Publication type: Article in scientific journal
Type of review: Peer review (publication)
Title: An in situ and in vitro investigation for the transglutaminase potential in tissue engineering
Authors: Zeugolis, D. I.
Panengad, P. P.
Yew, E. S. Y.
Sheppard, C.
Phan, T. T.
Raghunath, M.
DOI: 10.1002/jbm.a.32383
Published in: Journal of Biomedical Materials Research
Volume(Issue): 92A
Issue: 4
Page(s): 1310
Pages to: 1320
Issue Date: 2009
Publisher / Ed. Institution: Wiley
ISSN: 1552-4965
Language: English
Subject (DDC): 571: Physiology and related subjects
610: Medicine and health
Abstract: Transglutaminases (TGases) constitute a family of enzymes that stabilize protein assemblies by γ‐glutamyl‐ε‐lysine crosslinks. The role of tissue transglutaminase (TGase 2) in several pathophysiologies, wound healing applications, biomaterials functionalization, and drug delivery systems provides grounds for its use in tissue engineering. Herein, we initially studied the endogenous TGase activity and expression under normal (skin, duodenum, colon, and small bowel) and pathophysiological (keloid scar) conditions on cadaveric human tissues. Successful inhibition was achieved using low concentrations of BOC‐DON‐QIV‐OMe (0.1 mM and 1 mM for normal skin and keloid scar, respectively), iodoacetamide (0.1 mM and 1 mM for normal skin and keloid scar, respectively), and cystamine dihydrochloride (1 mM and 10 mM for normal skin and keloid scar, respectively), whilst di‐BOC‐cystamine was found ineffective even at 100 mM concentration. Secondly, the addition of exogenous guinea pig liver transglutaminase (gpTGase) onto the inhibited tissues and collagen scaffolds was studied, and results presented advocate its use as potential tissue adhesive and drug delivery tool. However, the investigation of its crosslinking extent using second harmonic generation microscopy and differentially scanning calorimetry revealed rather poor stabilization function. Overall, our study indicates that TGase 2 has a role as a biological glue to consolidate various micro‐structural components of tissues and biomaterials.
URI: https://digitalcollection.zhaw.ch/handle/11475/12202
Fulltext version: Published version
License (according to publishing contract): Licence according to publishing contract
Departement: Life Sciences and Facility Management
Organisational Unit: Institute of Chemistry and Biotechnology (ICBT)
Appears in collections:Publikationen Life Sciences und Facility Management

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Zeugolis, D. I., Panengad, P. P., Yew, E. S. Y., Sheppard, C., Phan, T. T., & Raghunath, M. (2009). An in situ and in vitro investigation for the transglutaminase potential in tissue engineering. Journal of Biomedical Materials Research, 92A(4), 1310–1320. https://doi.org/10.1002/jbm.a.32383
Zeugolis, D.I. et al. (2009) ‘An in situ and in vitro investigation for the transglutaminase potential in tissue engineering’, Journal of Biomedical Materials Research, 92A(4), pp. 1310–1320. Available at: https://doi.org/10.1002/jbm.a.32383.
D. I. Zeugolis, P. P. Panengad, E. S. Y. Yew, C. Sheppard, T. T. Phan, and M. Raghunath, “An in situ and in vitro investigation for the transglutaminase potential in tissue engineering,” Journal of Biomedical Materials Research, vol. 92A, no. 4, pp. 1310–1320, 2009, doi: 10.1002/jbm.a.32383.
ZEUGOLIS, D. I., P. P. PANENGAD, E. S. Y. YEW, C. SHEPPARD, T. T. PHAN und M. RAGHUNATH, 2009. An in situ and in vitro investigation for the transglutaminase potential in tissue engineering. Journal of Biomedical Materials Research. 2009. Bd. 92A, Nr. 4, S. 1310–1320. DOI 10.1002/jbm.a.32383
Zeugolis, D. I., P. P. Panengad, E. S. Y. Yew, C. Sheppard, T. T. Phan, and M. Raghunath. 2009. “An in Situ and in Vitro Investigation for the Transglutaminase Potential in Tissue Engineering.” Journal of Biomedical Materials Research 92A (4): 1310–20. https://doi.org/10.1002/jbm.a.32383.
Zeugolis, D. I., et al. “An in Situ and in Vitro Investigation for the Transglutaminase Potential in Tissue Engineering.” Journal of Biomedical Materials Research, vol. 92A, no. 4, 2009, pp. 1310–20, https://doi.org/10.1002/jbm.a.32383.


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