Phenoloxidase-dependent cytotoxic mechanism in ascidian (Styela plicata) hemocytes active against erythrocytes and K562 tumor cells

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Abstract

The cytotoxic activity against rabbit erythrocytes (RE) and human K562 tumor cells by Styela plicata hemocytes was significantly related to the phenoloxidase (PO) which converts phenols to quinone and initiates the melanogenic pathway. The effector hemocyte population, separated in a Percoll density gradient band, enriched in a granulocyte type named "morula cells", was examined with RE in a hemocyte cytotoxic assay and plaque forming cell assay. Inhibition experiments with the copper chelating agents 1-phenyl-2-thiourea and tropolone, the substrate analogue sodium benzoate and sodium ascorbate support the notion that hemocyte cytotoxic activity is a PO-dependent mechanism. Treatments of hemocytes with the antioxidant enzymes, superoxide dismutase and catalase rule out oxy radicals produced by the melanogenic process as responsible of erythrolysis. Such a result suggests that quinone compounds derived from the melanogenic pathway might be the cytotoxic molecules. The PO-dependent anti-RE activity was also shown in a plaque forming assay in which "morula cells", containing polyphenols and PO, were identified as cytotoxic.
Lingua originaleEnglish
pagine (da-a)302-7-
Numero di pagine6
RivistaEuropean Journal of Cell Biology
Volume74
Stato di pubblicazionePublished - 1997

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Hemocytes
Urochordata
K562 Cells
Monophenol Monooxygenase
Erythrocytes
Morula
Neoplasms
Rabbits
Tropolone
Phenylthiourea
Sodium Benzoate
Phenols
Polyphenols
Chelating Agents
Granulocytes
Catalase
Ascorbic Acid
Superoxide Dismutase
Copper
Antioxidants

All Science Journal Classification (ASJC) codes

  • Pathology and Forensic Medicine
  • Cell Biology
  • Histology

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title = "Phenoloxidase-dependent cytotoxic mechanism in ascidian (Styela plicata) hemocytes active against erythrocytes and K562 tumor cells",
abstract = "The cytotoxic activity against rabbit erythrocytes (RE) and human K562 tumor cells by Styela plicata hemocytes was significantly related to the phenoloxidase (PO) which converts phenols to quinone and initiates the melanogenic pathway. The effector hemocyte population, separated in a Percoll density gradient band, enriched in a granulocyte type named {"}morula cells{"}, was examined with RE in a hemocyte cytotoxic assay and plaque forming cell assay. Inhibition experiments with the copper chelating agents 1-phenyl-2-thiourea and tropolone, the substrate analogue sodium benzoate and sodium ascorbate support the notion that hemocyte cytotoxic activity is a PO-dependent mechanism. Treatments of hemocytes with the antioxidant enzymes, superoxide dismutase and catalase rule out oxy radicals produced by the melanogenic process as responsible of erythrolysis. Such a result suggests that quinone compounds derived from the melanogenic pathway might be the cytotoxic molecules. The PO-dependent anti-RE activity was also shown in a plaque forming assay in which {"}morula cells{"}, containing polyphenols and PO, were identified as cytotoxic.",
keywords = "Cytotoxicity;, Erythrocytes;, Hemocytes;, K562;, Phenoloxidase;, Quinones;, Tunicate",
author = "Nicolo' Parrinello and Giuseppina Candore and Vincenzo Arizza",
year = "1997",
language = "English",
volume = "74",
pages = "302--7--",
journal = "European Journal of Cell Biology",
issn = "0171-9335",
publisher = "Urban und Fischer Verlag GmbH und Co. KG",

}

TY - JOUR

T1 - Phenoloxidase-dependent cytotoxic mechanism in ascidian (Styela plicata) hemocytes active against erythrocytes and K562 tumor cells

AU - Parrinello, Nicolo'

AU - Candore, Giuseppina

AU - Arizza, Vincenzo

PY - 1997

Y1 - 1997

N2 - The cytotoxic activity against rabbit erythrocytes (RE) and human K562 tumor cells by Styela plicata hemocytes was significantly related to the phenoloxidase (PO) which converts phenols to quinone and initiates the melanogenic pathway. The effector hemocyte population, separated in a Percoll density gradient band, enriched in a granulocyte type named "morula cells", was examined with RE in a hemocyte cytotoxic assay and plaque forming cell assay. Inhibition experiments with the copper chelating agents 1-phenyl-2-thiourea and tropolone, the substrate analogue sodium benzoate and sodium ascorbate support the notion that hemocyte cytotoxic activity is a PO-dependent mechanism. Treatments of hemocytes with the antioxidant enzymes, superoxide dismutase and catalase rule out oxy radicals produced by the melanogenic process as responsible of erythrolysis. Such a result suggests that quinone compounds derived from the melanogenic pathway might be the cytotoxic molecules. The PO-dependent anti-RE activity was also shown in a plaque forming assay in which "morula cells", containing polyphenols and PO, were identified as cytotoxic.

AB - The cytotoxic activity against rabbit erythrocytes (RE) and human K562 tumor cells by Styela plicata hemocytes was significantly related to the phenoloxidase (PO) which converts phenols to quinone and initiates the melanogenic pathway. The effector hemocyte population, separated in a Percoll density gradient band, enriched in a granulocyte type named "morula cells", was examined with RE in a hemocyte cytotoxic assay and plaque forming cell assay. Inhibition experiments with the copper chelating agents 1-phenyl-2-thiourea and tropolone, the substrate analogue sodium benzoate and sodium ascorbate support the notion that hemocyte cytotoxic activity is a PO-dependent mechanism. Treatments of hemocytes with the antioxidant enzymes, superoxide dismutase and catalase rule out oxy radicals produced by the melanogenic process as responsible of erythrolysis. Such a result suggests that quinone compounds derived from the melanogenic pathway might be the cytotoxic molecules. The PO-dependent anti-RE activity was also shown in a plaque forming assay in which "morula cells", containing polyphenols and PO, were identified as cytotoxic.

KW - Cytotoxicity;

KW - Erythrocytes;

KW - Hemocytes;

KW - K562;

KW - Phenoloxidase;

KW - Quinones;

KW - Tunicate

UR - http://hdl.handle.net/10447/146419

M3 - Article

VL - 74

SP - 302-7-

JO - European Journal of Cell Biology

JF - European Journal of Cell Biology

SN - 0171-9335

ER -