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Article ; Online: Monitoring Protein Endocytosis and Recycling Using FACS-Based Assays.

Walseng, Even / Roche, Paul A

Methods in molecular biology (Clifton, N.J.)

2019 Volume 1988, Page(s) 279–288

Abstract: ... to the plasma membrane. This assay allows for quantitation of trafficking of proteins on even rare subsets of cells ...

Abstract	Cell surface MHC class II (MHC-II) is known to internalize and can recycle back to the plasma membrane from endosomes in antigen presenting cells. We now describe a simple protocol that allows one to follow the internalization kinetics of proteins from the surface of cells. Furthermore, a simple adaptation of this assay allows one to monitor the rate of appearance of internalized proteins back to the plasma membrane. This assay allows for quantitation of trafficking of proteins on even rare subsets of cells, something that is not possible with traditional biochemical assays.
MeSH term(s)	Antibodies/metabolism ; Biological Assay/methods ; Dendritic Cells/metabolism ; Endocytosis ; Flow Cytometry/methods ; HeLa Cells ; Histocompatibility Antigens Class II/metabolism ; Humans
Chemical Substances	Antibodies ; Histocompatibility Antigens Class II
Language	English
Publishing date	2019-05-30
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-9450-2_20
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Article ; Online: Conformation-selective rather than avidity-based binding to tumor associated antigen derived peptide-MHC enables targeting of WT1-pMHC low expressing cancer cells by anti-WT1-pMHC/CD3 T cell engagers.

Walseng, Even / Wang, Bo / Yang, Chunning / Patel, Pooja / Zhao, Chihao / Zhang, Hanzhi / Zhao, Peng / Mazor, Yariv

Frontiers in immunology

2023 Volume 14, Page(s) 1275304

Abstract: T cell engagers, a category of T cell-retargeting immunotherapy, are rapidly transforming clinical cancer care. However, the lack of tumor-specific targets poses a significant roadblock for broad adaptation of this therapeutic modality in many ... ...

Abstract	T cell engagers, a category of T cell-retargeting immunotherapy, are rapidly transforming clinical cancer care. However, the lack of tumor-specific targets poses a significant roadblock for broad adaptation of this therapeutic modality in many indications, often resulting in systemic on-target off-tumor toxicity. Though various tumor-derived intracellular mutations provide a massive pool of potential tumor-specific antigens, targeting them is extremely challenging, partly due to the low copy number of tumor associated antigen (TAA)-derived pMHC on tumor cell surface. Further, the interplay of binding geometry and format valency in relation to the capacity of a T cell engager to efficiently target low density cell-surface pMHC is not well understood. Using the Wilms' tumor 1 (WT1) oncoprotein as a proof-of-principle TAA, combined with an array of IgG-like T cell engager modalities that differ in their anti-TAA valency and binding geometry, we show that the ability to induce an immunological synapse formation, resulting in potent killing of WT1 positive cancer cell lines is primarily dependent on the distinct geometrical conformations between the Fab arms of anti-WT1-HLA-A02:01 and anti-CD3. The augmented avidity conferred by the binding of two anti-WT1-HLA-A02:01 Fab arms has only minimal influence on cell killing potency. These findings demonstrate the need for careful examination of key design parameters for the development of next-generation T cell engagers targeting low density TAA-pMHCs on tumor cells.
MeSH term(s)	Humans ; T-Lymphocytes ; WT1 Proteins/genetics ; Neoplasms/genetics ; Neoplasms/therapy ; Antigens, Neoplasm ; Immunoproteins ; HLA-A Antigens ; Peptides
Chemical Substances	WT1 Proteins ; Antigens, Neoplasm ; Immunoproteins ; HLA-A Antigens ; Peptides ; WT1 protein, human
Language	English
Publishing date	2023-11-10
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2023.1275304
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Article ; Online: Robust production of monovalent bispecific IgG antibodies through novel electrostatic steering mutations at the C

mAbs

2023 Volume 15, Issue 1, Page(s) 2273449

Abstract: Bispecific antibodies represent an increasingly large fraction of biologics in therapeutic development due to their expanded scope in functional capabilities. Asymmetric monovalent bispecific IgGs (bsIgGs) have the additional advantage of maintaining a ... ...

