The hydrophobic C‐terminal sequence of transthyretin affects its catalytic kinetics towards amidated neuropeptide Y

Tangthavewattana, Sukanya; Leelawatwattana, Ladda; Prapunpoj, Porntip

doi:10.1002/2211-5463.12604

Cited by 5 publications

(4 citation statements)

References 69 publications

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“…It is a transporter for thyroid hormones and a retinol binding protein with very modest proteolytic activity towards very few substrates. 22 In human medicine, a reduction in plasma transthyretin could be related to severe acute phase response to thyroid diseases, but in veterinary medicine its role is not completely elucidated. 23 The few studies performed in animals have shown a lower concentration of transthyretin in 1 month diarrheic calves compared with healthy controls and reduced plasma concentrations in Mycobacterium avium paratuberculosis seropositive cows compared to healthy cattle.…”

Section: Discussionmentioning

confidence: 99%

Faecal proteome in clinically healthy dogs and cats: Findings in pooled faeces from 10 cats and 10 dogs

Cerquetella

Marchegiani

Mangiaterra

et al. 2021

Veterinary Record Open

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Background In the scientific literature, there are only a few manuscripts available on small animal faecal proteomics. Methods In the present pilot study, this evaluation was performed using pooled faecal samples from 10 clinically healthy dogs and, for the first time, in 10 clinically healthy cats by mean of two‐dimensional electrophoresis followed by liquid chromatography‐tandem mass spectrometry. Results Our results showed the presence of nine (albumin, alkaline phosphatase, chymotrypsin‐C‐like, cytosol aminopeptidase, elastase‐3B/proteinase E, immunoglobulins and nuclear pore membrane glycoprotein 210) and 14 (albumin, caspase recruitment domain‐containing protein, chymotrypsin‐like, deleted in malignant brain tumours 1 protein‐like, hypothetical protein LOC107375, immunoglobulin, kallikrein‐1, superoxide dismutase, transthyretin precursor, interstitial collagenase‐like) different proteins in canine and feline faeces, respectively. Conclusion These preliminary findings document the presence of a range of proteins in the faeces of apparently healthy dogs and cats and may serve as a basis for larger, prospective studies to establish reference proteomic data against which diseased populations can be compared.

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Section: Discussionmentioning

confidence: 99%

Faecal proteome in clinically healthy dogs and cats: Findings in pooled faeces from 10 cats and 10 dogs

Cerquetella

Marchegiani

Mangiaterra

et al. 2021

Veterinary Record Open

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“…A sensitive fluorescence-based method for detecting the proteolytic activity towards Aβ and other substrates of TTR has been previously developed in our laboratory [10,17]. The pattern and the kinetic parameters of the specific cleavage of Aβ 1-42 by C. porosus and human TTRs were also demonstrated [17].…”

Section: Discussionmentioning

confidence: 99%

“…Predominant changes in TTR structure occur at the N-terminal sequence, and the N-terminal region of the avian and the reptilian are longer and more hydrophobic than that of the eutherian [5,6]. The changes influence on not only the function of TTR as distributors for TH and retinal [7,8], but also its catalytic property [9,10]. Beside functioning as TH and retinal distributors, TTR proteolytic activity towards amyloid beta (Aβ) and a few specific target proteins is evidenced for its important physiological roles in the central and peripheral nervous systems of human [11,12].…”

Section: Introductionmentioning

confidence: 99%

The influence of Zn2+-binding motif sequence on the catalytic activity of transthyretin towards amyloid beta

Krainara¹,

Leelawatwattana²,

Prapunpoj³

2021

ScienceAsia

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The proteolysis property of transthyretin (TTR) was believed to be important for physiological processes and have therapeutic potential. In the present study, we interchanged the corresponding sequences of Zn 2+ binding motif between human and Crocodylus porosus TTRs. The kinetic parameters of the proteolytic activity towards amyloid beta 1-42 (Aβ 1-42 ) of the mutated TTRs were determined by using a sensitive fluorescence-based method, and compared with the wild types. The results showed that C. porosus TTR with Zn 2+ -binding motif sequence of human TTR (hu-motif/crocTTR) has apparent K m (K app m ) of 118 ± 13 µM which was significantly higher than those for human TTR (53.6 ± 1.5 µM), C. porosus TTR (crocTTR) (30.2 ± 4.0 µM), and human TTR with Zn 2+ -binding motif sequence of C. porosus TTR (croc-motif/huTTR) (53.4 ± 0.87 µM). In addition, the catalytic efficiency (V max /K app m ) of croc-motif/huTTR (1.16 ± 0.0066 RFU min −1 µM −1 ) was significantly higher than human TTR (0.639 ± 0.0085 RFU min −1 µM −1 ) but similar to those of crocTTR (1.11 ± 0.082 M −1 min −1 ) and hu-motif/crocTTR (0.894 ± 0.031 RFU min −1 µM −1 ). The obtained results provided insight of the influence of the Zn 2+ -binding motif sequence and the evolutionary change structure on the proteolytic activity towards Aβ of TTR and useful information for designing a therapeutic TTR.

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“…The SDS-PAGE was performed under reducing condition according to previous study ( Tangthavewattana et al, 2019 ), and immunoblotting was performed as described previously ( Kawahara et al, 2011 ). Samples were boiled with sodium dodecyl sulfate sample buffer, denatured on 13% polyacrylamide gels, transferred onto a nitrocellulose membrane, and blocked in 4% skim milk in TBS-T (0.5% Triton-X 100 with TBS) for 30 min at room temperature then washed with TBS-T three times.…”

Section: Methodsmentioning

confidence: 99%

Extracellular Vesicles Contribute to the Metabolism of Transthyretin Amyloid in Hereditary Transthyretin Amyloidosis

Yamaguchi

Kawahara

Kodera

et al. 2022

Front. Mol. Biosci.

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Hereditary (variant) transthyretin amyloidosis (ATTRv amyloidosis), which is caused by variants in the transthyretin (TTR) gene, leads to TTR amyloid deposits in multiple organs and various symptoms such as limb ataxia, muscle weakness, and cardiac failure. Interaction between amyloid proteins and extracellular vesicles (EVs), which are secreted by various cells, is known to promote the clearance of the proteins, but it is unclear whether EVs are involved in the formation and deposition of TTR amyloid in ATTRv amyloidosis. To clarify the relationship between ATTRv amyloidosis and EVs, serum-derived EVs were analyzed. In this study, we showed that cell-derived EVs are involved in the formation of TTR amyloid deposits on the membrane of small EVs, as well as the deposition of TTR amyloid in cells. Human serum-derived small EVs also altered the degree of aggregation and deposition of TTR. Furthermore, the amount of TTR aggregates in serum-derived small EVs in patients with ATTRv amyloidosis was lower than that in healthy controls. These results indicate that EVs contribute to the metabolism of TTR amyloid, and suggest that TTR in serum-derived small EVs is a potential target for future ATTRv amyloidosis diagnosis and therapy.

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The hydrophobic C‐terminal sequence of transthyretin affects its catalytic kinetics towards amidated neuropeptide Y

Cited by 5 publications

References 69 publications

Faecal proteome in clinically healthy dogs and cats: Findings in pooled faeces from 10 cats and 10 dogs

Faecal proteome in clinically healthy dogs and cats: Findings in pooled faeces from 10 cats and 10 dogs

The influence of Zn2+-binding motif sequence on the catalytic activity of transthyretin towards amyloid beta

Extracellular Vesicles Contribute to the Metabolism of Transthyretin Amyloid in Hereditary Transthyretin Amyloidosis

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