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Article: Peptide generation in the major histocompatibility complex class I antigen processing and presentation pathway.

Androlewicz, M J

2000 Volume 8, Issue 1, Page(s) 12–16

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, ... ...

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.
MeSH term(s)	Animals ; Antigen Presentation ; Cysteine Endopeptidases/immunology ; Histocompatibility Antigens Class I/immunology ; Humans ; Multienzyme Complexes/immunology ; Peptides/immunology ; Proteasome Endopeptidase Complex ; Signal Transduction/immunology
Chemical Substances	Histocompatibility Antigens Class I ; Multienzyme Complexes ; Peptides ; Cysteine Endopeptidases (EC 3.4.22.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2000-07-07
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	1153887-9
ISSN	1531-7048 ; 1065-6251
ISSN (online)	1531-7048
ISSN	1065-6251
DOI	10.1097/00062752-200101000-00003
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Article: The role of tapasin in MHC class I antigen assembly.

Androlewicz, M J

Immunologic research

1999 Volume 20, Issue 2, Page(s) 79–88

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, ...

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.
MeSH term(s)	ATP Binding Cassette Transporter, Subfamily B, Member 2 ; ATP-Binding Cassette Transporters/metabolism ; Antigen Presentation ; Antiporters/physiology ; Calcium-Binding Proteins/metabolism ; Calreticulin ; Endoplasmic Reticulum/metabolism ; Heat-Shock Proteins/metabolism ; Histocompatibility Antigens Class I/metabolism ; Humans ; Immunoglobulins/physiology ; Isomerases/metabolism ; Membrane Transport Proteins ; Peptides/metabolism ; Protein Disulfide-Isomerases ; Ribonucleoproteins/metabolism
Chemical Substances	ATP Binding Cassette Transporter, Subfamily B, Member 2 ; ATP-Binding Cassette Transporters ; Antiporters ; Calcium-Binding Proteins ; Calreticulin ; Heat-Shock Proteins ; Histocompatibility Antigens Class I ; Immunoglobulins ; Membrane Transport Proteins ; Peptides ; Ribonucleoproteins ; TAP1 protein, human ; tapasin ; Isomerases (EC 5.-) ; Protein Disulfide-Isomerases (EC 5.3.4.1) ; PDIA3 protein, human (EC 5.3.4.1.)
Language	English
Publishing date	1999
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	632857-x
ISSN	1559-0755 ; 0257-277X
ISSN (online)	1559-0755
ISSN	0257-277X
DOI	10.1007/BF02786464
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Zs.A 1755: Show issues

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Article: An N-glycosylated tyrosinase epitope associates with newly synthesized MHC class I molecules in melanoma cells.

Androlewicz, M J

Human immunology

1996 Volume 51, Issue 2, Page(s) 81–88

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 ...

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.
MeSH term(s)	Biological Transport/immunology ; CD8-Positive T-Lymphocytes/immunology ; Epitopes/analysis ; Epitopes/immunology ; Epitopes/metabolism ; Glycosylation ; HLA-A2 Antigen/genetics ; HLA-A2 Antigen/immunology ; HLA-A2 Antigen/metabolism ; Histocompatibility Antigens Class I/genetics ; Histocompatibility Antigens Class I/immunology ; Histocompatibility Antigens Class I/metabolism ; Humans ; Melanoma/enzymology ; Melanoma/immunology ; Monophenol Monooxygenase/analysis ; Monophenol Monooxygenase/immunology ; Monophenol Monooxygenase/metabolism ; Precipitin Tests ; Protein Binding/immunology ; Tumor Cells, Cultured
Chemical Substances	Epitopes ; HLA-A2 Antigen ; Histocompatibility Antigens Class I ; Monophenol Monooxygenase (EC 1.14.18.1)
Language	English
Publishing date	1996-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	801524-7
ISSN	1879-1166 ; 0198-8859
ISSN (online)	1879-1166
ISSN	0198-8859
DOI	10.1016/s0198-8859(96)00237-6
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Zs.A 1597: Show issues

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Article: Targeting of HIV-1 Nef to the centrosome: implications for antigen processing.

Lacaille, V G / Androlewicz, M J

Traffic (Copenhagen, Denmark)

2001 Volume 1, Issue 11, Page(s) 884–891

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 ... ...