Abstract	Bispecific antibodies represent an increasingly large fraction of biologics in therapeutic development due to their expanded scope in functional capabilities. Asymmetric monovalent bispecific IgGs (bsIgGs) have the additional advantage of maintaining a native antibody-like structure, which can provide favorable pharmacology and pharmacokinetic profiles. The production of correctly assembled asymmetric monovalent bsIgGs, however, is a complex engineering endeavor due to the propensity for non-cognate heavy and light chains to mis-pair. Previously, we introduced the DuetMab platform as a general solution for the production of bsIgGs, which utilizes an engineered interchain disulfide bond in one of the C
MeSH term(s)	Antibodies, Bispecific/genetics ; Static Electricity ; Disulfides ; Mutation ; Immunoglobulin G/genetics
Chemical Substances	Antibodies, Bispecific ; Disulfides ; Immunoglobulin G
Language	English
Publishing date	2023-11-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2537838-7
ISSN	1942-0870 ; 1942-0870
ISSN (online)	1942-0870
ISSN	1942-0870
DOI	10.1080/19420862.2023.2273449
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Article ; Online: Ubiquitination by March-I prevents MHC class II recycling and promotes MHC class II turnover in antigen-presenting cells.

Cho, Kyung-Jin / Walseng, Even / Ishido, Satoshi / Roche, Paul A

Proceedings of the National Academy of Sciences of the United States of America

2015 Volume 112, Issue 33, Page(s) 10449–10454

Abstract: MHC class II (MHC-II)-dependent antigen presentation by antigen-presenting cells (APCs) is carefully controlled to achieve specificity of immune responses; the regulated assembly and degradation of antigenic peptide-MHC-II complexes (pMHC-II) is one ... ...

Abstract	MHC class II (MHC-II)-dependent antigen presentation by antigen-presenting cells (APCs) is carefully controlled to achieve specificity of immune responses; the regulated assembly and degradation of antigenic peptide-MHC-II complexes (pMHC-II) is one aspect of such control. In this study, we have examined the role of ubiquitination in regulating pMHC-II biosynthesis, endocytosis, recycling, and turnover in APCs. By using APCs obtained from MHC-II ubiquitination mutant mice, we find that whereas ubiquitination does not affect pMHC-II formation in dendritic cells (DCs), it does promote the subsequent degradation of newly synthesized pMHC-II. Acute activation of DCs or B cells terminates expression of the MHC-II E3 ubiquitin ligase March-I and prevents pMHC-II ubiquitination. Most importantly, this change results in very efficient pMHC-II recycling from the surface of DCs and B cells, thereby preventing targeting of internalized pMHC-II to lysosomes for degradation. Biochemical and functional assays confirmed that pMHC-II turnover is suppressed in MHC-II ubiquitin mutant DCs or by acute activation of wild-type DCs. These studies demonstrate that acute APC activation blocks the ubiquitin-dependent turnover of pMHC-II by promoting efficient pMHC-II recycling and preventing lysosomal targeting of internalized pMHC-II, thereby enhancing pMHC-II stability for efficient antigen presentation to CD4 T cells.
MeSH term(s)	Animals ; Antigen Presentation ; Antigen-Presenting Cells/cytology ; B-Lymphocytes/cytology ; CD4-Positive T-Lymphocytes/cytology ; Dendritic Cells/cytology ; Endocytosis ; Histocompatibility Antigens Class II/chemistry ; Lipopolysaccharides/chemistry ; Lysosomes/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Peptides/chemistry ; Ubiquitin/chemistry ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/physiology
Chemical Substances	Histocompatibility Antigens Class II ; Lipopolysaccharides ; Peptides ; Ubiquitin ; MARCH1 protein, mouse (EC 2.3.2.27) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2015-08-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1507981112
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Article ; Online: Internalizing MHC class II-peptide complexes are ubiquitinated in early endosomes and targeted for lysosomal degradation.

Furuta, Kazuyuki / Walseng, Even / Roche, Paul A

Proceedings of the National Academy of Sciences of the United States of America

2013 Volume 110, Issue 50, Page(s) 20188–20193

Abstract: As sentinels of the immune system, dendritic cells (DCs) continuously generate and turnover antigenic peptide-MHC class II complexes (pMHC-II). pMHC-II generation is a complex process that involves many well-characterized MHC-II biosynthetic ... ...

