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1.
Immunol Lett ; 75(2): 143-8, 2001 Jan 01.
Article in English | MEDLINE | ID: mdl-11137139

ABSTRACT

Hsp70 molecules are capable of binding antigenic peptides and eliciting CTL responses to the bound peptide. However, the precise mechanism for the induction of CTL has not been determined. One possibility is that hsp molecules can directly shuttle peptides in the MHC class I antigen processing and presentation pathway, as previously postulated. Here, we have addressed this issue by testing the effect of purified hsp70 molecules on peptide binding and transport by the transporter associated with antigen processing (TAP). Our results indicate that purified hsp70 molecules moderately enhance TAP function. In addition, we detect a physical association between hsp70 molecules and TAP, as well as the homologous drug transporter P-glycoprotein. We conclude that while hsp70 molecules may not be directly involved in the delivery of peptide to TAP, they may play an important role in TAP transport by binding to TAP and promoting its function.


Subject(s)
ATP-Binding Cassette Transporters/immunology , ATP-Binding Cassette Transporters/metabolism , Antigen Presentation , HSP70 Heat-Shock Proteins/pharmacology , ATP Binding Cassette Transporter, Subfamily B, Member 2 , Amino Acid Sequence , Animals , Biological Transport, Active/drug effects , Cell Line , HSP70 Heat-Shock Proteins/isolation & purification , HSP70 Heat-Shock Proteins/metabolism , Humans , Male , Mice , Mice, Inbred BALB C , Oligopeptides/chemistry , Oligopeptides/metabolism , Protein Binding/drug effects
2.
Curr Opin Hematol ; 8(1): 12-6, 2001 Jan.
Article in English | MEDLINE | ID: mdl-11138620

ABSTRACT

The bulk of antigens that are presented by major histocompatibility complex (MHC) class I molecules are processed in the cytosol. Therefore, the cellular protein degradation machinery is thought to play a major role in antigen processing. For example, there is clear evidence that the ubiquitin-proteasome pathway, the major proteolytic pathway in the cytosol, plays a role in the processing of class I-associated antigens. In addition, peptide chaperones must exist to properly target peptides to the transporter associated with antigen processing. Here, the author reviews some of the more important advances over the past year that further define the pathways of antigen breakdown in the cytosol. This includes a look at the distinctive roles of proteasomes versus immunoproteasomes, the isolation of peptide processing intermediates in the cytosol, and the role of defective ribosomal products. These findings highlight the importance of understanding basic cellular protein degradation pathways in antigen processing.


Subject(s)
Histocompatibility Antigens Class I/immunology , Peptides/immunology , Signal Transduction/immunology , Animals , Antigen Presentation , Cysteine Endopeptidases/immunology , Humans , Multienzyme Complexes/immunology , Proteasome Endopeptidase Complex
4.
Biochem Biophys Res Commun ; 271(1): 22-7, 2000 Apr 29.
Article in English | MEDLINE | ID: mdl-10777675

ABSTRACT

The effect of glucosidase and mannosidase inhibitors on the ER-associated degradation of tyrosinase was assessed in transiently transfected COS-7 cells. We found that the glucosidase inhibitors castanospermine and deoxynojirimycin had very little effect on tyrosinase degradation, whereas the mannosidase inhibitors deoxymannojirimycin and kifunensine significantly delayed the rate of tyrosinase degradation as measured by pulse-chase analysis. In addition, we show that tyrosinase degradation is sensitive to the proteasome inhibitor lactacystin and that tyrosinase associates with endogenous calnexin in COS-7 cells. Our data support a model of tyrosinase degradation that involves mannose trimming, calnexin association, and the retrograde transport of tyrosinase from the ER to the cytosol for proteasomal degradation. The pathways of tyrosinase degradation have important ramifications with regard to the exact types of antigenic epitopes that are presented to the immune system.


