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1.
JBJS Case Connect ; 10(3): e20.00130, 2020.
Article in English | MEDLINE | ID: mdl-32910610

ABSTRACT

CASE: We present a 20-year-old man who suffered anaphylactic shock during posterior spinal fusion for neuromuscular scoliosis with the offending agent later identified via intradermal testing to be tranexamic acid (TXA). CONCLUSION: TXA, although an increasingly common drug, can be the cause of sudden anaphylactic shock intraoperatively. This now represents the fifth reported case in the literature of patients ranging from 15 years to 80 years old with no previous exposure to the drug.


Subject(s)
Anaphylaxis/chemically induced , Antifibrinolytic Agents/immunology , Intraoperative Complications/chemically induced , Scoliosis/surgery , Tranexamic Acid/immunology , Adult , Antifibrinolytic Agents/adverse effects , Humans , Male , Pelizaeus-Merzbacher Disease/complications , Scoliosis/etiology , Spinal Fusion , Tranexamic Acid/adverse effects
2.
J Agric Food Chem ; 65(34): 7542-7552, 2017 Aug 30.
Article in English | MEDLINE | ID: mdl-28771001

ABSTRACT

Wheat gluten confers superior baking quality to wheat based products but elicits a pro-inflammatory immune response in patients with celiac disease. Transamidation of gluten by microbial transglutaminase (mTG) and tissue transglutaminase (tTG) reduces the immunogenicity of gluten; however, little information is available on the minimal modification sufficient to eliminate gliadin immunogenicity nor has the effectiveness of transamidation been studied with T-cell clones from patients. Here we demonstrate that mTG can efficiently couple three different acyl-acceptor molecules, l-lysine, glycine ethyl ester, and hydroxylamine, to gliadin peptides and protein. While all three acyl-acceptor molecules were cross-linked to the same Q-residues, not all modifications were equally effective in silencing T-cell reactivity. Finally, we observed that tTG can partially reverse the mTG-catalyzed transamidation by its isopeptidase activity. These results set the stage to determine the impact of these modifications on the baking quality of gluten proteins and in vivo immunogenicity of such food products.


Subject(s)
Gliadin/chemistry , Gliadin/immunology , Streptomyces/enzymology , Transglutaminases/metabolism , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Biocatalysis , Glutens/chemistry , Glutens/immunology , Humans , Molecular Structure , Streptomyces/genetics , T-Lymphocytes/immunology , Tranexamic Acid/immunology , Transglutaminases/genetics
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