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Article ; Online: Targeting FAK in anticancer combination therapies.

Dawson, John C / Serrels, Alan / Stupack, Dwayne G / Schlaepfer, David D / Frame, Margaret C

2021 Volume 21, Issue 5, Page(s) 313–324

Abstract: Focal adhesion kinase (FAK) is both a non-receptor tyrosine kinase and an adaptor protein that primarily regulates adhesion signalling and cell migration, but FAK can also promote cell survival in response to stress. FAK is commonly overexpressed in ... ...

Abstract	Focal adhesion kinase (FAK) is both a non-receptor tyrosine kinase and an adaptor protein that primarily regulates adhesion signalling and cell migration, but FAK can also promote cell survival in response to stress. FAK is commonly overexpressed in cancer and is considered a high-value druggable target, with multiple FAK inhibitors currently in development. Evidence suggests that in the clinical setting, FAK targeting will be most effective in combination with other agents so as to reverse failure of chemotherapies or targeted therapies and enhance efficacy of immune-based treatments of solid tumours. Here, we discuss the recent preclinical evidence that implicates FAK in anticancer therapeutic resistance, leading to the view that FAK inhibitors will have their greatest utility as combination therapies in selected patient populations.
MeSH term(s)	Animals ; Antineoplastic Combined Chemotherapy Protocols ; Focal Adhesion Protein-Tyrosine Kinases/antagonists & inhibitors ; Humans ; Molecular Targeted Therapy ; Neoplasms/drug therapy ; Neoplasms/enzymology ; Neoplasms/pathology ; Protein Kinase Inhibitors/therapeutic use
Chemical Substances	Protein Kinase Inhibitors ; Focal Adhesion Protein-Tyrosine Kinases (EC 2.7.10.2)
Language	English
Publishing date	2021-03-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2062767-1
ISSN	1474-1768 ; 1474-175X
ISSN (online)	1474-1768
ISSN	1474-175X
DOI	10.1038/s41568-021-00340-6
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Zs.A 5563: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Underlying Subwavelength Aperture Architecture Drives the Optical Properties of Microcavity Surface Plasmon Resonance Sensors.

Amarie, Dragos / Mosavian, Nazanin / Waters, Elijah L / Stupack, Dwayne G

Sensors (Basel, Switzerland)

2020 Volume 20, Issue 17

Abstract: Microcavity surface plasmon resonance sensors (MSPRSs) develop out of the classic surface plasmon resonance technologies and aim at producing novel lab-on-a-chip devices. MSPRSs generate a series of spectral resonances sensitive to minute changes in the ... ...

Abstract	Microcavity surface plasmon resonance sensors (MSPRSs) develop out of the classic surface plasmon resonance technologies and aim at producing novel lab-on-a-chip devices. MSPRSs generate a series of spectral resonances sensitive to minute changes in the refractive index. Related sensitivity studies and biosensing applications are published elsewhere. The goal of this work is to test the hypothesis that MSPRS resonances are standing surface plasmon waves excited at the surface of the sensor that decay back into propagating photons. Their optical properties (mean wavelength, peak width, and peak intensity) appear highly dependent on the internal morphology of the sensor and the underlying subwavelength aperture architecture in particular. Numerous optical experiments were designed to investigate trends that confirm this hypothesis. An extensive study of prior works was supportive of our findings and interpretations. A complete understanding of those mechanisms and parameters driving the formations of the MSPRS resonances would allow further improvement in sensor sensitivity, reliability, and manufacturability.
Language	English
Publishing date	2020-08-30
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2052857-7
ISSN	1424-8220 ; 1424-8220
ISSN (online)	1424-8220
ISSN	1424-8220
DOI	10.3390/s20174906
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Article ; Online: Caspase-8 function, and phosphorylation, in cell migration.

Keller, Nadine / Ozmadenci, Duygu / Ichim, Gabriel / Stupack, Dwayne

Seminars in cell & developmental biology

2018 Volume 82, Page(s) 105–117

Abstract: Caspase-8 is involved in a number of cellular functions, with the most well established being the control of cell death. Yet caspase-8 is unique among the caspases in that it acts as an environmental sensor, transducing a range of signals to cells, ... ...

