Loss of adhesion impairs invasiveness and cell survival, contributing to the antimetastatic effect of cysteine proteases from Vasconcella cundinamarcensis in melanoma

Abstract Based on available evidence showing the antitumoral/antimetastatic activity of the proteolytic fraction (P1G10) from Vasconcellea cundinamarcensis, we analyze possible mechanisms involved in the antimetastasic effect of this fraction and subfractions (CMS1, CMS2) after incubation with B16F1...

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Main Authors: Dalton Dittz, Isabela Paula Nunes, Hortência Maciel de Castro Oliveira, Gustavo Batista de Menezes, Carlos Edmundo Salas Bravo, Miriam Teresa Paz Lopes
Format: Article
Language:English
Published: Nature Portfolio 2025-07-01
Series:Scientific Reports
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Online Access:https://doi.org/10.1038/s41598-024-73489-3
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author Dalton Dittz
Isabela Paula Nunes
Hortência Maciel de Castro Oliveira
Gustavo Batista de Menezes
Carlos Edmundo Salas Bravo
Miriam Teresa Paz Lopes
author_facet Dalton Dittz
Isabela Paula Nunes
Hortência Maciel de Castro Oliveira
Gustavo Batista de Menezes
Carlos Edmundo Salas Bravo
Miriam Teresa Paz Lopes
author_sort Dalton Dittz
collection DOAJ
description Abstract Based on available evidence showing the antitumoral/antimetastatic activity of the proteolytic fraction (P1G10) from Vasconcellea cundinamarcensis, we analyze possible mechanisms involved in the antimetastasic effect of this fraction and subfractions (CMS1, CMS2) after incubation with B16F10 melanoma cells in vitro and in vivo under sub-apoptotic conditions. The goal was to investigate potential mediators of the antitumoral/antimetastatic effect of P1G10 triggered before the onset of apoptosis. In B16F10 preincubated viable cells, it was observed changes in adhesion to ECM (extracellular matrix), reduced activity of metalloproteases and invasivity, reduction of pAkt and pErk mostly affecting the rate of lung metastasis in mice injected with B16F10 treated cells. In most of these assays the effects depend of the proteolytic activity of the fractions. Unexpectedly, the CMS2-IAA (CMS2 with proteolytically activity inhibited by iodoacetamide), enhanced pErk phosphorylation and increased procaspase-3 levels. The invasivity of B16F10 was impaired following incubation with the proteolytic fraction without affecting cell viability under the conditions analyzed. In conclusion, CMS2 reduces in vitro cell invasion and metastasis in murine melanoma B16F10.
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spelling doaj-art-7599e18a1988491fbc164c607cbb048b2025-08-20T03:45:28ZengNature PortfolioScientific Reports2045-23222025-07-0115111510.1038/s41598-024-73489-3Loss of adhesion impairs invasiveness and cell survival, contributing to the antimetastatic effect of cysteine proteases from Vasconcella cundinamarcensis in melanomaDalton Dittz0Isabela Paula Nunes1Hortência Maciel de Castro Oliveira2Gustavo Batista de Menezes3Carlos Edmundo Salas Bravo4Miriam Teresa Paz Lopes5Department of Biochemistry and Pharmacology, Federal University of PiauíDepartment of Pharmacology, Federal University of Minas GeraisDepartment of Morphology, Federal University of Minas GeraisDepartment of Morphology, Federal University of Minas GeraisDepartmente of Biochemistry and Immunology, Federal University of Minas GeraisDepartment of Pharmacology, Federal University of Minas GeraisAbstract Based on available evidence showing the antitumoral/antimetastatic activity of the proteolytic fraction (P1G10) from Vasconcellea cundinamarcensis, we analyze possible mechanisms involved in the antimetastasic effect of this fraction and subfractions (CMS1, CMS2) after incubation with B16F10 melanoma cells in vitro and in vivo under sub-apoptotic conditions. The goal was to investigate potential mediators of the antitumoral/antimetastatic effect of P1G10 triggered before the onset of apoptosis. In B16F10 preincubated viable cells, it was observed changes in adhesion to ECM (extracellular matrix), reduced activity of metalloproteases and invasivity, reduction of pAkt and pErk mostly affecting the rate of lung metastasis in mice injected with B16F10 treated cells. In most of these assays the effects depend of the proteolytic activity of the fractions. Unexpectedly, the CMS2-IAA (CMS2 with proteolytically activity inhibited by iodoacetamide), enhanced pErk phosphorylation and increased procaspase-3 levels. The invasivity of B16F10 was impaired following incubation with the proteolytic fraction without affecting cell viability under the conditions analyzed. In conclusion, CMS2 reduces in vitro cell invasion and metastasis in murine melanoma B16F10.https://doi.org/10.1038/s41598-024-73489-3MetastasisMelanomaCell adhesionCell invasionCysteine proteases
spellingShingle Dalton Dittz
Isabela Paula Nunes
Hortência Maciel de Castro Oliveira
Gustavo Batista de Menezes
Carlos Edmundo Salas Bravo
Miriam Teresa Paz Lopes
Loss of adhesion impairs invasiveness and cell survival, contributing to the antimetastatic effect of cysteine proteases from Vasconcella cundinamarcensis in melanoma
Scientific Reports
Metastasis
Melanoma
Cell adhesion
Cell invasion
Cysteine proteases
title Loss of adhesion impairs invasiveness and cell survival, contributing to the antimetastatic effect of cysteine proteases from Vasconcella cundinamarcensis in melanoma
title_full Loss of adhesion impairs invasiveness and cell survival, contributing to the antimetastatic effect of cysteine proteases from Vasconcella cundinamarcensis in melanoma
title_fullStr Loss of adhesion impairs invasiveness and cell survival, contributing to the antimetastatic effect of cysteine proteases from Vasconcella cundinamarcensis in melanoma
title_full_unstemmed Loss of adhesion impairs invasiveness and cell survival, contributing to the antimetastatic effect of cysteine proteases from Vasconcella cundinamarcensis in melanoma
title_short Loss of adhesion impairs invasiveness and cell survival, contributing to the antimetastatic effect of cysteine proteases from Vasconcella cundinamarcensis in melanoma
title_sort loss of adhesion impairs invasiveness and cell survival contributing to the antimetastatic effect of cysteine proteases from vasconcella cundinamarcensis in melanoma
topic Metastasis
Melanoma
Cell adhesion
Cell invasion
Cysteine proteases
url https://doi.org/10.1038/s41598-024-73489-3
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