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: | , |
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| Formato: | article |
| Lenguaje: | RU |
| Publicado: |
Sankt-Peterburg : NIIÈM imeni Pastera
2014
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/904c3c32ac15408f98979553e39e666b |
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| Sumario: | 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. |
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