Abstract	As sentinels of the immune system, dendritic cells (DCs) continuously generate and turnover antigenic peptide-MHC class II complexes (pMHC-II). pMHC-II generation is a complex process that involves many well-characterized MHC-II biosynthetic intermediates; however, the mechanisms leading to MHC-II turnover/degradation are poorly understood. We now show that pMHC-II complexes undergoing clathrin-independent endocytosis from the DC surface are efficiently ubiquitinated by the E3 ubiquitin ligase March-I in early endosomes, whereas biosynthetically immature MHC-II-Invariant chain (Ii) complexes are not. The inability of MHC-II-Ii to serve as a March-I substrate is a consequence of Ii sorting motifs that divert the MHC-II-Ii complex away from March-I(+) early endosomes. When these sorting motifs are mutated, or when clathrin-mediated endocytosis is inhibited, MHC-II-Ii complexes internalize by using a clathrin-independent endocytosis pathway and are now ubiquitinated as efficiently as pMHC-II complexes. These data show that the selective ubiquitination of internalizing surface pMHC-II in March-I(+) early endosomes promotes degradation of "old" pMHC-II and spares forms of MHC-II that have not yet loaded antigenic peptides or have not yet reached the DC surface.
MeSH term(s)	Biotinylation ; Dendritic Cells/immunology ; Endosomes/metabolism ; Genes, MHC Class II/genetics ; HEK293 Cells ; HeLa Cells ; Humans ; Immunoblotting ; Immunoprecipitation ; Lysosomes/metabolism ; Multiprotein Complexes/genetics ; Multiprotein Complexes/immunology ; Multiprotein Complexes/metabolism ; Peptides/immunology ; Peptides/metabolism ; Proteolysis ; RNA, Small Interfering/genetics ; Ubiquitination
Chemical Substances	Multiprotein Complexes ; Peptides ; RNA, Small Interfering
Language	English
Publishing date	2013-11-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1312994110
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Article ; Online: Harnessing a catalytic lysine residue for the one-step preparation of homogeneous antibody-drug conjugates.

Nanna, Alex R / Li, Xiuling / Walseng, Even / Pedzisa, Lee / Goydel, Rebecca S / Hymel, David / Burke, Terrence R / Roush, William R / Rader, Christoph

Nature communications

2017 Volume 8, Issue 1, Page(s) 1112

Abstract: Current strategies to produce homogeneous antibody-drug conjugates (ADCs) rely on mutations or inefficient conjugation chemistries. Here we present a strategy to produce site-specific ADCs using a highly reactive natural buried lysine embedded in a dual ... ...

Abstract	Current strategies to produce homogeneous antibody-drug conjugates (ADCs) rely on mutations or inefficient conjugation chemistries. Here we present a strategy to produce site-specific ADCs using a highly reactive natural buried lysine embedded in a dual variable domain (DVD) format. This approach is mutation free and drug conjugation proceeds rapidly at neutral pH in a single step without removing any charges. The conjugation chemistry is highly robust, enabling the use of crude DVD for ADC preparation. In addition, this strategy affords the ability to precisely monitor the efficiency of drug conjugation with a catalytic assay. ADCs targeting HER2 were prepared and demonstrated to be highly potent and specific in vitro and in vivo. Furthermore, the modular DVD platform was used to prepare potent and specific ADCs targeting CD138 and CD79B, two clinically established targets overexpressed in multiple myeloma and non-Hodgkin lymphoma, respectively.
MeSH term(s)	Animals ; Antineoplastic Agents/chemistry ; Catalysis ; Cell Line, Tumor ; Chemistry, Pharmaceutical ; Epitopes, T-Lymphocyte/chemistry ; Female ; Humans ; Hydrogen-Ion Concentration ; Immunoconjugates/chemistry ; K562 Cells ; Lymphoma, Non-Hodgkin/drug therapy ; Lysine/chemistry ; Mice ; Multiple Myeloma/drug therapy ; Mutation ; Neoplasm Transplantation ; Pharmaceutical Preparations/chemistry ; Syndecan-1/chemistry ; Trastuzumab/chemistry ; Xenograft Model Antitumor Assays ; beta-Lactams/chemistry
Chemical Substances	Antineoplastic Agents ; Epitopes, T-Lymphocyte ; Immunoconjugates ; Pharmaceutical Preparations ; SDC1 protein, human ; Syndecan-1 ; beta-Lactams ; Lysine (K3Z4F929H6) ; Trastuzumab (P188ANX8CK)
Language	English
Publishing date	2017-10-24
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ISSN	2041-1723
ISSN (online)	2041-1723
DOI	10.1038/s41467-017-01257-1
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Article ; Online: A TCR-based Chimeric Antigen Receptor.

