NDLI: Effects of the regulatory ligands calcium and GTP on the thermal stability of tissue transglutaminase

Content Provider	Springer Nature Link
Author	Cervellati, Carlo Montin, Katy Squerzanti, Monica Mischiati, Carlo Ferrari, Carlo Spizzi, Francesco Mariani, Paolo Amenitsch, Heinz Bergamini, Carlo M. Lanzara, Vincenzo
Copyright Year	2011
Abstract	Tissue transglutaminase undergoes thermal inactivation with first-order kinetics at moderate temperatures, in a process which is affected in opposite way by the regulatory ligands calcium and GTP, which stabilize different conformations. We have explored the processes of inactivation and of unfolding of transglutaminase and the effects of ligands thereon, combining approaches of differential scanning calorimetry (DSC) and of thermal analysis coupled to fluorescence spectroscopy and small angle scattering. At low temperature (38–45°C), calcium promotes and GTP protects from inactivation, which occurs without detectable disruption of the protein structure but only local perturbations at the active site. Only at higher temperatures (52–56°C), the protein structure undergoes major rearrangements with alterations in the interactions between the N- and C-terminal domain pairs. Experiments by DSC and fluorescence spectroscopy clearly indicate reinforced and weakened interactions of the domains in the presence of GTP and of calcium, and different patterns of unfolding. Small angle scattering experiments confirm different pathways of unfolding, with attainment of limiting values of gyration radius of 52, 60 and 90 Å in the absence of ligands and in the presence of GTP and calcium. Data by X-rays scattering indicate that ligands influence retention of a relatively compact structure in the protein even after denaturation at 70°C. These results suggest that the complex regulation of the enzyme by ligands involves both short- and long-range effects which might be relevant for understanding the turnover of the protein in vivo.
Starting Page	2233
Ending Page	2242
Page Count	10
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	42
Issue Number	6
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2011-06-26
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Tissue transglutaminase Regulatory ligands Thermal inactivation Fluorescence spectroscopy Differential scanning calorimetry Small-angle scattering Biochemical Engineering Analytical Chemistry Biochemistry Proteomics Life Sciences Neurobiology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Thermodynamics of binding of regulatory ligands to tissue transglutaminase

Unfolding studies of tissue transglutaminase

Effects of ligands on the stability of tissue transglutaminase: studies in vitro suggest possible modulation by ligands of protein turn-over in vivo

Tissue transglutaminase and the stress response

Tissue transglutaminase in celiac disease: role of autoantibodies

Role of tissue transglutaminase in age-associated ventricular stiffness

Tissue transglutaminase: a new target to reverse cancer drug resistance

Tissue transglutaminase in tumour progression: friend or foe?

Effects of the regulatory ligands calcium and GTP on the thermal stability of tissue transglutaminase

Effects of the regulatory ligands calcium and GTP on the thermal stability of tissue transglutaminase

Similar Documents

Thermodynamics of binding of regulatory ligands to tissue transglutaminase

Unfolding studies of tissue transglutaminase

Effects of ligands on the stability of tissue transglutaminase: studies in vitro suggest possible modulation by ligands of protein turn-over in vivo

Tissue transglutaminase and the stress response

Tissue transglutaminase in celiac disease: role of autoantibodies

Role of tissue transglutaminase in age-associated ventricular stiffness

Tissue transglutaminase: a new target to reverse cancer drug resistance

Tissue transglutaminase in tumour progression: friend or foe?

Effects of the regulatory ligands calcium and GTP on the thermal stability of tissue transglutaminase

Effects of the regulatory ligands calcium and GTP on the thermal stability of tissue transglutaminase