SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE
Abstract. Besides the multiple hydrolytic enzymes, lysosomes are equipped with proteins apt to activate sphyngo-lipids — saposins (SAP). SAP belong to a broad and diverse family of moderate-size (~80 AA) saposin-like proteins (SAPLIP) containing specific domains with three disulfid e bonds bridging...
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Sankt-Peterburg : NIIÈM imeni Pastera
2014
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oai:doaj.org-article:904c3c32ac15408f98979553e39e666b2021-11-22T07:09:45ZSAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE2220-76192313-739810.15789/2220-7619-2012-3-597-602https://doaj.org/article/904c3c32ac15408f98979553e39e666b2014-07-01T00:00:00Zhttps://www.iimmun.ru/iimm/article/view/75https://doaj.org/toc/2220-7619https://doaj.org/toc/2313-7398Abstract. Besides the multiple hydrolytic enzymes, lysosomes are equipped with proteins apt to activate sphyngo-lipids — saposins (SAP). SAP belong to a broad and diverse family of moderate-size (~80 AA) saposin-like proteins (SAPLIP) containing specific domains with three disulfid e bonds bridging six cysteine residues. The diversity of SAPLIPS is likely explained by their involvement in distinct phases of engulfed bacteria digesting. Functionally similar SAPLIP were identified in a wide range of species — from amoeba to mammals, including humans. Saposins per se form a subfamily with six members: saposins A-D and the protein GM2 which possesses activatory functions. SAP do not have enzymatic activity, are heat-stable and protease resistant. The major in vivo function of SAP is released via participation in sphyngolipid catabolism and membrane digestion. In addition, complex association of SAP with membrane bi-layer and CD1 glycolipids is essential for loading lipid antigens onto antigen-presenting CD1 molecules for subsequent activation of lipid-specific T-cells. Of particular interest is participation of SAP in cross-presentation of bacterial antigens to CD8+ T-cells. A broad spectrum of SAP and SAPLIP involvement in the reactions of innate and adaptive immunity indicates their evolutionary conserved role in host defense.V. V. YeremeevA. S. AptSankt-Peterburg : NIIÈM imeni Pasteraarticlesaposinssaposin-like proteinsimmunityInfectious and parasitic diseasesRC109-216RUInfekciâ i Immunitet, Vol 2, Iss 3, Pp 597-602 (2014) |
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saposins saposin-like proteins immunity Infectious and parasitic diseases RC109-216 |
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saposins saposin-like proteins immunity Infectious and parasitic diseases RC109-216 V. V. Yeremeev A. S. Apt SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
description |
Abstract. Besides the multiple hydrolytic enzymes, lysosomes are equipped with proteins apt to activate sphyngo-lipids — saposins (SAP). SAP belong to a broad and diverse family of moderate-size (~80 AA) saposin-like proteins (SAPLIP) containing specific domains with three disulfid e bonds bridging six cysteine residues. The diversity of SAPLIPS is likely explained by their involvement in distinct phases of engulfed bacteria digesting. Functionally similar SAPLIP were identified in a wide range of species — from amoeba to mammals, including humans. Saposins per se form a subfamily with six members: saposins A-D and the protein GM2 which possesses activatory functions. SAP do not have enzymatic activity, are heat-stable and protease resistant. The major in vivo function of SAP is released via participation in sphyngolipid catabolism and membrane digestion. In addition, complex association of SAP with membrane bi-layer and CD1 glycolipids is essential for loading lipid antigens onto antigen-presenting CD1 molecules for subsequent activation of lipid-specific T-cells. Of particular interest is participation of SAP in cross-presentation of bacterial antigens to CD8+ T-cells. A broad spectrum of SAP and SAPLIP involvement in the reactions of innate and adaptive immunity indicates their evolutionary conserved role in host defense. |
format |
article |
author |
V. V. Yeremeev A. S. Apt |
author_facet |
V. V. Yeremeev A. S. Apt |
author_sort |
V. V. Yeremeev |
title |
SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
title_short |
SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
title_full |
SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
title_fullStr |
SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
title_full_unstemmed |
SAPOSIN-LIKE PROTEINS IN ANTI-INFECTIOUS IMMUNE RESPONSE |
title_sort |
saposin-like proteins in anti-infectious immune response |
publisher |
Sankt-Peterburg : NIIÈM imeni Pastera |
publishDate |
2014 |
url |
https://doaj.org/article/904c3c32ac15408f98979553e39e666b |
work_keys_str_mv |
AT vvyeremeev saposinlikeproteinsinantiinfectiousimmuneresponse AT asapt saposinlikeproteinsinantiinfectiousimmuneresponse |
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1718418054042353664 |