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Structural changes in hemoglobin and glycation.
Nascimento, Amanda Luise Alves; Guimarães, Ari Souza; Rocha, Tauane Dos Santos; Goulart, Marilia Oliveira Fonseca; Xavier, Jadriane de Almeida; Santos, Josué Carinhanha Caldas.
Afiliación
  • Nascimento ALA; Federal University of Alagoas, Institute of Chemistry and Biotechnology, Campus A. C. Simões, Maceió, Alagoas, Brazil.
  • Guimarães AS; Federal University of Alagoas, Institute of Chemistry and Biotechnology, Campus A. C. Simões, Maceió, Alagoas, Brazil.
  • Rocha TDS; Federal University of Alagoas, Institute of Chemistry and Biotechnology, Campus A. C. Simões, Maceió, Alagoas, Brazil.
  • Goulart MOF; Federal University of Alagoas, Institute of Chemistry and Biotechnology, Campus A. C. Simões, Maceió, Alagoas, Brazil.
  • Xavier JA; Federal University of Alagoas, Institute of Chemistry and Biotechnology, Campus A. C. Simões, Maceió, Alagoas, Brazil. Electronic address: jadrianexavier@iqb.ufal.br.
  • Santos JCC; Federal University of Alagoas, Institute of Chemistry and Biotechnology, Campus A. C. Simões, Maceió, Alagoas, Brazil. Electronic address: josue@iqb.ufal.br.
Vitam Horm ; 125: 183-229, 2024.
Article en En | MEDLINE | ID: mdl-38997164
ABSTRACT
Hemoglobin (Hb) is a hemeprotein found inside erythrocytes and is crucial in transporting oxygen and carbon dioxide in our bodies. In erythrocytes (Ery), the main energy source is glucose metabolized through glycolysis. However, a fraction of Hb can undergo glycation, in which a free amine group from the protein spontaneously binds to the carbonyl of glucose in the bloodstream, resulting in the formation of glycated hemoglobin (HbA1c), widely used as a marker for diabetes. Glycation leads to structural and conformational changes, compromising the function of proteins, and is intensified in the event of hyperglycemia. The main changes in Hb include structural alterations to the heme group, compromising its main function (oxygen transport). In addition, amyloid aggregates can form, which are strongly related to diabetic complications and neurodegenerative diseases. Therefore, this chapter discusses in vitro protocols for producing glycated Hb, as well as the main techniques and biophysical assays used to assess changes in the protein's structure before and after the glycation process. This more complete understanding of the effects of glycation on Hb is fundamental for understanding the complications associated with hyperglycemia and for developing more effective prevention and treatment strategies.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hemoglobinas Límite: Animals / Humans Idioma: En Revista: Vitam Horm Año: 2024 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hemoglobinas Límite: Animals / Humans Idioma: En Revista: Vitam Horm Año: 2024 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Estados Unidos