Walseng, Even / Köksal, Hakan / Sektioglu, Ibrahim M / Fåne, Anne / Skorstad, Gjertrud / Kvalheim, Gunnar / Gaudernack, Gustav / Inderberg, Else Marit / Wälchli, Sébastien

Scientific reports

2017 Volume 7, Issue 1, Page(s) 10713

Abstract: Effector T cells equipped with engineered antigen receptors specific for cancer targets have proven to be very efficient. Two methods have emerged: the Chimeric Antigen Receptors (CARs) and T-cell Receptor (TCR) redirection. Although very potent, CAR ... ...

Abstract	Effector T cells equipped with engineered antigen receptors specific for cancer targets have proven to be very efficient. Two methods have emerged: the Chimeric Antigen Receptors (CARs) and T-cell Receptor (TCR) redirection. Although very potent, CAR recognition is limited to membrane antigens which represent around 1% of the total proteins expressed, whereas TCRs have the advantage of targeting any peptide resulting from cellular protein degradation. However, TCRs depend on heavy signalling machinery only present in T cells which restricts the type of eligible therapeutic cells. Hence, an introduced therapeutic TCR will compete with the endogenous TCR for the signalling proteins and carries the potential risk of mixed dimer formation giving rise to a new TCR with unpredictable specificity. We have fused a soluble TCR construct to a CAR-signalling tail and named the final product TCR-CAR. We here show that, if expressed, the TCR-CAR conserved the specificity and the functionality of the original TCR. In addition, we demonstrate that TCR-CAR redirection was not restricted to T cells. Indeed, after transduction, the NK cell line NK-92 became TCR positive and reacted against pMHC target. This opens therapeutic avenues combing the killing efficiency of NK cells with the diversified target recognition of TCRs.
MeSH term(s)	Cell Line, Tumor ; Cytokines/metabolism ; Cytotoxicity, Immunologic ; Flow Cytometry ; Gene Expression ; Gene Order ; Genetic Vectors/genetics ; Histocompatibility Antigens Class I/immunology ; Histocompatibility Antigens Class I/metabolism ; Humans ; Immunotherapy, Adoptive ; Killer Cells, Natural/immunology ; Killer Cells, Natural/metabolism ; Protein Interaction Domains and Motifs/genetics ; Receptors, Antigen, T-Cell/chemistry ; Receptors, Antigen, T-Cell/genetics ; Receptors, Antigen, T-Cell/metabolism ; Receptors, Chimeric Antigen/chemistry ; Receptors, Chimeric Antigen/genetics ; Receptors, Chimeric Antigen/metabolism ; Recombinant Fusion Proteins ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism ; Transduction, Genetic
Chemical Substances	Cytokines ; Histocompatibility Antigens Class I ; Receptors, Antigen, T-Cell ; Receptors, Chimeric Antigen ; Recombinant Fusion Proteins
Language	English
Publishing date	2017-09-06
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-11126-y
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Article ; Online: A TCR-based Chimeric Antigen Receptor

Even Walseng / Hakan Köksal / Ibrahim M. Sektioglu / Anne Fåne / Gjertrud Skorstad / Gunnar Kvalheim / Gustav Gaudernack / Else Marit Inderberg / Sébastien Wälchli

Scientific Reports, Vol 7, Iss 1, Pp 1-

2017 Volume 10

Abstract: Abstract Effector T cells equipped with engineered antigen receptors specific for cancer targets have proven to be very efficient. Two methods have emerged: the Chimeric Antigen Receptors (CARs) and T-cell Receptor (TCR) redirection. Although very potent, ...

Abstract	Abstract Effector T cells equipped with engineered antigen receptors specific for cancer targets have proven to be very efficient. Two methods have emerged: the Chimeric Antigen Receptors (CARs) and T-cell Receptor (TCR) redirection. Although very potent, CAR recognition is limited to membrane antigens which represent around 1% of the total proteins expressed, whereas TCRs have the advantage of targeting any peptide resulting from cellular protein degradation. However, TCRs depend on heavy signalling machinery only present in T cells which restricts the type of eligible therapeutic cells. Hence, an introduced therapeutic TCR will compete with the endogenous TCR for the signalling proteins and carries the potential risk of mixed dimer formation giving rise to a new TCR with unpredictable specificity. We have fused a soluble TCR construct to a CAR-signalling tail and named the final product TCR-CAR. We here show that, if expressed, the TCR-CAR conserved the specificity and the functionality of the original TCR. In addition, we demonstrate that TCR-CAR redirection was not restricted to T cells. Indeed, after transduction, the NK cell line NK-92 became TCR positive and reacted against pMHC target. This opens therapeutic avenues combing the killing efficiency of NK cells with the diversified target recognition of TCRs.
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publishing date	2017-09-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article: Major histocompatibility complex class II-peptide complexes internalize using a clathrin- and dynamin-independent endocytosis pathway.