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.
MeSH term(s)	Animals ; Antigen Presentation/drug effects ; Base Sequence ; COS Cells ; Centrosome/drug effects ; Centrosome/immunology ; Centrosome/metabolism ; DNA Primers/genetics ; Gene Products, nef/genetics ; Gene Products, nef/immunology ; Gene Products, nef/metabolism ; HIV-1/genetics ; HIV-1/immunology ; HIV-1/metabolism ; Humans ; Nocodazole/pharmacology ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; nef Gene Products, Human Immunodeficiency Virus
Chemical Substances	DNA Primers ; Gene Products, nef ; Recombinant Fusion Proteins ; nef Gene Products, Human Immunodeficiency Virus ; Nocodazole (SH1WY3R615)
Language	English
Publishing date	2001-01-31
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1034/j.1600-0854.2000.011107.x
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Zs.A 5634: Show issues

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Article: Photolabeling the transporter associated with antigen processing.

Lacaille, V G / Androlewicz, M J

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

2000 Volume 156, Page(s) 143–151

MeSH term(s)	ATP Binding Cassette Transporter, Subfamily B, Member 2 ; ATP Binding Cassette Transporter, Subfamily B, Member 3 ; ATP-Binding Cassette Transporters/analysis ; ATP-Binding Cassette Transporters/metabolism ; Affinity Labels ; Antigen Presentation ; Azides ; B-Lymphocytes ; Cell Line ; Chromatography, High Pressure Liquid/methods ; Cross-Linking Reagents ; Dimerization ; Electrophoresis, Polyacrylamide Gel/methods ; Humans ; Major Histocompatibility Complex ; Protein Subunits
Chemical Substances	ATP Binding Cassette Transporter, Subfamily B, Member 2 ; ATP Binding Cassette Transporter, Subfamily B, Member 3 ; ATP-Binding Cassette Transporters ; Affinity Labels ; Azides ; Cross-Linking Reagents ; Protein Subunits ; TAP1 protein, human ; TAP2 protein, human (145892-13-3) ; hydroxysuccinimidyl-4-azidobenzoate (53053-08-0)
Language	English
Publishing date	2000-11-01
Publishing country	United States
Document type	Journal Article
ISSN	1064-3745
ISSN	1064-3745
DOI	10.1385/1-59259-062-4:143
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Article: Heat shock protein 70 moderately enhances peptide binding and transport by the transporter associated with antigen processing.

Chen, D / Androlewicz, M J

Immunology letters

2000 Volume 75, Issue 2, Page(s) 143–148

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 ... ...

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.
MeSH term(s)	ATP Binding Cassette Transporter, Subfamily B, Member 2 ; ATP-Binding Cassette Transporters/immunology ; ATP-Binding Cassette Transporters/metabolism ; Amino Acid Sequence ; Animals ; Antigen Presentation ; Biological Transport, Active/drug effects ; Cell Line ; HSP70 Heat-Shock Proteins/isolation & purification ; HSP70 Heat-Shock Proteins/metabolism ; HSP70 Heat-Shock Proteins/pharmacology ; Humans ; Male ; Mice ; Mice, Inbred BALB C ; Oligopeptides/chemistry ; Oligopeptides/metabolism ; Protein Binding/drug effects
Chemical Substances	ATP Binding Cassette Transporter, Subfamily B, Member 2 ; ATP-Binding Cassette Transporters ; HSP70 Heat-Shock Proteins ; Oligopeptides ; TAP1 protein, human ; Tap1 protein, mouse
Language	English
Publishing date	2000-12-14
Publishing country	Netherlands
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	445150-8
ISSN	1879-0542 ; 0165-2478
ISSN (online)	1879-0542
ISSN	0165-2478
DOI	10.1016/s0165-2478(00)00294-7
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Article: Oligosaccharide trimming plays a role in the endoplasmic reticulum-associated degradation of tyrosinase.

Wang, Y / Androlewicz, M J

Biochemical and biophysical research communications

2000 Volume 271, Issue 1, Page(s) 22–27

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 ... ...

