Hormonogenic donor Tyr2522 of bovine thyroglobulin. Insight into preferential T3 formation at thyroglobulin carboxyl terminus at low iodination level

Cetrangolo, Giovanni Paolo; Arcaro, Alessia; Lepore, Alessio; Graf, Maria; Mamone, Gianfranco; Ferranti, Pasquale; Palumbo, Giuseppe; Gentile, Fabrizio

doi:10.1016/j.bbrc.2014.05.144

Cited by 8 publications

(8 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast to Ca ions, there are more conflicting results on optimal Mg ion concentration for enhancing the osteogenic function of bone-forming cells 19–22,33,34. In this study, the total concentration of Mg ions released from the Mg samples at static and dynamic mode was 1.9 ppm (0.08 mM) and 2.9 ppm (0.12 mM), respectively, which are lower than that reportedly enhanced osteoblast function in other studies 19–22,33,34. Mg ion supplementation (up to 1.8 mM) dose dependently promoted osteoblast differentiation and mineralization of rabbit bone marrow MSCs 22.…”

Section: Resultsmentioning

confidence: 99%

<p>The relative effects of Ca and Mg ions on MSC osteogenesis in the surface modification of microrough Ti implants</p>

Park¹,

Hanawa²,

Chung³

2019

IJN

View full text Add to dashboard Cite

Purpose Calcium (Ca) and magnesium (Mg) ions have been used as promising bioactive ions in the surface chemistry modification of titanium (Ti) bone implants to increase bone regeneration capacity. However, it is not clear which (Ca or Mg) plays the more important role in the early osteogenic differentiation of mesenchymal stem cells (MSCs) when applied to the surface of commercially available microstructured Ti implants. This study investigated the relative effect of these two ions on the early osteogenic functionality of primary mouse bone marrow MSCs in order to obtain insights into the surface design of Ti implants with enhanced early osteogenic capacity. Methods and results Wet chemical treatment was performed to modify a microrough Ti implant surface using Ca or Mg ions. Both the Ca and Mg-incorporated surfaces accelerated early cellular events and the subsequent osteogenic differentiation of MSCs compared with an unmodified microrough Ti surface. Surface Mg modification exhibited a more potent osteoblast differentiation-promoting effect than the Ca modification. Surface Mg incorporation markedly inhibited the phosphorylation of β-catenin. Conclusion These results indicate that alteration of the surface chemistry of microstructured Ti implants by wet chemical treatment with Mg ions exerts a more effect on promoting the early osteogenic differentiation of MSCs than Ca ions by enhancing early cellular functions, including focal adhesion development and stabilization of intracellular β-catenin.

show abstract

Section: Resultsmentioning

confidence: 99%

<p>The relative effects of Ca and Mg ions on MSC osteogenesis in the surface modification of microrough Ti implants</p>

Park¹,

Hanawa²,

Chung³

2019

IJN

View full text Add to dashboard Cite

show abstract

“…3). The ChEL domain could either provide potential MIT donor residues to the DIT acceptor within the unique tail sequence (12) or it could provide the potential for ChEL dimerization (22,31). Indeed, we demonstrate that mutagenic by guest on May 11, 2018 http://www.jbc.org/ Downloaded from replacement of Y2744C confers covalent homodimerization of TG (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, however, neither of these mass spectrometry studies considered the possible significance that the conserved antepenultimate Tyr residue itself abundantly forms both MIT (making it a possible donor residue in T 3 formation) and DIT (as expected for an acceptor residue) (12).…”

Section: Introductionmentioning

confidence: 99%

“…Based on mass spectrometry analysis of a lightly iodinated carboxyl-terminal fragment of bovine Tg, Cetrangolo et al (12) reported that Y2522 (equivalent to Y2519 of mouse TG) and Y2555 (equivalent to Y2552 of mouse TG) exclusively form MIT, and these authors have suggested that both residues could be potential donors in T 3 formation at Y2748 [Dedieu et al used mass spectromety of mouse TG to confirm the donor site at Y2519 but argued in contrast that Y2552 was a probable T 3 acceptor site (13)]. Interestingly, however, neither of these mass spectrometry studies considered the possible significance that the conserved antepenultimate Tyr residue itself abundantly forms both MIT (making it a possible donor residue in T 3 formation) and DIT (as expected for an acceptor residue) (12).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Relationship between the dimerization of thyroglobulin and its ability to form triiodothyronine

Citterio

Morishita

Dakka

et al. 2018

Journal of Biological Chemistry

View full text Add to dashboard Cite

“…Remarkably, within the huge TG polypeptide, the most frequent site of T 4 formation resides just 5 residues from the N terminus (42), whereas more than half of all T 3 in TG is formed just 3 residues from the C terminus (24). It is known that DIT located at Tyr 130 is the DIT "donor" to form T 4 at Tyr 5 , but the precise mechanism of T 3 formation at the C terminus has not been established (19), although it has been postulated to involve one of several potential upstream MIT donor residues in the TG polypeptide (43) including residue 2520 of human TG (44).…”

Section: Thyroglobulin In T 3 Toxicosismentioning

confidence: 99%

De novo triiodothyronine formation from thyrocytes activated by thyroid-stimulating hormone

Citterio

Veluswamy

Morgan

et al. 2017

Journal of Biological Chemistry

View full text Add to dashboard Cite

The thyroid gland secretes primarily tetraiodothyronine (T), and some triiodothyronine (T). Under normal physiological circumstances, only one-fifth of circulating T is directly released by the thyroid, but in states of hyperactivation of thyroid-stimulating hormone receptors (TSHRs), patients develop a syndrome of relative T toxicosis. Thyroidal T production results from iodination of thyroglobulin (TG) at residues Tyr and Tyr, whereas thyroidal T production may originate in several different ways. In this study, the data demonstrate that within the carboxyl-terminal portion of mouse TG, T is formed independently of deiodination from T We found that upon iodination , T formation in TG was decreased in mice lacking TSHRs. Conversely, T that can be formed upon iodination of TG secreted from PCCL3 (rat thyrocyte) cells was augmented from cells previously exposed to increased TSH, a TSHR agonist, a cAMP analog, or a TSHR-stimulating antibody. We present data suggesting that TSH-stimulated TG phosphorylation contributes to enhanced T formation. These effects were reversed within a few days after removal of the hyperstimulating conditions. Indeed, direct exposure of PCCL3 cells to human serum from two patients with Graves' disease, but not control sera, led to secretion of TG with an increased intrinsic ability to form T upon iodination. Furthermore, TG secreted from human thyrocyte cultures hyperstimulated with TSH also showed an increased intrinsic ability to form T Our data support the hypothesis that TG processing in the secretory pathway of TSHR-hyperstimulated thyrocytes alters the structure of the iodination substrate in a way that enhances T formation, contributing to the relative T toxicosis of Graves' disease.

show abstract

Hormonogenic donor Tyr2522 of bovine thyroglobulin. Insight into preferential T3 formation at thyroglobulin carboxyl terminus at low iodination level

Cited by 8 publications

References 36 publications

<p>The relative effects of Ca and Mg ions on MSC osteogenesis in the surface modification of microrough Ti implants</p>

<p>The relative effects of Ca and Mg ions on MSC osteogenesis in the surface modification of microrough Ti implants</p>

Relationship between the dimerization of thyroglobulin and its ability to form triiodothyronine

De novo triiodothyronine formation from thyrocytes activated by thyroid-stimulating hormone

Contact Info

Product

Resources

About