Walseng, Even / Bakke, Oddmund / Roche, Paul A

The Journal of biological chemistry

2008 Volume 283, Issue 21, Page(s) 14717–14727

Abstract: Major histocompatibility complex (MHC) class II molecules (MHC-II) function by binding antigenic peptides and displaying these peptides on the surface of antigen presenting cells (APCs) for recognition by peptide-MHC-II (pMHC-II)-specific CD4 T cells. It ...

Abstract	Major histocompatibility complex (MHC) class II molecules (MHC-II) function by binding antigenic peptides and displaying these peptides on the surface of antigen presenting cells (APCs) for recognition by peptide-MHC-II (pMHC-II)-specific CD4 T cells. It is known that cell surface MHC-II can internalize, exchange antigenic peptides in endosomes, and rapidly recycle back to the plasma membrane; however, the molecular machinery and trafficking pathways utilized by internalizing/recycling MHC-II have not been identified. We now demonstrate that unlike newly synthesized invariant chain-associated MHC-II, mature cell surface pMHC-II complexes internalize following clathrin-, AP-2-, and dynamin-independent endocytosis pathways. Immunofluorescence microscopy of MHC-II expressing HeLa-CIITA cells, human B cells, and human DCs revealed that pMHC enters Arf6(+)Rab35(+)EHD1(+) tubular endosomes following endocytosis. These data contrast the internalization pathways followed by newly synthesized and peptide-loaded MHC-II molecules and demonstrates that cell surface pMHC-II internalize and rapidly recycle from early endocytic compartments in tubular endosomes.
MeSH term(s)	ADP-Ribosylation Factors/metabolism ; Adaptor Protein Complex 2/genetics ; Adaptor Protein Complex 2/metabolism ; Antigen Presentation/immunology ; Clathrin/genetics ; Clathrin/metabolism ; Dynamins/metabolism ; Endocytosis ; HeLa Cells ; Histocompatibility Antigens Class II/chemistry ; Histocompatibility Antigens Class II/immunology ; Histocompatibility Antigens Class II/metabolism ; Humans ; Kinetics ; Peptides/chemistry ; rab GTP-Binding Proteins/metabolism
Chemical Substances	Adaptor Protein Complex 2 ; Clathrin ; Histocompatibility Antigens Class II ; Peptides ; RAB35 protein, human (EC 3.6.1.-) ; ADP-Ribosylation Factors (EC 3.6.5.2) ; ADP-ribosylation factor 6 (EC 3.6.5.2) ; rab GTP-Binding Proteins (EC 3.6.5.2) ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2008-03-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M801070200
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Article: Major Histocompatibility Complex Class II-Peptide Complexes Internalize Using a Clathrin- and Dynamin-independent Endocytosis Pathway

Walseng, Even / Bakke, Oddmund / Roche, Paul A

Journal of biological chemistry. 2008 May 23, v. 283, no. 21

2008

Abstract	Major histocompatibility complex (MHC) class II molecules (MHC-II) function by binding antigenic peptides and displaying these peptides on the surface of antigen presenting cells (APCs) for recognition by peptide-MHC-II (pMHC-II)-specific CD4 T cells. It is known that cell surface MHC-II can internalize, exchange antigenic peptides in endosomes, and rapidly recycle back to the plasma membrane; however, the molecular machinery and trafficking pathways utilized by internalizing/recycling MHC-II have not been identified. We now demonstrate that unlike newly synthesized invariant chain-associated MHC-II, mature cell surface pMHC-II complexes internalize following clathrin-, AP-2-, and dynamin-independent endocytosis pathways. Immunofluorescence microscopy of MHC-II expressing HeLa-CIITA cells, human B cells, and human DCs revealed that pMHC enters Arf6⁺Rab35⁺EHD1⁺ tubular endosomes following endocytosis. These data contrast the internalization pathways followed by newly synthesized and peptide-loaded MHC-II molecules and demonstrates that cell surface pMHC-II internalize and rapidly recycle from early endocytic compartments in tubular endosomes.
Language	English
Dates of publication	2008-0523
Size	p. 14717-14727.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
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