scholarly journals Thymosin β4 Regulates Focal Adhesion Formation in Human Melanoma Cells and Affects Their Migration and Invasion

2019 ◽  
Vol 7 ◽  
Author(s):  
Aleksandra Makowiecka ◽  
Natalia Malek ◽  
Ewa Mazurkiewicz ◽  
Ewa Mrówczyńska ◽  
Dorota Nowak ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Adhesion Formation ◽  
Melanoma Cells ◽  
Human Melanoma ◽  
Migration And Invasion ◽  
Thymosin Β4 ◽  
Human Melanoma Cells ◽  
Focal Adhesion Formation

scholarly journals Knockout of ACTB and ACTG1 with CRISPR/Cas9(D10A) Technique Shows that Non-Muscle β and γ Actin Are Not Equal in Relation to Human Melanoma Cells’ Motility and Focal Adhesion Formation

2020 ◽  
Vol 21 (8) ◽  
pp. 2746 ◽  
Author(s):  
Natalia Malek ◽  
Ewa Mrówczyńska ◽  
Aleksandra Michrowska ◽  
Ewa Mazurkiewicz ◽  
Iuliia Pavlyk ◽  
...  
Keyword(s):  
Formation Rate ◽  
Adhesion Formation ◽  
Focal Adhesions ◽  
Melanoma Cells ◽  
Human Melanoma ◽  
Migration And Invasion ◽  
Human Melanoma Cells ◽  
Cas9 Nuclease ◽  
Focal Adhesion Formation ◽  
Actin Isoform

Non-muscle actins have been studied for many decades; however, the reason for the existence of both isoforms is still unclear. Here we show, for the first time, a successful inactivation of the ACTB (CRISPR clones with inactivated ACTB, CR-ACTB) and ACTG1 (CRISPR clones with inactivated ACTG1, CR-ACTG1) genes in human melanoma cells (A375) via the RNA-guided D10A mutated Cas9 nuclease gene editing [CRISPR/Cas9(D10A)] technique. This approach allowed us to evaluate how melanoma cell motility was impacted by the lack of either β actin coded by ACTB or γ actin coded by ACTG1. First, we observed different distributions of β and γ actin in the cells, and the absence of one actin isoform was compensated for via increased expression of the other isoform. Moreover, we noted that γ actin knockout had more severe consequences on cell migration and invasion than β actin knockout. Next, we observed that the formation rate of bundled stress fibers in CR-ACTG1 cells was increased, but lamellipodial activity in these cells was impaired, compared to controls. Finally, we discovered that the formation rate of focal adhesions (FAs) and, subsequently, FA-dependent signaling were altered in both the CR-ACTB and CR-ACTG1 clones; however, a more detrimental effect was observed for γ actin-deficient cells. Our research shows that both non-muscle actins play distinctive roles in melanoma cells’ FA formation and motility.

scholarly journals The origin of the expressed retrotransposed gene ACTBL2 and its influence on human melanoma cells’ motility and focal adhesion formation

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Natalia Malek ◽  
Aleksandra Michrowska ◽  
Ewa Mazurkiewicz ◽  
Ewa Mrówczyńska ◽  
Paweł Mackiewicz ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Actin Polymerization ◽  
Adhesion Formation ◽  
Melanoma Cells ◽  
Human Melanoma ◽  
Small Subset ◽  
Human Melanoma Cells ◽  
Focal Adhesion Formation ◽  
Actin Isoform ◽  
Melanoma Cell Lines

AbstractWe have recently found that β-actin-like protein 2 (actbl2) forms complexes with gelsolin in human melanoma cells and can polymerize. Phylogenetic and bioinformatic analyses showed that actbl2 has a common origin with two non-muscle actins, which share a separate history from the muscle actins. The actin groups’ divergence started at the beginning of vertebrate evolution, and actbl2 actins are characterized by the largest number of non-conserved amino acid substitutions of all actins. We also discovered that ACTBL2 is expressed at a very low level in several melanoma cell lines, but a small subset of cells exhibited a high ACTBL2 expression. We found that clones with knocked-out ACTBL2 (CR-ACTBL2) or overexpressing actbl2 (OE-ACTBL2) differ from control cells in the invasion, focal adhesion formation, and actin polymerization ratio, as well as in the formation of lamellipodia and stress fibers. Thus, we postulate that actbl2 is the seventh actin isoform and is essential for cell motility.

scholarly journals CREPT Promotes Melanoma Progression Through Accelerated Proliferation and Enhanced Migration by RhoA-Mediated Actin Filaments and Focal Adhesion Formation

