The use of IgM-enriched immunoglobulin in adult patients with sepsis.

08:00 EDT 3rd June 2018 | BioPortfolio

Summary of "The use of IgM-enriched immunoglobulin in adult patients with sepsis."

The administration of intravenous immunoglobulins (IVIG) is one of the adjunct therapies investigated and applied to sepsis patients, with the first studies being published nearly four decades ago. Intravenous immunoglobulin preparations have several mechanisms of action e.g. antigen neutralization, Fc-receptor blockade on phagocytic cells, modulation of cytokine responses and modulation of immune cell functions. The currently available evidence suggesting the use of intravenous immunoglobulins in sepsis is weak, but results from recent trials and systematic metanalyses seem more promising for the use of intravenous IgM-enriched immunoglobulins (IVIgGM) in septic patients. Nevertheless, the results of studies examining its value are contradicting. The purpose of this review is to summarize and present, clearly and thoroughly, the currently available data regarding established and future potential clinical uses of IVIgGM in patients with sepsis.


Journal Details

This article was published in the following journal.

Name: Journal of critical care
ISSN: 1557-8615
Pages: 30-35


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Adult Patients with Severe Sepsis

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A 15 kD "joining" peptide that forms one of the linkages between monomers of IMMUNOGLOBULIN A or IMMUNOGLOBULIN M in the formation of polymeric immunoglobulins. There is one J chain per one IgA dimer or one IgM pentamer. It is also involved in binding the polymeric immunoglobulins to POLYMERIC IMMUNOGLOBULIN RECEPTOR which is necessary for their transcytosis to the lumen. It is distinguished from the IMMUNOGLOBULIN JOINING REGION which is part of the IMMUNOGLOBULIN VARIABLE REGION of the immunoglobulin light and heavy chains.

The class of heavy chains found in IMMUNOGLOBULIN E. They have a molecular weight of approximately 72 kDa and they contain about 550 amino acid residues arranged in five domains and about three times more carbohydrate than the heavy chains of IMMUNOGLOBULIN A; IMMUNOGLOBULIN D; and IMMUNOGLOBULIN G.

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