Asset Details
Do you wish to reserve the book?
Identification of a receptor required for the anti-inflammatory activity of IVIG
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Identification of a receptor required for the anti-inflammatory activity of IVIG
Do you wish to request the book?
Identification of a receptor required for the anti-inflammatory activity of IVIG
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Identification of a receptor required for the anti-inflammatory activity of IVIG
2008
Overview
The anti-inflammatory activity of intravenous Ig (IVIG) results from a minor population of the pooled IgG molecules that contains terminal α2,6-sialic acid linkages on their Fc-linked glycans. These anti-inflammatory properties can be recapitulated with a fully recombinant preparation of appropriately sialylated IgG Fc fragments. We now demonstrate that these sialylated Fcs require a specific C-type lectin, SIGN-R1, (specific ICAM-3 grabbing non-integrin-related 1) expressed on macrophages in the splenic marginal zone. Splenectomy, loss of SIGN-R1⁺ cells in the splenic marginal zone, blockade of the carbohydrate recognition domain (CRD) of SIGN-R1, or genetic deletion of SIGN-R1 abrogated the anti-inflammatory activity of IVIG or sialylated Fc fragments. Although SIGN-R1 has not previously been shown to bind to sialylated glycans, we demonstrate that it preferentially binds to 2,6-sialylated Fc compared with similarly sialylated, biantennary glycoproteins, thus suggesting that a specific binding site is created by the sialylation of IgG Fc. A human orthologue of SIGN-R1, DC-SIGN, displays a similar binding specificity to SIGN-R1 but differs in its cellular distribution, potentially accounting for some of the species differences observed in IVIG protection. These studies thus identify an antibody receptor specific for sialylated Fc, and present the initial step that is triggered by IVIG to suppress inflammation.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Animals
/ Anti-Inflammatory Agents, Non-Steroidal - immunology
/ Anti-Inflammatory Agents, Non-Steroidal - pharmacology
/ Cell Adhesion Molecules - genetics
/ Cell Adhesion Molecules - immunology
/ Humans
/ Immunoglobulin Fc Fragments - immunology
/ Immunoglobulins, Intravenous - immunology
/ Immunoglobulins, Intravenous - pharmacology
/ Lectins
/ Lectins, C-Type - immunology
/ Mice
/ N-Acetylneuraminic Acid - immunology
/ Receptors, Cell Surface - genetics
/ Receptors, Cell Surface - immunology
/ Spleen
