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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Autores principales: V. V. Yeremeev, A. S. Apt
Formato: article
Lenguaje:RU
Publicado: Sankt-Peterburg : NIIÈM imeni Pastera 2014
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Acceso en línea:https://doaj.org/article/904c3c32ac15408f98979553e39e666b
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spelling 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)
institution DOAJ
collection DOAJ
language RU
topic saposins
saposin-like proteins
immunity
Infectious and parasitic diseases
RC109-216
spellingShingle 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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