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Chawla, Aarti (2)
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Zoltewicz, J. Susie (1)
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Characterization of Antibodies that Detect Human GFAP after Traumatic Brain Injury
Zoltewicz, J. Susie
Newsom, Kimberly J.
After traumatic brain injury (TBI), glial fibrillary acidic protein (GFAP) and other brain-derived proteins and their breakdown products are released into biofluids such as CSF and blood. Recently, a sandwich ELISA was constructed that measured GFAP concentrations in CSF or serum from human mild-moderate TBI patients. The goals of the present study were to characterize the same two antibodies used in this ELISA, and to determine which GFAP bands are detected by this antibody combination. Here, both antibodies recognized GFAP specifically in human brain and post-TBI CSF in a cluster of bands ranging from 50–38 kDa, that resembled bands from calpain-cleaved GFAP. By immunoprecipitation, the anti-GFAP Capture antibody recovered full length GFAP and its breakdown products from human brain lysate and post-TBI CSF. These findings demonstrate that the anti-GFAP ELISA antibodies non-preferentially detect intact GFAP and GFAP breakdown products, underscoring their utility for detecting brain injury in human patients.
GFAP; GFAP-BDP; traumatic brain injury; human
Community signaling between Streptococcus gordonii and Porphyromonas gingivalis is controlled by the transcriptional regulator CdhR
Bainbridge, Brian W.
Demuth, Donald R.
Lamont, Richard J.
Interspecies signaling between P. gingivalis and S. gordonii serves to constrain development of dual species communities. Contact with S. gordonii propagates a tyrosine phosphorylation dependent signal within P. gingivalis that culminates in reduced transcription of adhesin and signaling genes. Here we demonstrate the involvement of the P. gingivalis orphan LuxR family transcription factor PGN_1373, which we designate CdhR, in this control pathway. Expression of cdhR is elevated following contact with S. gordonii; however, regulation of cdhR did not occur in a mutant lacking the tyrosine phosphatase Ltp1, indicating that CdhR and Ltp1 are components of the same regulon. Contact between S. gordonii and a CdhR mutant resulted in increased transcription of mfa, encoding the subunit of the short fimbriae, along with higher levels of Mfa protein. Expression of luxS, encoding AI-2 synthase, was also increased in the cdhR mutant after contact with S. gordonii. The Mfa adhesive function and AI-2-dependent signaling participate in the formation and development of dual species communities, and consistent with this the cdhR mutant displayed elevated accumulation on a substratum of S. gordonii. Recombinant CdhR protein bound to upstream regulatory regions of both mfa and luxS, indicating that CdhR has a direct effect on gene expression. LuxS was also found to participate in a positive feedback loop that suppresses CdhR expression. Interaction of Mfa fimbriae with S. gordonii is necessary to initiate signaling through CdhR. These results reveal CdhR to be an effector molecule in a negative regulatory network that controls P. gingivalis-S. gordonii heterotypic communities.
biofilm; fimbriae; luxS; signaling
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