Catabodies to Degrade Transthyretin Amyloid

We describe nucleophilic catabodies from healthy humans without amyloidosis that degraded misfolded TTR (misTTR) without reactivity to the [correctly folded] TTR (phyTTR). IgM class B cell receptors specifically recognized the electrophilic analog of misTTR but not phyTTR. IgM but not IgG class antibodies hydrolyzed the particulate and soluble misTTR species. No misTTR-IgM binding was detected. The IgMs accounted for essentially all of the misTTR hydrolytic activity of unfractionated human serum. The IgMs did not degrade non-amyloidogenic, non-superantigenic proteins. The studies reveal a novel antibody property, the innate ability of IgMs to selectively degrade and dissolve toxic misTTR species as a first line immune function. Catalytic IgMs may clear misfolded TTR and delay amyloidosis [and] the innate antibody repertoire is a source of selective catabodies to toxic proteins. Link: http://dx.doi.org/10.1074/jbc.M114.557231
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