Subject(s)
Endoplasmic Reticulum/enzymology , Endoplasmic Reticulum/metabolism , Monophenol Monooxygenase/metabolism , 1-Deoxynojirimycin/pharmacology , Acetylcysteine/analogs & derivatives , Acetylcysteine/pharmacology , Alkaloids/pharmacology , Animals , Antigens/metabolism , COS Cells , Calcium-Binding Proteins/metabolism , Calnexin , Cysteine Proteinase Inhibitors/pharmacology , Enzyme Inhibitors/pharmacology , Glucosidases/antagonists & inhibitors , Humans , Indolizines/pharmacology , Mannosidases/antagonists & inhibitors , Models, Biological , Precipitin Tests , Time Factors
5.
Traffic ; 1(11): 884-91, 2000 Nov.
Article in English | MEDLINE | ID: mdl-11208077

ABSTRACT

To gain a better understanding of the intracellular sites of antigen processing we have looked at the localization of human immunodeficiency virus (HIV)-1 Nef protein by confocal microscopic and biochemical means. We found that ubiquitin (Ub)-Nef fusion proteins were localized to the centrosome in transfected COS-7 cells, and that the colocalization was inhibited by the microtubule-disrupting agent, nocodazole. Interestingly, we found that Ub-Nef trafficking to the centrosome was not dependent upon the metabolic stability of Ub-Nef nor on the inhibition of proteasome activity. We also analyzed the MHC class I antigen processing of a reporter epitope linked to the Ub-Nef fusion proteins and found that Ub-Nef was processed in COS-7 cells. In addition, we show that this processing was inhibited by nocodazole. We suggest that the centrosome may serve as a site of antigen processing in vivo.


Subject(s)
Centrosome/metabolism , Gene Products, nef/metabolism , HIV-1/metabolism , Animals , Antigen Presentation/drug effects , Base Sequence , COS Cells , Centrosome/drug effects , Centrosome/immunology , DNA Primers/genetics , Gene Products, nef/genetics , Gene Products, nef/immunology , HIV-1/genetics , HIV-1/immunology , Humans , Nocodazole/pharmacology , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , nef Gene Products, Human Immunodeficiency Virus
6.
Immunol Res ; 20(2): 79-88, 1999.
Article in English | MEDLINE | ID: mdl-10580633

ABSTRACT

The discovery of tapasin has shed new light on the mechanisms of major histocompatibility complex (MHC) class I assembly in the endoplasmic reticulum (ER). Tapasin appears to play an important role in the stable assembly of class I molecules with peptide, however, the precise function of tapasin remains elusive. The pursuit of tapasin function is complicated by the observation that tapasin is not required for successful antigen presentation by all class I molecules. In addition, current data suggest that the putative role of tapasin as a bridging molecule between transporter associated with antigen presentation (TAP) and class I is only of minor importance in tapasin action, and tapasin' s major role appears to be as an active cofactor in the assembly of class I. Furthermore, it is clear that class I molecules can follow multiple pathways for successful assembly in the ER. These pathways may or may not include the interaction of class I molecules with the accessory proteins tapasin, calreticulin, ERp57, or TAP. I would like to suggest that the particular pathway utilized by a given class I molecule depends more upon the availability of appropriate peptides rather than on an intrinsic property of the class I molecule, and that tapasin may serve a peptide editing function.


Subject(s)
Antiporters/physiology , Histocompatibility Antigens Class I/metabolism , Immunoglobulins/physiology , ATP Binding Cassette Transporter, Subfamily B, Member 2 , ATP-Binding Cassette Transporters/metabolism , Antigen Presentation , Calcium-Binding Proteins/metabolism , Calreticulin , Endoplasmic Reticulum/metabolism , Heat-Shock Proteins/metabolism , Humans , Isomerases/metabolism , Membrane Transport Proteins , Peptides/metabolism , Protein Disulfide-Isomerases , Ribonucleoproteins/metabolism
7.
Immunol Rev ; 172: 67-72, 1999 Dec.
Article in English | MEDLINE | ID: mdl-10631937

ABSTRACT

The processing and presentation of secretory glycoprotein antigens by the MHC class I processing pathway presents an interesting topological problem. That is, how do the luminal glycoprotein antigens gain access to the class I processing machinery located in the cell cytosol? Current data indicate that the retrograde transport of glycoproteins from the endoplasmic reticulum (ER) to cytosol represents the major pathway for ER-associated protein degradation, and most likely represents a major pathway for the processing of glycoprotein antigens by MHC class I molecules as well. There is now a growing list of viral and tumor glycoprotein antigens that undergo retrograde transport from the ER to the cytosol and processing by the ubiquitin-proteasome pathway of degradation. We review here some general aspects of this "ER degradation" pathway, and how it relates to the processing and presentation of class I-associated viral and tumor antigens. In particular, we analyze the role of oligosaccharide trimming and ER molecular chaperones in this process. We would like to emphasize that the class I processing machinery has adapted a common cellular pathway for its use, and that this could lead to the identification of unique characteristics with regard to ER degradation and antigen processing.


