A novel mechanism for protein delivery: granzyme B undergoes electrostatic exchange from serglycin to target cells
(2005) In Journal of Biological Chemistry 280(21). p.20752-20761- Abstract
- The molecular interaction of secreted granzyme B-serglycin complexes with target cells remains undefined. Targets exposed to double-labeled granzyme B-serglycin complexes show solely the uptake of granzyme B. An in vitro model demonstrates the exchange of the granzyme from serglycin to immobilized, sulfated glycosaminoglycans. Using a combination of cell binding and internalization assays, granzyme B was found to exchange to sulfated glycosaminoglycans and, depending on the cell type, to higher affinity sites. Apoptosis induced by purified granzyme B and cytotoxic T-cells was diminished in targets with reduced cell surface glycosaminoglycan content. A mechanism of delivery is proposed entailing electrostatic transfer of granzyme B from... (More)
- The molecular interaction of secreted granzyme B-serglycin complexes with target cells remains undefined. Targets exposed to double-labeled granzyme B-serglycin complexes show solely the uptake of granzyme B. An in vitro model demonstrates the exchange of the granzyme from serglycin to immobilized, sulfated glycosaminoglycans. Using a combination of cell binding and internalization assays, granzyme B was found to exchange to sulfated glycosaminoglycans and, depending on the cell type, to higher affinity sites. Apoptosis induced by purified granzyme B and cytotoxic T-cells was diminished in targets with reduced cell surface glycosaminoglycan content. A mechanism of delivery is proposed entailing electrostatic transfer of granzyme B from serglycin to cell surface proteins. (Less)
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https://lup.lub.lu.se/record/1132915
- author
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 280
- issue
- 21
- pages
- 20752 - 20761
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:15788411
- scopus:20144380101
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M501181200
- language
- English
- LU publication?
- no
- id
- 88255dee-9b11-4621-b413-2949d88ce21b (old id 1132915)
- date added to LUP
- 2016-04-01 11:56:21
- date last changed
- 2022-01-26 20:27:16
@article{88255dee-9b11-4621-b413-2949d88ce21b, abstract = {{The molecular interaction of secreted granzyme B-serglycin complexes with target cells remains undefined. Targets exposed to double-labeled granzyme B-serglycin complexes show solely the uptake of granzyme B. An in vitro model demonstrates the exchange of the granzyme from serglycin to immobilized, sulfated glycosaminoglycans. Using a combination of cell binding and internalization assays, granzyme B was found to exchange to sulfated glycosaminoglycans and, depending on the cell type, to higher affinity sites. Apoptosis induced by purified granzyme B and cytotoxic T-cells was diminished in targets with reduced cell surface glycosaminoglycan content. A mechanism of delivery is proposed entailing electrostatic transfer of granzyme B from serglycin to cell surface proteins.}}, author = {{Raja, Srikumar M and Metkar, Sunil S and Honing, Stefan and Wang, Baikun and Russin, William A and Pipalia, Nina H and Menaa, Cheikh and Belting, Mattias and Cao, Xuefang and Dressel, Ralf and Froelich, Christopher J}}, issn = {{1083-351X}}, language = {{eng}}, number = {{21}}, pages = {{20752--20761}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{A novel mechanism for protein delivery: granzyme B undergoes electrostatic exchange from serglycin to target cells}}, url = {{http://dx.doi.org/10.1074/jbc.M501181200}}, doi = {{10.1074/jbc.M501181200}}, volume = {{280}}, year = {{2005}}, }