| An in situ and in vitro investigation for the transglutaminase potential in tissue engineering. | |
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MedLine Citation:
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PMID: 19353617 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Transglutaminases (TGases) constitute a family of enzymes that stabilize protein assemblies by gamma-glutamyl-epsilon-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. |
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Authors:
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D I Zeugolis; P P Panengad; E S Y Yew; C Sheppard; T T Phan; M Raghunath |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of biomedical materials research. Part A Volume: 92 ISSN: 1552-4965 ISO Abbreviation: J Biomed Mater Res A Publication Date: 2010 Mar |
Date Detail:
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Created Date: 2010-02-03 Completed Date: 2010-04-12 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101234237 Medline TA: J Biomed Mater Res A Country: United States |
Other Details:
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Languages: eng Pagination: 1310-20 Citation Subset: IM |
Copyright Information:
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(c) 2009 Wiley Periodicals, Inc. |
Affiliation:
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Tissue Modulation Laboratory, National University of Singapore, Singapore. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Biocompatible Materials / chemistry, metabolism Biological Assay / instrumentation, methods Collagen / chemistry, metabolism Drug Carriers / chemistry, metabolism Glutamine / chemistry, metabolism Humans Isoenzymes / metabolism* Keloid / enzymology Lysine / chemistry, metabolism Materials Testing Molecular Structure Skin / enzymology Tissue Distribution Tissue Engineering / methods* Tissue Scaffolds Transglutaminases / metabolism* Wound Healing / physiology |
| Chemical | |
Reg. No./Substance:
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0/Biocompatible Materials; 0/Drug Carriers; 0/Isoenzymes; 0/atelocollagen; 56-85-9/Glutamine; 56-87-1/Lysine; 9007-34-5/Collagen; EC 2.3.2.13/Transglutaminases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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