Subject(s)
Antigen Presentation , Endoplasmic Reticulum/immunology , Endoplasmic Reticulum/metabolism , Glycoproteins/immunology , Glycoproteins/metabolism , Histocompatibility Antigens Class I/metabolism , Animals , Antigens, Neoplasm/metabolism , Antigens, Viral/metabolism , Biological Transport, Active , Cysteine Endopeptidases/metabolism , Cytosol/immunology , Cytosol/metabolism , Glycoproteins/chemistry , Humans , Multienzyme Complexes/metabolism , Oligosaccharides/chemistry , Proteasome Endopeptidase Complex
9.
Melanoma Res ; 8(4): 345-53, 1998 Aug.
Article in English | MEDLINE | ID: mdl-9764810

ABSTRACT

Many melanoma epitopes are presented to cytotoxic T-lymphocytes (CTLs) by major histocompatibility complex (MHC) class I molecules, and it is reasonable to expect that the epitopes would be good substrates for the transporter associated with antigen processing (TAP), as TAP plays a major role in the transport of peptides into the endoplasmic reticulum (ER) for binding to MHC class I molecules. However, we have previously shown that several melanoma-associated epitopes, such as those derived from tyrosinase, gp100, MAGE-1 and MAGE-2 antigens, are in fact poor substrates for TAP. During the process of determining why these epitopes were capable of eliciting a strong CTL response, yet were poor substrates for TAP, it was observed that the epitopes possessed amino acids at their N-terminus that were deleterious for TAP binding as described for the peptide-binding motif for human TAP. We therefore postulated that the epitopes were transported by TAP as longer precursor molecules, and then trimmed in the ER to the appropriate size for presentation to T-cells. In an effort to test this hypothesis we synthesized a set of peptides, derived from the tyrosinase (YMNGTMSQV) and MAGE-1 (EADPTGHSY) epitopes, which possess N-terminal extensions of up to four amino acids. We show here that the longer peptides are indeed transported into the ER at a significantly higher level than the original epitopes. The data indicate that the longer melanoma-associated peptides are the preferred substrates for TAP, and further support the notion that peptides can be trimmed at the N-terminus in the ER during antigen processing.


Subject(s)
ATP-Binding Cassette Transporters/metabolism , Antigen Presentation , Antigens, Neoplasm/metabolism , Endoplasmic Reticulum/metabolism , Epitopes/metabolism , Peptide Fragments/metabolism , ATP Binding Cassette Transporter, Subfamily B, Member 2 , ATP Binding Cassette Transporter, Subfamily B, Member 3 , Antigens, Neoplasm/chemistry , Antigens, Neoplasm/immunology , Biological Transport , Burkitt Lymphoma/pathology , Epitopes/chemistry , Humans , Melanoma-Specific Antigens , Microsomes/metabolism , Molecular Weight , Monophenol Monooxygenase/chemistry , Monophenol Monooxygenase/immunology , Monophenol Monooxygenase/metabolism , Neoplasm Proteins/chemistry , Neoplasm Proteins/immunology , Neoplasm Proteins/metabolism , Peptide Fragments/chemistry , Peptide Fragments/immunology , Substrate Specificity , Tumor Cells, Cultured
11.
J Biol Chem ; 273(28): 17386-90, 1998 Jul 10.
Article in English | MEDLINE | ID: mdl-9651323

ABSTRACT

Chemical cross-linking of the transporter associated with antigen processing (TAP) heterodimer was used to determine whether the herpes simplex virus inhibitor of TAP, ICP47, induces a conformational change in TAP. Cross-linking of TAP in cellular membranes produced a major species of approximately 220 kDa which was comprised solely of TAP.1 and TAP.2 and most likely represents the TAP heterodimer. Interestingly, prior treatment of TAP-containing membranes with TAP peptide substrates stimulated the formation of the cross-linked TAP heterodimer, whereas pretreatment of membranes with ICP47 completely blocked the formation of the cross-linked heterodimer. These data suggest that suitable substrates for TAP stabilize the TAP heterodimer, whereas ICP47 destabilizes the heterodimer. The results indicate that subtle conformational changes occur in the TAP heterodimer upon the binding of peptides and the inhibitor ICP47 and that ICP47 has a deleterious effect on TAP heterodimer structure, in addition to its role as a potent blocker of substrate binding to TAP.


