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A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells

Publikation: Bidrag til tidsskriftTidsskriftartikel

Standard

A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells. / Buus, S; Werdelin, O.

I: Journal of Immunology, Bind 136, Nr. 2, 1986, s. 452-8.

Publikation: Bidrag til tidsskriftTidsskriftartikel

Harvard

Buus, S & Werdelin, O 1986, 'A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells', Journal of Immunology, bind 136, nr. 2, s. 452-8.

APA

Buus, S., & Werdelin, O. (1986). A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells. Journal of Immunology, 136(2), 452-8.

Vancouver

Buus S, Werdelin O. A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells. Journal of Immunology. 1986;136(2):452-8.

Author

Buus, S ; Werdelin, O. / A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells. I: Journal of Immunology. 1986 ; Bind 136, Nr. 2. s. 452-8.

Bibtex

@article{cac23b20ebce11ddbf70000ea68e967b,
title = "A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells",
abstract = "A limited intralysosomal proteolytic degradation is probably a key event in the accessory cell processing of large protein antigens before their presentation to T cells. With the aid of highly specific inhibitors of proteinases, we have examined the role of proteolysis in the presentation of antigens by guinea pig accessory cells. The proteinase inhibitor benzyloxycarbonyl-phenylalanylalanine-diazomethyl-ketone, which selectively inhibits cysteine proteinases, was used to block this set of enzymes in cultured cells. We demonstrate that the selective inhibition of the cysteine proteinases of antigen-presenting cells causes a profound inhibition of both the proteolytic degradation and the presentation of the synthetic antigen dinitrophenyl-poly-L-lysine. In contrast, the presentation of another synthetic antigen, the copolymer of L-glutamic acid and L-alanine, was enhanced by the same inhibitor. Another inhibitor, pepstatin A, which selectively blocks aspartic proteinases, did not block the presentation of dinitrophenyl-poly-L-lysine. The results identify cysteine proteinases, probably lysosomal, as one of the groups of enzymes involved in antigen processing.",
author = "S Buus and O Werdelin",
note = "Keywords: Animals; Antigen-Presenting Cells; Binding, Competitive; Cysteine Proteinase Inhibitors; Dinitrophenols; Dose-Response Relationship, Immunologic; Guinea Pigs; Immunosuppressive Agents; Lysine; Lysosomes; Pepstatins; Peptides; Peritoneal Cavity; Polylysine; Proteins; T-Lymphocytes; Tuberculin",
year = "1986",
language = "English",
volume = "136",
pages = "452--8",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "2",

}

RIS

TY - JOUR

T1 - A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells

AU - Buus, S

AU - Werdelin, O

N1 - Keywords: Animals; Antigen-Presenting Cells; Binding, Competitive; Cysteine Proteinase Inhibitors; Dinitrophenols; Dose-Response Relationship, Immunologic; Guinea Pigs; Immunosuppressive Agents; Lysine; Lysosomes; Pepstatins; Peptides; Peritoneal Cavity; Polylysine; Proteins; T-Lymphocytes; Tuberculin

PY - 1986

Y1 - 1986

N2 - A limited intralysosomal proteolytic degradation is probably a key event in the accessory cell processing of large protein antigens before their presentation to T cells. With the aid of highly specific inhibitors of proteinases, we have examined the role of proteolysis in the presentation of antigens by guinea pig accessory cells. The proteinase inhibitor benzyloxycarbonyl-phenylalanylalanine-diazomethyl-ketone, which selectively inhibits cysteine proteinases, was used to block this set of enzymes in cultured cells. We demonstrate that the selective inhibition of the cysteine proteinases of antigen-presenting cells causes a profound inhibition of both the proteolytic degradation and the presentation of the synthetic antigen dinitrophenyl-poly-L-lysine. In contrast, the presentation of another synthetic antigen, the copolymer of L-glutamic acid and L-alanine, was enhanced by the same inhibitor. Another inhibitor, pepstatin A, which selectively blocks aspartic proteinases, did not block the presentation of dinitrophenyl-poly-L-lysine. The results identify cysteine proteinases, probably lysosomal, as one of the groups of enzymes involved in antigen processing.

AB - A limited intralysosomal proteolytic degradation is probably a key event in the accessory cell processing of large protein antigens before their presentation to T cells. With the aid of highly specific inhibitors of proteinases, we have examined the role of proteolysis in the presentation of antigens by guinea pig accessory cells. The proteinase inhibitor benzyloxycarbonyl-phenylalanylalanine-diazomethyl-ketone, which selectively inhibits cysteine proteinases, was used to block this set of enzymes in cultured cells. We demonstrate that the selective inhibition of the cysteine proteinases of antigen-presenting cells causes a profound inhibition of both the proteolytic degradation and the presentation of the synthetic antigen dinitrophenyl-poly-L-lysine. In contrast, the presentation of another synthetic antigen, the copolymer of L-glutamic acid and L-alanine, was enhanced by the same inhibitor. Another inhibitor, pepstatin A, which selectively blocks aspartic proteinases, did not block the presentation of dinitrophenyl-poly-L-lysine. The results identify cysteine proteinases, probably lysosomal, as one of the groups of enzymes involved in antigen processing.

M3 - Journal article

C2 - 3079785

VL - 136

SP - 452

EP - 458

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 2

ER -

ID: 9948332