Abstract	Caspase-8 is involved in a number of cellular functions, with the most well established being the control of cell death. Yet caspase-8 is unique among the caspases in that it acts as an environmental sensor, transducing a range of signals to cells, modulating responses that extend far beyond simple survival. Ranging from the control of apoptosis and necroptosis and gene regulation to cell adhesion and migration, caspase-8 uses proteolytic and non-proteolytic functions to alter cell behavior. Novel interacting partners provide mechanisms for caspase-8 to position itself at signaling nodes that affect a variety of signaling pathways. Here, we examine the catalytic and noncatalytic modes of action by which caspase-8 influences cell adhesion and migration. The mechanisms vary from post-cleavage remodeling of the cytoskeleton to signaling elements that control focal adhesion turnover. This is facilitated by caspase-8 interaction with a host of cell proteins ranging from the proteases caspase-3 and calpain-2 to adaptor proteins such as p85 and Crk, to the Src family of tyrosine kinases.
MeSH term(s)	Animals ; Caspase 8/metabolism ; Cell Movement ; Humans ; Phosphorylation
Chemical Substances	Caspase 8 (EC 3.4.22.-)
Language	English
Publishing date	2018-02-17
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1312473-0
ISSN	1096-3634 ; 1084-9521
ISSN (online)	1096-3634
ISSN	1084-9521
DOI	10.1016/j.semcdb.2018.01.009
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Zs.A 2918: Show issues

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Article ; Online: Retraction for Nasimuzzaman et al., "Hepatitis C Virus Stabilizes Hypoxia-Inducible Factor 1α and Stimulates the Synthesis of Vascular Endothelial Growth Factor".

Nasimuzzaman, Md / Waris, Gulam / Mikolon, David / Stupack, Dwayne G / Siddiqui, Aleem

Journal of virology

2020 Volume 94, Issue 19

Language	English
Publishing date	2020-09-15
Publishing country	United States
Document type	Journal Article ; Retraction of Publication
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01403-20
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Article: Integrins as a distinct subtype of dependence receptors.

Stupack, D G

Cell death and differentiation

2005 Volume 12, Issue 8, Page(s) 1021–1030

Abstract: In the absence of their cognate ligand, dependence receptors trigger programmed cell death. This function is the defining feature of dependence receptors, which include members of several different protein families. The integrins are a family of ... ...

Abstract	In the absence of their cognate ligand, dependence receptors trigger programmed cell death. This function is the defining feature of dependence receptors, which include members of several different protein families. The integrins are a family of heterodimeric receptors for extracellular matrix (ECM) proteins, mediating cell anchorage and migration. Integrins share characteristics with dependence receptors, and integrin binding to substrate ECM ligands is essential for cell survival. Although integrins do not conform in all characteristics to the established definitions of dependence receptors, alterations in the expression of integrins and their ligands during physiological and pathological events, such as wound healing, angiogenesis and tumorigenesis, do regulate cell fate in a ligand-dependent manner. This biosensory function of integrins fits well with our current concept of dependence receptor action, and thus integrins may rightly be considered to comprise a distinct subclass of dependence receptor.
MeSH term(s)	Animals ; Apoptosis/physiology ; Extracellular Matrix/physiology ; Humans ; Integrins/physiology ; Ligands
Chemical Substances	Integrins ; Ligands
Language	English
Publishing date	2005-08
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1225672-9
ISSN	1350-9047
ISSN	1350-9047
DOI	10.1038/sj.cdd.4401658
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Zs.A 4230: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Regulation of angiogenesis: apoptotic cues from the ECM.

Cheresh, D A / Stupack, D G

Oncogene

2008 Volume 27, Issue 48, Page(s) 6285–6298

Abstract: The extracellular matrix (ECM) acts both as a physical scaffold for cells and as a repository for growth factors. Moreover, ECM structure and physical-chemical properties convey precise information to cells that profoundly influences their biology by ... ...

Abstract	The extracellular matrix (ECM) acts both as a physical scaffold for cells and as a repository for growth factors. Moreover, ECM structure and physical-chemical properties convey precise information to cells that profoundly influences their biology by interactions with cell surface receptors termed integrins. During angiogenesis, the perivascular ECM plays a critical role in determining the proliferative, invasive and survival responses of the local vascular cells to the angiogenic growth factors. Dynamic changes in both the ECM and the local vascular cells act in concert to regulate new blood vessel growth. The digestion of ECM components by proteolysis is critical for the invasive capacity of endothelial cells, but also creates ECM fragments, which antagonize the mechanosensory function of integrins, and can be apoptogenic. Here, we discuss the roles of integrins in modulating cellular responses to a changing ECM, in particular the regulation of survival and invasion among invasive endothelial cells.
MeSH term(s)	Animals ; Apoptosis ; Cell Adhesion ; Cell Survival ; Extracellular Matrix/physiology ; Humans ; Integrins/physiology ; Neovascularization, Physiologic/physiology ; Signal Transduction
Chemical Substances	Integrins
Language	English
Publishing date	2008-10-20
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	639046-8
ISSN	1476-5594 ; 0950-9232
ISSN (online)	1476-5594
ISSN	0950-9232
DOI	10.1038/onc.2008.304
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Zs.A 2218: Show issues

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Article ; Online: Caspase-8 as a novel mediator linking Src kinase signaling to enhanced glioblastoma malignancy.

