Protein-carbohydrate complex reveals circulating metastatic cells in a microfluidic assay

Giuseppina Simone; Natalia Maria Malara; Valentina Trunzo; Gerardo Perozziello; Pavel Neužil; Marco Francardi; Laura Roveda; Maria Renne; Ubaldo Prati; Vincenzo Mollace; Andreas Manz; Enzo M. Di Fabrizio

doi:10.1002/smll.201202867

Protein-carbohydrate complex reveals circulating metastatic cells in a microfluidic assay

Giuseppina Simone, Natalia Maria Malara, Valentina Trunzo, Gerardo Perozziello, Pavel Neužil, Marco Francardi, Laura Roveda, Maria Renne, Ubaldo Prati, Vincenzo Mollace, Andreas Manz, Enzo M. Di Fabrizio

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

31 Scopus citations

Abstract

Advances in carbohydrate sequencing technologies reveal the tremendous complexity of the glycome and the role that glycomics might have to bring insight into the biological functions. Carbohydrate-protein interactions, in particular, are known to be crucial to most mammalian physiological processes as mediators of cell adhesion and metastasis, signal transducers, and organizers of protein interactions. An assay is developed here to mimic the multivalency of biological complexes that selectively and sensitively detect carbohydrate-protein interactions. The binding of β-galactosides and galectin-3 - a protein that is correlated to the progress of tumor and metastasis - is examined. The efficiency of the assay is related to the expression of the receptor while anchoring to the interaction's strength. Comparative binding experiments reveal molecular binding preferences. This study establishes that the assay is robust to isolate metastatic cells from colon affected patients and paves the way to personalized medicine. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Original language	English (US)
Pages (from-to)	2152-2161
Number of pages	10
Journal	Small
Volume	9
Issue number	12
DOIs	https://doi.org/10.1002/smll.201202867
State	Published - Feb 11 2013

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: This work was partially supported by the project PON "Nuove strategie nanotecnologiche per la messa a punto di farmaci e presidi diagnostici diretti verso cellule cancerose circolanti." (cod. PON01_02782, CUP B71H11000870005), and the project FIRB "Rete Nazionale di Ricerca sulle Nanoscienze ItalNanoNet" (cod. RBPR05JH2P_010, CUP B41J09000110005) granted to the nanotechnology laboratory of the Department of Experimental Medicine of the University of Magna Graecia of Catanzaro, the foundation "T. Campanella" and RSA (ANASTE Calabria).

ASJC Scopus subject areas

General Medicine

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10.1002/smll.201202867

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title = "Protein-carbohydrate complex reveals circulating metastatic cells in a microfluidic assay",

abstract = "Advances in carbohydrate sequencing technologies reveal the tremendous complexity of the glycome and the role that glycomics might have to bring insight into the biological functions. Carbohydrate-protein interactions, in particular, are known to be crucial to most mammalian physiological processes as mediators of cell adhesion and metastasis, signal transducers, and organizers of protein interactions. An assay is developed here to mimic the multivalency of biological complexes that selectively and sensitively detect carbohydrate-protein interactions. The binding of β-galactosides and galectin-3 - a protein that is correlated to the progress of tumor and metastasis - is examined. The efficiency of the assay is related to the expression of the receptor while anchoring to the interaction's strength. Comparative binding experiments reveal molecular binding preferences. This study establishes that the assay is robust to isolate metastatic cells from colon affected patients and paves the way to personalized medicine. Copyright {\textcopyright} 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

author = "Giuseppina Simone and Malara, {Natalia Maria} and Valentina Trunzo and Gerardo Perozziello and Pavel Neu{\v z}il and Marco Francardi and Laura Roveda and Maria Renne and Ubaldo Prati and Vincenzo Mollace and Andreas Manz and {Di Fabrizio}, {Enzo M.}",

note = "KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: This work was partially supported by the project PON {"}Nuove strategie nanotecnologiche per la messa a punto di farmaci e presidi diagnostici diretti verso cellule cancerose circolanti.{"} (cod. PON01_02782, CUP B71H11000870005), and the project FIRB {"}Rete Nazionale di Ricerca sulle Nanoscienze ItalNanoNet{"} (cod. RBPR05JH2P_010, CUP B41J09000110005) granted to the nanotechnology laboratory of the Department of Experimental Medicine of the University of Magna Graecia of Catanzaro, the foundation {"}T. Campanella{"} and RSA (ANASTE Calabria).",

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doi = "10.1002/smll.201202867",

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AU - Simone, Giuseppina

AU - Malara, Natalia Maria

AU - Trunzo, Valentina

AU - Perozziello, Gerardo

AU - Neužil, Pavel

AU - Francardi, Marco

AU - Roveda, Laura

AU - Renne, Maria

AU - Prati, Ubaldo

AU - Mollace, Vincenzo

AU - Manz, Andreas

AU - Di Fabrizio, Enzo M.

N1 - KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: This work was partially supported by the project PON "Nuove strategie nanotecnologiche per la messa a punto di farmaci e presidi diagnostici diretti verso cellule cancerose circolanti." (cod. PON01_02782, CUP B71H11000870005), and the project FIRB "Rete Nazionale di Ricerca sulle Nanoscienze ItalNanoNet" (cod. RBPR05JH2P_010, CUP B41J09000110005) granted to the nanotechnology laboratory of the Department of Experimental Medicine of the University of Magna Graecia of Catanzaro, the foundation "T. Campanella" and RSA (ANASTE Calabria).

PY - 2013/2/11

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N2 - Advances in carbohydrate sequencing technologies reveal the tremendous complexity of the glycome and the role that glycomics might have to bring insight into the biological functions. Carbohydrate-protein interactions, in particular, are known to be crucial to most mammalian physiological processes as mediators of cell adhesion and metastasis, signal transducers, and organizers of protein interactions. An assay is developed here to mimic the multivalency of biological complexes that selectively and sensitively detect carbohydrate-protein interactions. The binding of β-galactosides and galectin-3 - a protein that is correlated to the progress of tumor and metastasis - is examined. The efficiency of the assay is related to the expression of the receptor while anchoring to the interaction's strength. Comparative binding experiments reveal molecular binding preferences. This study establishes that the assay is robust to isolate metastatic cells from colon affected patients and paves the way to personalized medicine. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

AB - Advances in carbohydrate sequencing technologies reveal the tremendous complexity of the glycome and the role that glycomics might have to bring insight into the biological functions. Carbohydrate-protein interactions, in particular, are known to be crucial to most mammalian physiological processes as mediators of cell adhesion and metastasis, signal transducers, and organizers of protein interactions. An assay is developed here to mimic the multivalency of biological complexes that selectively and sensitively detect carbohydrate-protein interactions. The binding of β-galactosides and galectin-3 - a protein that is correlated to the progress of tumor and metastasis - is examined. The efficiency of the assay is related to the expression of the receptor while anchoring to the interaction's strength. Comparative binding experiments reveal molecular binding preferences. This study establishes that the assay is robust to isolate metastatic cells from colon affected patients and paves the way to personalized medicine. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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EP - 2161

JO - Small

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IS - 12

ER -

Protein-carbohydrate complex reveals circulating metastatic cells in a microfluidic assay

Abstract

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