Characterization of Highly Reactive Sequences for Transglutaminase 2 and Factor XIIIa

2008 ◽  
pp. 325-331
Author(s):  
Yoshiaki Sugimura ◽  
Miyako Kitamura ◽  
Masayo Hosono ◽  
Hideki Shibata ◽  
Masatoshi Maki ◽  
...  
Keyword(s):  
Transglutaminase 2 ◽  
Factor Xiiia

scholarly journals HLA‐DQ genotype and biochemical characterization of anti‐transglutaminase 2 antibodies in patients with type 1 diabetes mellitus in Taiwan

2020 ◽  
Vol 34 (6) ◽  
pp. 8459-8474
Author(s):  
Yann‐Jinn Lee ◽  
Wei‐Hsin Ting ◽  
Yi‐Wen Yang ◽  
Cheng‐Jui Lin ◽  
Yu‐Ting Hsieh ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Type 1 Diabetes ◽  
Type 1 Diabetes Mellitus ◽  
Biochemical Characterization ◽  
Transglutaminase 2 ◽  
Hla Dq

scholarly journals Reactivity of the N-terminal Region of Fibronectin Protein to Transglutaminase 2 and Factor XIIIA

2011 ◽  
Vol 286 (37) ◽  
pp. 32220-32230 ◽  
Author(s):  
Brian R. Hoffmann ◽  
Douglas S. Annis ◽  
Deane F. Mosher
Keyword(s):  
Transglutaminase 2 ◽  
Terminal Region ◽  
Factor Xiiia

HPLC–MS characterization of cyclo-statherin Q-37, a specific cyclization product of human salivary statherin generated by transglutaminase 2

2006 ◽  
Vol 29 (17) ◽  
pp. 2600-2608 ◽  
Author(s):  
Tiziana Cabras ◽  
Rosanna Inzitari ◽  
Chiara Fanali ◽  
Emanuele Scarano ◽  
Maria Patamia ◽  
...  
Keyword(s):  
Transglutaminase 2 ◽  
Cyclization Product

scholarly journals Erratum

2010 ◽  
Vol 15 (9) ◽  
pp. 1178-1178
Keyword(s):  
Transglutaminase 2 ◽  
Correct Structure

Schaertl S, Prime M, Wityak J, Dominguez C, Munoz-Sanjuan I, Pacifici RE, et al: A profiling platform for the characterization of transglutaminase 2 (TG2) inhibitors. J Biomol Screen 2010;15:478-487. (Original DOI: 10.1177/1087057110366035) In the June 2010 issue of the Journal of Biomolecular Screening, Figure 5 of the above-mentioned article by Schaertl et al. contained an incorrect structure. The correct structure for “Z-DON” (Z-DON-Val-Pro-Leu-OMe) appears below. The authors apologize for the error.

Expression, Purification and Characterization of Recombinant Human Coagulation Factor XIIIa in Pichia Pastoris

2020 ◽  
Vol 27 ◽  
Author(s):  
Linyan Cheng ◽  
Ting Zhang ◽  
Yuchang Fei ◽  
Hao Shen ◽  
Hui Huang ◽  
...  
Keyword(s):  
Wound Healing ◽  
Biological Activity ◽  
Pichia Pastoris ◽  
Critical Role ◽  
Coagulation Factor ◽  
Factor Xiiia ◽  
Expression And Purification ◽  
Methanol Induction ◽  
Healing Tissue

Background: Coagulation factor XIIIa(FXIIIa) plays a critical role in the final stage of blood coagulation. It is extremely important in wound healing, tissue repairing and promoting cell adhesion. The deficiency of the coagulation factor can cause hemorrhage and slow wound healing. Objective: In this study, recombinant pPICZαC-FXIIIa was expressed in Pichia pastoris, purified as well as its biological activity was determined. Methods: The FXIIIa fragment obtained from the human placenta was inserted into pPICZαC to obtain pPICZαC-FXIIIa, which was transformed into X33 after linearization, and FXIIIa inserted into Pichia pastoris X33 was screened for methanol induction. The expressed product was identified by western blotting, then the supernatant was purified by affinity chromatography, and the purified product was determined by plasma coagulation experiment. Results: Polymerase Chain Reaction(PCR) showed that the FXIIIa fragment of 2250 bp was inserted successfully into pPICZαC. The expression and purification products of the same molecular weight as target protein(about 83 kDa) were obtained, which solidified significantly when reacted with plasma. Conclusion: The expression and purification products were successful, with sufficient biological activity, which can be used as a candidate FXIIIa hemostatic agent in genetic engineering.

