg-induced Fas resistance was examined. Dysfunction of Btk through mutation, and absence of Btk through deletion did not interfere with induction of Fas resistance by anti-Ig. This may be due, at least in part, to induction of Btk-dependent Bcl-2 family members by anti-Ig after CD40 ligand treatment. However, the susceptibility to Fas-mediated apoptosis of B cell targets stimulated by CD40 ligand alone was increased in the absence of Btk. These results indicate that Fas resistance produced by sIg triggering does not require Btk, but suggests that in certain situations Btk modulates B cell susceptibility to Fas killing.</jats:p> BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase The Journal of Immunology |
| spellingShingle | Tumang, Joseph R., Negm, Robert S., Solt, Laura A., Schneider, Thomas J., Colarusso, Thomas P., Hastings, William D., Woodland, Robert T., Rothstein, Thomas L., The Journal of Immunology, BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase, Immunology, Immunology and Allergy |
| title | BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_full | BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_fullStr | BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_full_unstemmed | BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_short | BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| title_sort | bcr engagement induces fas resistance in primary b cells in the absence of functional bruton’s tyrosine kinase |
| title_unstemmed | BCR Engagement Induces Fas Resistance in Primary B Cells in the Absence of Functional Bruton’s Tyrosine Kinase |
| topic | Immunology, Immunology and Allergy |
| url | http://dx.doi.org/10.4049/jimmunol.168.6.2712 |