Glycosylated and non-glycosylated quantum dot-displayed peptides trafficked indiscriminately inside lung cancer cells but discriminately sorted in normal lung cells: An indispensable part in nanoparticle-based intracellular drug delivery

Difference in sub-cellular trafficking of glycosylated and naked peptides, between normal and lung cancer cells, was established. Normal lung tissue discriminately sorted glycosylated from non-glycosylated peptides by allowing golgi localization of the glycosylated peptides while restricting golgi e...

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Main Author: Tan, Roger Salvacion
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Published: Animo Repository 2018
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Online Access:https://animorepository.dlsu.edu.ph/faculty_research/3395
https://animorepository.dlsu.edu.ph/context/faculty_research/article/4397/type/native/viewcontent/j.ajps.2017.12.002
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spelling oai:animorepository.dlsu.edu.ph:faculty_research-43972021-09-07T05:54:26Z Glycosylated and non-glycosylated quantum dot-displayed peptides trafficked indiscriminately inside lung cancer cells but discriminately sorted in normal lung cells: An indispensable part in nanoparticle-based intracellular drug delivery Tan, Roger Salvacion Difference in sub-cellular trafficking of glycosylated and naked peptides, between normal and lung cancer cells, was established. Normal lung tissue discriminately sorted glycosylated from non-glycosylated peptides by allowing golgi localization of the glycosylated peptides while restricting golgi entry of the naked peptides. This mechanism was surprisingly not observed in its cancer cell counterpart. Lung cancer cells tend to allow unrestricted localization of both glycosylated and naked peptides in the golgi apparatus. This newly discovered difference in sub-cellular trafficking between normal and lung cancer cells could potentially be used as an effective strategy in targeted intracellular delivery, especially targeting golgi-resident enzymes for possible treatment of diseases associated with glycans and glycoproteins, such as, congenital disease of glycosylation (CDG). This very important detail in intracellular trafficking inside normal and cancer cells is an indispensable part in nanoparticle-based intracellular drug delivery. © 2018 Shenyang Pharmaceutical University 2018-05-01T07:00:00Z text text/html https://animorepository.dlsu.edu.ph/faculty_research/3395 info:doi/10.1016/j.ajps.2017.12.002 https://animorepository.dlsu.edu.ph/context/faculty_research/article/4397/type/native/viewcontent/j.ajps.2017.12.002 Faculty Research Work Animo Repository Peptides Glycopeptides Golgi apparatus Lungs Cancer cells Lungs—Cancer Quantum dots Chemistry
institution De La Salle University
building De La Salle University Library
continent Asia
country Philippines
Philippines
content_provider De La Salle University Library
collection DLSU Institutional Repository
topic Peptides
Glycopeptides
Golgi apparatus
Lungs
Cancer cells
Lungs—Cancer
Quantum dots
Chemistry
spellingShingle Peptides
Glycopeptides
Golgi apparatus
Lungs
Cancer cells
Lungs—Cancer
Quantum dots
Chemistry
Tan, Roger Salvacion
Glycosylated and non-glycosylated quantum dot-displayed peptides trafficked indiscriminately inside lung cancer cells but discriminately sorted in normal lung cells: An indispensable part in nanoparticle-based intracellular drug delivery
description Difference in sub-cellular trafficking of glycosylated and naked peptides, between normal and lung cancer cells, was established. Normal lung tissue discriminately sorted glycosylated from non-glycosylated peptides by allowing golgi localization of the glycosylated peptides while restricting golgi entry of the naked peptides. This mechanism was surprisingly not observed in its cancer cell counterpart. Lung cancer cells tend to allow unrestricted localization of both glycosylated and naked peptides in the golgi apparatus. This newly discovered difference in sub-cellular trafficking between normal and lung cancer cells could potentially be used as an effective strategy in targeted intracellular delivery, especially targeting golgi-resident enzymes for possible treatment of diseases associated with glycans and glycoproteins, such as, congenital disease of glycosylation (CDG). This very important detail in intracellular trafficking inside normal and cancer cells is an indispensable part in nanoparticle-based intracellular drug delivery. © 2018 Shenyang Pharmaceutical University
format text
author Tan, Roger Salvacion
author_facet Tan, Roger Salvacion
author_sort Tan, Roger Salvacion
title Glycosylated and non-glycosylated quantum dot-displayed peptides trafficked indiscriminately inside lung cancer cells but discriminately sorted in normal lung cells: An indispensable part in nanoparticle-based intracellular drug delivery
title_short Glycosylated and non-glycosylated quantum dot-displayed peptides trafficked indiscriminately inside lung cancer cells but discriminately sorted in normal lung cells: An indispensable part in nanoparticle-based intracellular drug delivery
title_full Glycosylated and non-glycosylated quantum dot-displayed peptides trafficked indiscriminately inside lung cancer cells but discriminately sorted in normal lung cells: An indispensable part in nanoparticle-based intracellular drug delivery
title_fullStr Glycosylated and non-glycosylated quantum dot-displayed peptides trafficked indiscriminately inside lung cancer cells but discriminately sorted in normal lung cells: An indispensable part in nanoparticle-based intracellular drug delivery
title_full_unstemmed Glycosylated and non-glycosylated quantum dot-displayed peptides trafficked indiscriminately inside lung cancer cells but discriminately sorted in normal lung cells: An indispensable part in nanoparticle-based intracellular drug delivery
title_sort glycosylated and non-glycosylated quantum dot-displayed peptides trafficked indiscriminately inside lung cancer cells but discriminately sorted in normal lung cells: an indispensable part in nanoparticle-based intracellular drug delivery
publisher Animo Repository
publishDate 2018
url https://animorepository.dlsu.edu.ph/faculty_research/3395
https://animorepository.dlsu.edu.ph/context/faculty_research/article/4397/type/native/viewcontent/j.ajps.2017.12.002
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