A 'turn-on' fluorescent probe for lysosomal phosphatase: A comparative study for labeling of cancer cells

Arup Podder; Sudipta Senapati; Pralay Maiti; Devaraj Kamalraj; Syed S. Jaffer; Sabina Khatun; Sankarprasad Bhuniya

doi:10.1039/c8tb01143e

A 'turn-on' fluorescent probe for lysosomal phosphatase: A comparative study for labeling of cancer cells

Arup Podder, Sudipta Senapati, Pralay Maiti, Devaraj Kamalraj, Syed S. Jaffer, Sabina Khatun, Sankarprasad Bhuniya

Research output: Contribution to journal › Article › peer-review

21 Scopus citations

Abstract

We have described the ability of a newly synthesized fluorescent probe (LP1) to detect phosphatase activity in lysosomes in cancer cells. Probe LP1 displayed a 33-fold fluorescence intensity enhancement at λ_em 532 nm in the presence of phosphatase in HEPES buffer (pH 4.5). The quantum yield of probe LP1 was increased by ∼21-fold upon exposure to phosphatase at acidic pH. The probe LP1 is highly chemoselective toward phosphatase (ALP/ACP) and is insensitive to interference by ubiquitous biological analytes. The high cell adhesion property and cell viability of LP1 indicate that LP1 is biocompatible and nontoxic; these two characteristic features make it a suitable candidate for phosphatase tracking in living cells. LP1 dose-dependent fluorescence images in living cells suggested that the expression of phosphatase in cancer cells (HeLa) is 2-fold higher as compared to the normal NIH-3T3 cells. The colocalization images confirmed that LP1 was exclusively localized in lysosomes. We envision that LP1 could be a potential tool in clinical diagnosis for discriminating cancer cells from normal cells depending on the expression of phosphatase in lysosomes.

Original language	English
Pages (from-to)	4514-4521
Number of pages	8
Journal	Journal of Materials Chemistry B
Volume	6
Issue number	27
DOIs	https://doi.org/10.1039/c8tb01143e
State	Published - 21 Jul 2018
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2018 The Royal Society of Chemistry.

Funding

SB gratefully acknowledges DST-SERB, India for a research grant (ECR/2015/000035). DK and SSJ acknowledge the Department of Science and Technology – Science and Engineering Research Board (DST-SERB) New Delhi, India for the financial support by offering Young Scientist Scheme (YSS) (YSS/2015/ 000377). SSJ is grateful to the Department of Chemistry, Coim-batore Institute of Technology (CIT) for their financial assistance for computational facility and Gaussian-16 software package. We also gratefully acknowledge KKM and his team at NIIST, Trivandrum, India for providing cell images.

Funders	Funder number
Coim-batore Institute of Technology
DST-SERB	ECR/2015/000035
Science and Engineering Research Board	YSS/2015/ 000377
Department of Science and Technology, Government of Kerala

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abstract = "We have described the ability of a newly synthesized fluorescent probe (LP1) to detect phosphatase activity in lysosomes in cancer cells. Probe LP1 displayed a 33-fold fluorescence intensity enhancement at λem 532 nm in the presence of phosphatase in HEPES buffer (pH 4.5). The quantum yield of probe LP1 was increased by ∼21-fold upon exposure to phosphatase at acidic pH. The probe LP1 is highly chemoselective toward phosphatase (ALP/ACP) and is insensitive to interference by ubiquitous biological analytes. The high cell adhesion property and cell viability of LP1 indicate that LP1 is biocompatible and nontoxic; these two characteristic features make it a suitable candidate for phosphatase tracking in living cells. LP1 dose-dependent fluorescence images in living cells suggested that the expression of phosphatase in cancer cells (HeLa) is 2-fold higher as compared to the normal NIH-3T3 cells. The colocalization images confirmed that LP1 was exclusively localized in lysosomes. We envision that LP1 could be a potential tool in clinical diagnosis for discriminating cancer cells from normal cells depending on the expression of phosphatase in lysosomes.",

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A 'turn-on' fluorescent probe for lysosomal phosphatase: A comparative study for labeling of cancer cells

Abstract

Bibliographical note

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