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.
MeSH term(s)	1-Deoxynojirimycin/pharmacology ; Acetylcysteine/analogs & derivatives ; Acetylcysteine/pharmacology ; Alkaloids/pharmacology ; Animals ; Antigens/metabolism ; COS Cells ; Calcium-Binding Proteins/metabolism ; Calnexin ; Cysteine Proteinase Inhibitors/pharmacology ; Endoplasmic Reticulum/enzymology ; Endoplasmic Reticulum/metabolism ; Enzyme Inhibitors/pharmacology ; Glucosidases/antagonists & inhibitors ; Humans ; Indolizines/pharmacology ; Mannosidases/antagonists & inhibitors ; Models, Biological ; Monophenol Monooxygenase/metabolism ; Precipitin Tests ; Time Factors
Chemical Substances	Alkaloids ; Antigens ; Calcium-Binding Proteins ; Cysteine Proteinase Inhibitors ; Enzyme Inhibitors ; Indolizines ; kifunensine (0NI8960271) ; lactacystin (133343-34-7) ; Calnexin (139873-08-8) ; 1-Deoxynojirimycin (19130-96-2) ; Monophenol Monooxygenase (EC 1.14.18.1) ; Glucosidases (EC 3.2.1.-) ; Mannosidases (EC 3.2.1.-) ; castanospermine (Q0I3184XM7) ; Acetylcysteine (WYQ7N0BPYC)
Language	English
Publishing date	2000-04-29
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1006/bbrc.2000.2577
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Zs.A 116: Show issues

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Article: Antigenic peptide transporter.

Lacaille, V G / Androlewicz, M J

Pharmaceutical biotechnology

1999 Volume 12, Page(s) 289–312

MeSH term(s)	ATP-Binding Cassette Transporters/antagonists & inhibitors ; ATP-Binding Cassette Transporters/metabolism ; Antigen Presentation ; Biological Transport ; Drug Design ; Histocompatibility Antigens Class I/metabolism ; Immediate-Early Proteins/metabolism ; Molecular Mimicry ; Peptides/metabolism ; Viral Envelope Proteins/metabolism ; Viral Proteins
Chemical Substances	ATP-Binding Cassette Transporters ; Histocompatibility Antigens Class I ; ICP47 protein, Herpes simplex virus ; Immediate-Early Proteins ; Peptides ; Viral Envelope Proteins ; Viral Proteins ; glycoprotein D, Human herpesvirus 1
Language	English
Publishing date	1999
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1078-0467
ISSN	1078-0467
DOI	10.1007/0-306-46812-3_11
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Article: Herpes simplex virus inhibitor ICP47 destabilizes the transporter associated with antigen processing (TAP) heterodimer.

Lacaille, V G / Androlewicz, M J

The Journal of biological chemistry

1998 Volume 273, Issue 28, Page(s) 17386–17390

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 ... ...

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.
MeSH term(s)	ATP-Binding Cassette Transporters/antagonists & inhibitors ; Amino Acid Sequence ; Animals ; Cell Line ; Dimerization ; Immediate-Early Proteins/metabolism ; Iodine Radioisotopes ; Spodoptera ; Viral Proteins
Chemical Substances	ATP-Binding Cassette Transporters ; ICP47 protein, Herpes simplex virus ; Immediate-Early Proteins ; Iodine Radioisotopes ; Viral Proteins
Language	English
Publishing date	1998-07-10
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.273.28.17386
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Article: Reconstitution of peptide-binding activity by TAP in proteoliposomes.

Stephens, D B / Androlewicz, M J

FEBS letters

1997 Volume 416, Issue 3, Page(s) 353–358

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 ...

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.
MeSH term(s)	ATP-Binding Cassette Transporters/chemistry ; ATP-Binding Cassette Transporters/metabolism ; Amino Acid Sequence ; Binding Sites ; Burkitt Lymphoma ; Cell Membrane/metabolism ; Humans ; Liposomes ; Oligopeptides/chemistry ; Phospholipids/chemistry ; Proteolipids/chemistry ; Proteolipids/metabolism ; Structure-Activity Relationship ; Tumor Cells, Cultured
Chemical Substances	ATP-Binding Cassette Transporters ; Liposomes ; Oligopeptides ; Phospholipids ; Proteolipids ; proteoliposomes
Language	English
Publishing date	1997-10-27
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/s0014-5793(97)01221-0
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