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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Evaluating biochemical differences in thyroglobulin from normal and goiter tissues by infrared spectral imaging

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Author(s):
Pereira, Thiago Martini [1, 2] ; Diem, Max [3] ; Bachmann, Luciano [4] ; Bird, Benjamin [3, 5] ; Miljkovic, Milos [3, 6] ; Zezell, Denise Maria [2]
Total Authors: 6
Affiliation:
[1] Univ Fed Sao Paulo, Inst Ciencia & Tecnol, Rua Talim 330, BR-12231280 Sao Jose Dos Campos - Brazil
[2] Inst Pesquisas Energet & Nucl, Ctr Lasers & Aplicacoes, Ave Prof Lineu Prestes 2242, BR-05508000 Sao Paulo, SP - Brazil
[3] Northeastern Univ, Dept Chem & Chem Biol, Lab Spectral Diag LSpD, 360 Huntington Ave, Boston, MA 02115 - USA
[4] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Ave Bandeirantes 3900, BR-14040901 Ribeirao Preto - Brazil
[5] Daylight Solut, 15378 Ave Sci, Suite 200, San Diego, CA 92128 - USA
[6] Tufts Univ, Dept Mech Engn, 200 Boston Ave, Medford, MA 02155 - USA
Total Affiliations: 6
Document type: Journal article
Source: ANALYST; v. 145, n. 24, p. 7907-7915, DEC 21 2020.
Web of Science Citations: 0
Abstract

Thyroglobulin is a glycoiodoprotein that is produced by thyroid follicular cells; it is stored in follicles in structures known as colloids. The main function of this protein is to stock the hormones triiodothyronine (T3) and thyroxine (T4) until the body requires them. This study aims to demonstrate that infrared spectral imaging with appropriate multivariate analysis can reveal biochemical changes in this glycoprotein. The results achieved herein point out biochemical differences in the colloid samples obtained from normal and goiter patients including glycosylation and changes in the secondary conformational structure. We have presented the first spectral histopathology-based method to detect biochemical differences in thyroid colloids, such as TG iodination, glycosylation, and changes in the secondary structure in normal and goiter patients. The observed changes in the colloids were mainly due to the alterations in amide I and amide II (secondary conformation of proteins) and there is a correlation with different glycosylation between normal and goiter tissues. (AU)

FAPESP's process: 05/51689-2 - Optics and Photonics Research Center at UNICAMP
Grantee:Hugo Luis Fragnito
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC