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Fibrinogen promotes autoimmunity and demyelination via chemokine release and antigen presentation [Rn]

ABSTRACT: Determination of the mechanism by which fibrinogen, a central blood coagulation protein drives immunological responses targeted to the CNS. Results identify the factors involved in the regulation and provide mechanistic basis. We subjected fibrin-stimulated microglia to microarray to determine the genes involved in innate and adaptive immune responses by fibrinogen deposited in the CNS after blood-brain barrier disruption.

ORGANISM(S): Rattus norvegicus

PROVIDER: GSE71083 | GEO | 2015/09/16

SECONDARY ACCESSION(S): PRJNA290323

REPOSITORIES: GEO

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Fibrinogen promotes autoimmunity and demyelination via chemokine release and antigen presentation [Rn]

Project description:Determination of the mechanism by which fibrinogen, a central blood coagulation protein drives immunological responses targeted to the CNS. Results identify the factors involved in the regulation and provide mechanistic basis. We subjected fibrin-stimulated microglia to microarray to determine the genes involved in innate and adaptive immune responses by fibrinogen deposited in the CNS after blood-brain barrier disruption. Rat microglia were stimulated with fibrin for 6 hr and subjected for RNA extraction and hybridization on Affymatrix microarrays. Two unstimulated and two fibrin-stimulated samples were generated.

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Fibrinogen promotes autoimmunity and demyelination via chemokine release and antigen presentation [Mm]

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Fibrinogen promotes autoimmunity and demyelination via chemokine release and antigen presentation

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

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Blood coagulation protein fibrinogen promotes autoimmunity and demyelination via chemokine release and antigen presentation.

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Fibrinogen function achieved through multiple covalent states

Project description:Disulfide bonds link pairs of cysteine amino acids and their formation is assumed to be complete in the mature, functional protein. We tested this assumption by quantifying the redox state of disulfide bonds in the thrombosis protein, fibrinogen. There is an extraordinary disulfide lability in fibrinogen, with 13 bonds in the protein ranging from 10 to 50% reduced in human donors, indicating that fibrinogen exists in hundreds of different disulfide-bonded states. The significance of this finding for fibrinogen conversion to fibrin was investigated. Fibrin polymer formation triggers formation of disulfides in fibrin molecules, which is required for a robust fibrin matrix that withstands the mechanical forces of flowing blood and resists premature fibrinolysis. The covalent states of fibrinogen are changed by fluid shear forces ex vivo and in vivo, indicating that the different states are dynamic. These findings demonstrate that proteins can exist and function as a multitude of covalent forms.

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