Contadini, Claudia / Ferri, Alessandra / Di Martile, Marta / Cirotti, Claudia / Del Bufalo, Donatella / De Nicola, Francesca / Pallocca, Matteo / Fanciulli, Maurizio / Sacco, Francesca / Donninelli, Gloria / Capone, Alessia / Volpe, Elisabetta / Keller, Nadine / Miki, Shunichiro / Kawauchi, Daisuke / Stupack, Dwayne / Furnari, Frank / Barilà, Daniela

Cell death and differentiation

2022 Volume 30, Issue 2, Page(s) 417–428

Abstract: Caspase-8 is a cysteine protease that plays an essential role in apoptosis. Consistently with its canonical proapoptotic function, cancer cells may genetically or epigenetically downregulate its expression. Unexpectedly, Caspase-8 is often retained in ... ...

Abstract	Caspase-8 is a cysteine protease that plays an essential role in apoptosis. Consistently with its canonical proapoptotic function, cancer cells may genetically or epigenetically downregulate its expression. Unexpectedly, Caspase-8 is often retained in cancer, suggesting the presence of alternative mechanisms that may be exploited by cancer cells to their own benefit. In this regard, we reported that Src tyrosine kinase, which is aberrantly activated in many tumors, promotes Caspase-8 phosphorylation on Tyrosine 380 (Y380) preventing its full activation. Here, we investigated the significance of Caspase-8 expression and of its phosphorylation on Y380 in glioblastoma, a brain tumor where both Caspase-8 expression and Src activity are often aberrantly upregulated. Transcriptomic analyses identified inflammatory response as a major target of Caspase-8, and in particular, NFκB signaling as one of the most affected pathways. More importantly, we could show that Src-dependent phosphorylation of Caspase-8 on Y380 drives the assembly of a multiprotein complex that triggers NFκB activation, thereby inducing the expression of inflammatory and pro-angiogenic factors. Remarkably, phosphorylation on Y380 sustains neoangiogenesis and resistance to radiotherapy. In summary, our work identifies a novel interplay between Src kinase and Caspase-8 that allows cancer cells to hijack Caspase-8 to sustain tumor growth.
MeSH term(s)	Humans ; Apoptosis ; Caspase 3/metabolism ; Caspase 8/metabolism ; Glioblastoma/genetics ; Phosphorylation ; Signal Transduction/physiology ; src-Family Kinases/metabolism
Chemical Substances	Caspase 3 (EC 3.4.22.-) ; Caspase 8 (EC 3.4.22.-) ; src-Family Kinases (EC 2.7.10.2)
Language	English
Publishing date	2022-12-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	1225672-9
ISSN	1476-5403 ; 1350-9047
ISSN (online)	1476-5403
ISSN	1350-9047
DOI	10.1038/s41418-022-01093-x
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Zs.A 4230: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Tumor FAK orchestrates immunosuppression in ovarian cancer via the CD155/TIGIT axis.

Proceedings of the National Academy of Sciences of the United States of America

2022 Volume 119, Issue 17, Page(s) e2117065119

Abstract: High-grade serous ovarian cancer (HGSOC) is a lethal malignancy characterized by an immunosuppressive tumor microenvironment containing few tumor infiltrating lymphocytes (TILs) and an insensitivity to checkpoint inhibitor immunotherapies. Gains in the ... ...

Abstract	High-grade serous ovarian cancer (HGSOC) is a lethal malignancy characterized by an immunosuppressive tumor microenvironment containing few tumor infiltrating lymphocytes (TILs) and an insensitivity to checkpoint inhibitor immunotherapies. Gains in the PTK2 gene encoding focal adhesion kinase (FAK) at Chr8 q24.3 occur in ∼70% of HGSOC tumors, and elevated FAK messenger RNA (mRNA) levels are associated with poor patient survival. Herein, we show that active FAK, phosphorylated at tyrosine-576 within catalytic domain, is significantly increased in late-stage HGSOC tumors. Active FAK costained with CD155, a checkpoint receptor ligand for TIGIT (T cell immunoreceptor with immunoglobulin and immunoreceptor tyrosine-based inhibitory motif domains), in HGSOC tumors and a selective association between FAK and TIGIT checkpoint ligands were supported by patient transcriptomic database analysis. HGSOC tumors with high FAK expression were associated with low CD3 mRNA levels. Accordingly, late-stage tumors showed elevated active FAK staining and significantly lower levels of CD3+ TILs. Using the KMF (Kras, Myc, FAK) syngeneic ovarian tumor model containing spontaneous PTK2 (FAK) gene gains, the effects of tumor intrinsic genetic or oral small molecule FAK inhibitior (FAKi; VS-4718) were evaluated in vivo. Blocking FAK activity decreased tumor burden, suppressed ascites KMF-associated CD155 levels, and increased peritoneal TILs. The combination of FAKi with blocking TIGIT antibody (1B4) maintained elevated TIL levels and reduced TIGIT+ T regulatory cell levels, prolonged host survival, increased CXCL13 levels, and led to the formation of omental tertiary lymphoid structures. Collectively, our studies support FAK and TIGIT targeting as a rationale immunotherapy combination for HGSOC.
MeSH term(s)	Animals ; Carcinoma, Ovarian Epithelial ; Female ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Humans ; Immunosuppression Therapy ; Ligands ; Mice ; Ovarian Neoplasms/pathology ; Receptors, Immunologic/metabolism
Chemical Substances	Ligands ; Receptors, Immunologic ; T cell Ig and ITIM domain protein, mouse ; TIGIT protein, human ; Focal Adhesion Kinase 1 (EC 2.7.10.2) ; Focal Adhesion Protein-Tyrosine Kinases (EC 2.7.10.2) ; PTK2 protein, human (EC 2.7.10.2) ; Ptk2 protein, mouse (EC 2.7.10.2)
Language	English
Publishing date	2022-04-25
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2117065119
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Article ; Online: Rgnef promotes ovarian tumor progression and confers protection from oxidative stress.