Subject(s)
ATP-Binding Cassette Transporters/antagonists & inhibitors , Immediate-Early Proteins/metabolism , Viral Proteins , Amino Acid Sequence , Animals , Cell Line , Dimerization , Iodine Radioisotopes , Spodoptera
12.
FEBS Lett ; 416(3): 353-8, 1997 Oct 27.
Article in English | MEDLINE | ID: mdl-9373184

ABSTRACT

The purification and functional reconstitution of the transporter associated with antigen processing (TAP) is crucial for a complete molecular understanding of its action. Here, we report the conditions for the successful solubilization of human TAP from cellular membranes while maintaining TAP peptide-binding activity. In addition, solubilized TAP was incorporated into proteoliposomes and shown to possess specific peptide-binding activity. These studies provide the foundation for future attempts to achieve the complete functional reconstitution of TAP, which includes peptide transport.


Subject(s)
ATP-Binding Cassette Transporters/chemistry , ATP-Binding Cassette Transporters/metabolism , Oligopeptides/chemistry , Proteolipids/metabolism , Amino Acid Sequence , Binding Sites , Burkitt Lymphoma , Cell Membrane/metabolism , Humans , Liposomes , Phospholipids/chemistry , Proteolipids/chemistry , Structure-Activity Relationship , Tumor Cells, Cultured
13.
Br J Haematol ; 98(2): 426-32, 1997 Aug.
Article in English | MEDLINE | ID: mdl-9266943

ABSTRACT

Immunotherapy involving cytotoxic T lymphocytes (CTLs) is an attractive alternative for treatment of various malignancies, including multiple myeloma. For tumour cells to be recognized and killed by CTLs they must express cell surface major histocompatibility complex (MHC) class I molecules and the transporter associated with antigen processing (TAP). However, loss of MHC class I and the TAP protein are common among several types of solid tumours. This study assessed the expression of TAP protein (by intracellular flow cytometry) and cell surface MHC class I molecules in three human myeloma cell lines as well as the plasma cell population (CD38+ bright) in bone marrow specimens from 13 multiple myeloma patients. In all of the patients, 100% of the plasma cell population expressed both the TAP subunits and cell surface MHC class I molecules, but at varying intensities. Both TAP and MHC class I were also expressed in the three myeloma lines. Additionally, the function of the antigen transport machinery was evaluated by a peptide transporter assay in the three myeloma lines. TAP transporter activity was readily detectable in two out of three myeloma lines, whereas the diminished activity in the third cell line was completely restored by co-culturing with recombinant interferon-gamma (rIFN-gamma).


Subject(s)
ATP-Binding Cassette Transporters/metabolism , Extracellular Matrix Proteins/metabolism , Histocompatibility Antigens Class I/metabolism , Multiple Myeloma/immunology , Nerve Tissue Proteins/metabolism , ATP Binding Cassette Transporter, Subfamily B, Member 2 , ATP Binding Cassette Transporter, Subfamily B, Member 3 , Aged , Female , Flow Cytometry , Humans , Male , Middle Aged , Plasma Cells/immunology , Tumor Cells, Cultured
14.
Hum Immunol ; 51(2): 81-8, 1996 Dec.
Article in English | MEDLINE | ID: mdl-8960909

ABSTRACT

Endogenous antigenic epitopes are presented to CD8+ T cells by MHC class I molecules. Many endogenous antigens are glycoproteins, and it is not clear what effect the attachment of carbohydrate to potential immunogenic epitopes has on their processing and presentation (i.e., is the carbohydrate moiety removed prior to presentation, or is it presented along with the peptide to T cells?). A major question in this regard is whether natural antigenic epitopes that possess N-linked carbohydrate can associate with class I molecules during assembly in the endoplasmic reticulum (ER). One such antigenic epitope, corresponding to amino acids 369-377 of the enzyme tyrosinase, possesses an N-linked glycosylation site. We have studied the transport and loading of this epitope in streptolysin O-permeabilized melanoma cells. We show here that that the glycosylated epitope is capable of loading onto newly synthesized HLA-A2 molecules in the ER of two melanoma cell lines. The results are discussed in respect to the processing and presentation of the tyrosinase epitope.