Synthesis and Functional Characterization of Tridegin and Its Analogues: Inhibitors and Substrates of Factor XIIIa

ChemMedChem ◽  
2011 ◽  
Vol 7 (2) ◽  
pp. 326-333 ◽  
Author(s):  
Miriam Böhm ◽  
Toni Kühl ◽  
Kornelia Hardes ◽  
Richard Coch ◽  
Christoph Arkona ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Factor Xiiia

scholarly journals Characterization of cDNA coding for human factor XIIIa.

1986 ◽  
Vol 83 (21) ◽  
pp. 8024-8028 ◽  
Author(s):  
U. Grundmann ◽  
E. Amann ◽  
G. Zettlmeissl ◽  
H. A. Kupper
Keyword(s):  
Human Factor ◽  
Factor Xiiia

scholarly journals Expression and Localization of Plasma Transglutaminase Factor XIIIA in Bone

2007 ◽  
Vol 55 (7) ◽  
pp. 675-685 ◽  
Author(s):  
Yukiko Nakano ◽  
Hadil F. Al-Jallad ◽  
Aisha Mousa ◽  
Mari T. Kaartinen
Keyword(s):  
Transglutaminase 2 ◽  
Pcr Primers ◽  
Cell Types ◽  
Proteolytic Processing ◽  
Factor Xiiia ◽  
Pcr Analysis ◽  
Rt Pcr ◽  
Osteoblast Cell Line

Transglutaminases (TGs) are protein crosslinking enzymes involved in cell adhesion and signaling and matrix stabilization and maturation, in many cell types and tissues. We previously described that in addition to transglutaminase 2 (TG2), cultured MC3T3-E1 osteoblasts also express the plasma TG Factor XIIIA (FXIIIA). Here we report on the expression and localization of FXIIIA in bone in vivo and provide confirmatory in vitro data. Immuno-histochemistry and in situ hybridization demonstrated that FXIIIA is expressed by osteoblasts and osteocytes in long bones formed by endochondral ossification (femur) and flat bones formed primarily by intramembranous ossification (calvaria and mandible). FXIIIA immuno-reactivity was localized to osteoblasts, osteocytes, and the osteoid. RT-PCR analysis revealed FXIIIA expression by both primary osteoblasts and by the MC3T3-E1 osteoblast cell line. Western blot analysis of bone and MC3T3-E1 culture extracts demonstrated that FXIIIA is produced mainly as a small, 37-kDa form. Sequential RT-PCR analysis using overlapping PCR primers spanning the full FXIIIA gene showed that the entire FXIIIA gene is expressed, thus indicating that the 37-kDa FXIIIA is not a splice variant but a product of posttranslational proteolytic processing. Forskolin inhibition of osteoblast differentiation revealed that FXIIIA processing is regulated by the protein kinase A pathway.

scholarly journals Characterization of Transglutaminase 2 activity inhibitors in monocytes in vitro and their effect in a mouse model for multiple sclerosis

PLoS ONE ◽  
2018 ◽  
Vol 13 (4) ◽  
pp. e0196433 ◽  
Author(s):  
Navina L. Chrobok ◽  
John G. J. M. Bol ◽  
Cornelis A. Jongenelen ◽  
John J. P. Brevé ◽  
Said El Alaoui ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Mouse Model ◽  
Transglutaminase 2

scholarly journals Correction: Characterization of Transglutaminase 2 activity inhibitors in monocytes in vitro and their effect in a mouse model for multiple sclerosis

PLoS ONE ◽  
2018 ◽  
Vol 13 (12) ◽  
pp. e0209522
Author(s):  
Navina L. Chrobok ◽  
John G. J. M. Bol ◽  
Cornelis A. Jongenelen ◽  
John J. P. Brevé ◽  
Said El Alaoui ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Mouse Model ◽  
Transglutaminase 2
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