Cancers ◽  
2019 ◽  
Vol 12 (1) ◽  
pp. 33 ◽  
Author(s):  
Hui Liu ◽  
Ann L. B. Seynhaeve ◽  
Rutger W. W. Brouwer ◽  
Wilfred F. J. van IJcken ◽  
Liu Yang ◽  
...  
Keyword(s):  
Focal Adhesion ◽  
Adhesion Formation ◽  
Distant Metastases ◽  
Melanoma Cells ◽  
Migration And Invasion ◽  
Actin Organization ◽  
Melanoma Progression ◽  
Elevated Protein ◽  
Focal Adhesion Formation ◽  
Accelerated Proliferation

Melanoma is one of the most aggressive cancers, and patients with distant metastases have dire outcomes. We observed previously that melanoma progression is driven by a high migratory potential of melanoma cells, which survive and proliferate under harsh environmental conditions. In this study, we report that CREPT (cell-cycle related and expression-elevated protein in tumor), an oncoprotein highly expressed in other cancers, is overexpressed in melanoma cells but not melanocytes. Overexpression of CREPT stimulates cell proliferation, migration, and invasion in several melanoma cell lines. Further, we show that CREPT enhances melanoma progression through upregulating and activating Ras homolog family member A (RhoA)-induced actin organization and focal adhesion assembly. Our study reveals a novel role of CREPT in promoting melanoma progression. Targeting CREPT may be a promising strategy for melanoma treatment.

scholarly journals Inhibition of Src Family Kinases with Dasatinib Blocks Migration and Invasion of Human Melanoma Cells

2008 ◽  
Vol 6 (11) ◽  
pp. 1766-1774 ◽  
Author(s):  
Ralf Buettner ◽  
Tania Mesa ◽  
Adina Vultur ◽  
Frank Lee ◽  
Richard Jove
Keyword(s):  
Melanoma Cells ◽  
Human Melanoma ◽  
Src Family Kinases ◽  
Migration And Invasion ◽  
Human Melanoma Cells

Geraniin-mediated apoptosis by cleavage of focal adhesion kinase through up-regulation of Fas ligand expression in human melanoma cells

2008 ◽  
Vol 52 (6) ◽  
pp. 655-663 ◽  
Author(s):  
Jang-Chang Lee ◽  
Chih-Yen Tsai ◽  
Jung-Yie Kao ◽  
Ming-Ching Kao ◽  
Shih-Chang Tsai ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Fas Ligand ◽  
Melanoma Cells ◽  
Human Melanoma ◽  
Human Melanoma Cells ◽  
Ligand Expression

scholarly journals Triptolide-Mediated Apoptosis by Suppression of Focal Adhesion Kinase through Extrinsic and Intrinsic Pathways in Human Melanoma Cells

2013 ◽  
Vol 2013 ◽  
pp. 1-10
Author(s):  
Haw-Young Kwon ◽  
Kyoung-Sook Kim ◽  
Ji-Sue Baik ◽  
Hyung-In Moon ◽  
Ji-Won Lee ◽  
...  
Keyword(s):  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Caspase 3 ◽  
Human Cancer ◽  
Melanoma Cells ◽  
Human Melanoma ◽  
Caspase 8 ◽  
Cytochrome C Release ◽  
Human Melanoma Cells ◽  
Induced Apoptosis

Triptolide (TPL) has been shown to inhibit cell proliferation and induce apoptosis in various human cancer cells; however, the precise mechanism of apoptosis induced by TPL in human melanoma cells has not yet been elucidated. In this study, we investigated the precise mechanism underlying cytocidal effects of TPL on human melanoma cells. Treatment of human melanoma cells with TPL significantly inhibited cell growth and induced apoptosis, as evidenced by flow cytometry and annexin V-fluorescein isothiocyanate analyses. TPL increased the levels of Fas and Fas-associated death domain (FADD) and induced cleavage of Bid by activation of caspase-8 and cytochrome c release from mitochondria to the cytosol, which resulted in activation of caspase-9 and caspase-3. Moreover, TPL-induced apoptosis in SK-MEL-2 cells was mediated through dephosphorylation of focal adhesion kinase (FAK) and its cleavage by caspase-8-mediated caspase-3 activation via upregulation of Fas expression. We also found that TPL mediated the dissociation of receptor-interacting protein (RIP) from FAK and enhanced the formation of RIP/Fas complex formation initiating cell death. In conclusion, our data firstly demonstrated that TPL induces apoptosis by both extrinsic and intrinsic apoptosis pathways in human melanoma cells and identified that RIP shuttles between Fas and FAK to mediate apoptosis.

Sign in / Sign up

Export Citation Format

Share Document