Subject(s)
Epitopes/analysis , Epitopes/metabolism , Histocompatibility Antigens Class I/genetics , Histocompatibility Antigens Class I/metabolism , Melanoma/enzymology , Melanoma/immunology , Monophenol Monooxygenase/analysis , Monophenol Monooxygenase/metabolism , Biological Transport/immunology , CD8-Positive T-Lymphocytes/immunology , Epitopes/immunology , Glycosylation , HLA-A2 Antigen/genetics , HLA-A2 Antigen/immunology , HLA-A2 Antigen/metabolism , Histocompatibility Antigens Class I/immunology , Humans , Monophenol Monooxygenase/immunology , Precipitin Tests , Protein Binding/immunology , Tumor Cells, Cultured
15.
Mol Immunol ; 33(15): 1165-9, 1996 Oct.
Article in English | MEDLINE | ID: mdl-9070664

ABSTRACT

To gain insight into how tumor antigens are generated and presented, a panel of peptides corresponding to melanoma-specific T cell epitopes were tested for their transport capacity by the transporter associated with antigen processing (TAP). The melanoma epitopes exhibited differential capacities to be transported by TAP in streptolysin O-permeabilized cells, as well as differential competition for peptide binding to TAP. The data indicate that some melanoma-specific epitopes are good substrates for TAP, while others are poor substrates for TAP. One of the epitopes, derived from tyrosinase, was transported into the endoplasmic reticulum (ER), in spite of being a poor competitor for reporter peptide transport and for peptide binding. These results suggest that the melanoma antigens follow distinct pathways for presentation, along the MHC class I pathway.


Subject(s)
ATP-Binding Cassette Transporters/immunology , Antigens, Neoplasm/metabolism , Melanoma/immunology , ATP Binding Cassette Transporter, Subfamily B, Member 3 , Amino Acid Sequence , Antigen Presentation , Epitopes , Humans , Major Histocompatibility Complex/immunology , Peptides/chemistry , Protein Binding
17.
Science ; 270(5233): 105-8, 1995 Oct 06.
Article in English | MEDLINE | ID: mdl-7569935

ABSTRACT

Major histocompatibility complex (MHC) class I molecules bind peptides that are delivered from the cytosol into the endoplasmic reticulum by the MHC-encoded transporter associated with antigen processing (TAP). Peptide capture by immature heterodimers of class I heavy chains and beta 2-microglobulin may be facilitated by their physical association with TAP. A genetic defect in a human mutant cell line causes the complete failure of diverse class I heterodimers to associate with TAP. This deficiency impairs the ability of the class I heterodimers to efficiently capture peptides and results from loss of function of an unidentified gene or genes linked to the MHC.


Subject(s)
ATP-Binding Cassette Transporters/metabolism , Histocompatibility Antigens Class I/metabolism , Major Histocompatibility Complex , Peptides/metabolism , ATP Binding Cassette Transporter, Subfamily B, Member 2 , ATP Binding Cassette Transporter, Subfamily B, Member 3 , Amino Acid Sequence , Calcium-Binding Proteins/metabolism , Calnexin , Cell Line , Endoplasmic Reticulum/metabolism , HLA Antigens/metabolism , HLA-A1 Antigen/metabolism , HLA-B Antigens/metabolism , HLA-B8 Antigen/metabolism , HLA-G Antigens , Humans , Ligands , Major Histocompatibility Complex/genetics , Molecular Sequence Data , Mutation , Transfection , beta 2-Microglobulin/metabolism
18.
Immunity ; 3(1): 65-77, 1995 Jul.
Article in English | MEDLINE | ID: mdl-7542549

ABSTRACT

We previously identified an HLA-B8+ donor, NW, whose lymphoblastoid cells failed to present a B8-restricted epitope from the influenza A nucleoprotein following viral infection, although added peptide could still be presented. The failure to present through HLA-B8 following viral infection appears to be specific for the NP epitope. Here, we report that donor NW makes an HLA-B2702-restricted influenza-specific CTL response to an epitope in the nucleoprotein that overlaps the B8-restricted epitope by 8 aa. Two mechanisms for the failure of this cell line to present the B8-restricted epitope following viral infection are investigated. One is that there is an antigen processing polymorphism specific to the NW cell line, so that there is either preferential generation or preferential transport of the B2702 epitope. The other is that B8 and B2702 compete for a common peptide fragment in the ER and this leads to suboptimal loading of HLA-B8.


