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A Study on Multiple Facets of Apolipoprotein A1 Milano.
Maarfi, Farah; Yusuf, Mohd Aslam; Ahmad, Mohammad Faizan Ali; Rehman, Shahnawaz; Aswal, Saloni; Dogra, Deepti; Singh, Ajay; Khan, Mohd Yasir.
Afiliación
  • Maarfi F; Department of Biotechnology, School of Applied and Life Science (SALS), Uttaranchal University, Dehradun, 248007, Uttarakhand, India.
  • Yusuf MA; Department of Biosciences, Integral University, Lucknow, 226026, India.
  • Ahmad MFA; Department of Biosciences, Integral University, Lucknow, 226026, India.
  • Rehman S; Department of Zoology, S.S. Faculty of Science, Mohammad Ali Jauhar University, Rampur, U. P, India.
  • Aswal S; Department of Biotechnology, School of Applied and Life Science (SALS), Uttaranchal University, Dehradun, 248007, Uttarakhand, India.
  • Dogra D; Department of Biotechnology, School of Applied and Life Science (SALS), Uttaranchal University, Dehradun, 248007, Uttarakhand, India.
  • Singh A; Department of Chemistry, School of Applied and Life Science (SALS), Uttaranchal University, Dehradun, 248007, Uttarakhand, India.
  • Khan MY; Department of Biotechnology, School of Applied and Life Science (SALS), Uttaranchal University, Dehradun, 248007, Uttarakhand, India. khanyasir707@gmail.com.
Appl Biochem Biotechnol ; 195(7): 4653-4672, 2023 Jul.
Article en En | MEDLINE | ID: mdl-36689166
For several strategies formulated to prevent atherosclerosis, Apolipoprotein A1 Milano (ApoA1M) remains a prime target. ApoA1M has been reported to have greater efficiency in reducing the incidence of coronary artery diseases. Furthermore, recombinant ApoA1M based mimetic peptide exhibits comparatively greater atheroprotective potential, offers a hope in reducing the burden of atherosclerosis in in vivo model system. The aim of this review is to emphasize on some of the observed ApoA1M structural and functional effects that are clinically and therapeutically meaningful that might converge on the basic role of ApoA1M in reducing the chances of glycation assisted ailments in diabetes. We also hypothesize that the nonenzymatic glycation prone arginine amino acid of ApoA1 gets replaced with cysteine residue and the rate of ApoA1 glycation may decrease due to change substitution of amino acid. Therefore, to circumvent the effect of ApoA1M glycation, the related mechanism should be explored at the cellular and functional levels, especially in respective experimental disease model in vivo.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Enfermedad de la Arteria Coronaria / Aterosclerosis Límite: Humans Idioma: En Revista: Appl Biochem Biotechnol Año: 2023 Tipo del documento: Article País de afiliación: India

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Enfermedad de la Arteria Coronaria / Aterosclerosis Límite: Humans Idioma: En Revista: Appl Biochem Biotechnol Año: 2023 Tipo del documento: Article País de afiliación: India