Subject(s)
Antigens, Viral/immunology , Histocompatibility Antigens Class I/immunology , Alleles , Antigen Presentation , Clone Cells , Epitopes/immunology , HLA-B8 Antigen/immunology , Histocompatibility Antigens Class I/genetics , Humans , T-Lymphocytes, Cytotoxic/cytology , T-Lymphocytes, Cytotoxic/immunology
19.
Proc Natl Acad Sci U S A ; 91(26): 12716-20, 1994 Dec 20.
Article in English | MEDLINE | ID: mdl-7809108

ABSTRACT

The transporter proteins associated with antigen processing (TAP proteins) transport antigenic peptides across the endoplasmic reticulum membrane where they can assemble with newly synthesized major histocompatibility complex (MHC) class I/beta 2-microglobulin (beta 2m) dimers. We have shown previously that TAP possesses a peptide-recognition site with broad specificity and that MHC class I/beta 2m dimers physically associate with TAP. Here, we further characterize the nature of the peptide-binding site on TAP, and the site of interaction of TAP with MHC class I/beta 2m dimers. TAP photoaffinity labeling experiments revealed that both TAP1 and TAP2 are photolabeled by two distinct photopeptide analogues, suggesting that elements of both TAP1 and TAP2 compose the peptide-recognition site. TAP photolabeling analysis on transfectant cell lines that express TAP1 and TAP2 both individually and together revealed that efficient formation of the peptide-binding site occurs only when TAP1 and TAP2 are coexpressed, which correlates with the finding that peptide translocation via TAP occurs only in the presence of both TAP1 and TAP2. These data strongly support the notion that TAP functions as a heterodimer. MHC class I/beta 2m dimers were shown to associate with individual TAP1 chains but were not detectable with individual TAP2 chains. This result suggests that the site of interaction for MHC class I/beta 2m dimers with TAP is on TAP1.


Subject(s)
ATP-Binding Cassette Transporters/metabolism , Histocompatibility Antigens Class I/metabolism , beta 2-Microglobulin/metabolism , ATP Binding Cassette Transporter, Subfamily B, Member 2 , ATP Binding Cassette Transporter, Subfamily B, Member 3 , Amino Acid Sequence , Antigen-Presenting Cells/metabolism , Biological Transport , Endoplasmic Reticulum/metabolism , Glycosylation , In Vitro Techniques , Macromolecular Substances , Molecular Sequence Data , Peptides/chemistry , Peptides/metabolism , Photochemistry
20.
Nature ; 368(6474): 864-7, 1994 Apr 28.
Article in English | MEDLINE | ID: mdl-8159247

ABSTRACT

Major histocompatibility complex class I molecules bind antigenic peptides in the endoplasmic reticulum (ER) and transport them to the cell surface for recognition by cytotoxic T lymphocytes. The peptides are predominantly generated from cytoplasmic proteins, probably by the action of the multicatalytic proteinase complex, or proteasome. They are transported into the ER by the transporters associated with antigen processing (TAP), a complex formed from two subunits, TAP.1 and TAP.2 (refs 3-5). Here we show that the TAP molecules are intimately involved in the assembly of the class I/beta 2-microglobulin (beta 2m) peptide complex. Free class I heavy chains are associated in the ER with the chaperone calnexin. In human B-cell lines, however, class I/beta 2m dimers in the ER are physically associated with TAP molecules rather than calnexin. Our results suggest that calnexin mediates class I/beta 2m dimerization, and subsequent binding of the dimers to TAP molecules facilitates their association with TAP-transported peptides.


Subject(s)
ATP-Binding Cassette Transporters , Carrier Proteins/metabolism , Histocompatibility Antigens Class I/metabolism , beta 2-Microglobulin/metabolism , ATP Binding Cassette Transporter, Subfamily B, Member 2 , ATP Binding Cassette Transporter, Subfamily B, Member 3 , Amino Acid Sequence , Animals , B-Lymphocytes/metabolism , Biological Transport , Calcium-Binding Proteins/metabolism , Calnexin , Cell Line , Digitonin/pharmacology , Endoplasmic Reticulum/metabolism , HLA-A3 Antigen/metabolism , Humans , Mice , Molecular Sequence Data , Protein Binding , Rabbits , Solubility
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