Kleinschmidt, Elizabeth G / Miller, Nichol L G / Ozmadenci, Duygu / Tancioni, Isabelle / Osterman, Carlos Díaz / Barrie, Allison M / Taylor, Kristin N / Ye, Aaron / Jiang, Shulin / Connolly, Denise C / Stupack, Dwayne G / Schlaepfer, David D

Oncogene

2019 Volume 38, Issue 36, Page(s) 6323–6337

Abstract: Ovarian cancer is the fifth-leading cause of cancer death among women. The dissemination of ovarian tumors and growth as spheroids accompanies late-stage disease. In cell culture, ovarian tumor cell spheroids can exhibit elevated resistance to ... ...

Abstract	Ovarian cancer is the fifth-leading cause of cancer death among women. The dissemination of ovarian tumors and growth as spheroids accompanies late-stage disease. In cell culture, ovarian tumor cell spheroids can exhibit elevated resistance to environmental stressors, such as reactive oxygen species. Homeostatic balance of the antioxidant response is a protective mechanism that prevents anoikis, a form of programmed cell death. Signaling pathways activated by integrin receptors suppress anoikis. Rgnef (ARHGEF28/p190RhoGEF) is a guanine nucleotide exchange factor that is activated downstream of integrins. We find that Rgnef protein levels are elevated in late-stage serous ovarian cancer, high Rgnef mRNA levels are associated with decreased progression-free and overall survival, and genomic ARHGEF28 loss is associated with increased patient survival. Using transgenic and transplantable Rgnef knockout mouse models, we find that Rgnef is essential for supporting three-dimensional ovarian spheroid formation in vitro and tumor growth in mice. Using RNA-sequencing and bioinformatic analyses, we identify a conserved Rgnef-supported anti-oxidant gene signature including Gpx4, Nqo1, and Gsta4; common targets of the NF-kB transcription factor. Antioxidant treatment enhanced growth of Rgnef-knockout spheroids and Rgnef re-expression facilitated NF-κB-dependent tumorsphere survival. These studies reveal a new role for Rgnef in ovarian cancer to facilitate NF-κB-mediated gene expression protecting cells from oxidative stress.
MeSH term(s)	Animals ; Cell Proliferation/genetics ; Cytoprotection/genetics ; Disease Progression ; Female ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/physiology ; HEK293 Cells ; Humans ; Mice ; Mice, Knockout ; NF-kappa B/metabolism ; Ovarian Neoplasms/genetics ; Ovarian Neoplasms/metabolism ; Ovarian Neoplasms/pathology ; Oxidative Stress/genetics ; Signal Transduction/genetics ; Tumor Cells, Cultured ; ras-GRF1/genetics ; ras-GRF1/physiology
Chemical Substances	ARHGEF28 protein, human ; Guanine Nucleotide Exchange Factors ; NF-kappa B ; Rasgrf1 protein, mouse ; ras-GRF1
Language	English
Publishing date	2019-07-15
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	639046-8
ISSN	1476-5594 ; 0950-9232
ISSN (online)	1476-5594
ISSN	0950-9232
DOI	10.1038/s41388-019-0881-8
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Article: Integrins and angiogenesis.

Stupack, D G / Cheresh, D A

Current topics in developmental biology

2004 Volume 64, Page(s) 207–238

Abstract: The growth of new blood vessels is a dynamic yet highly regulated process that depends on coordinated signaling by growth factor and cell adhesion receptors. As part of the molecular program regulating angiogenesis, endothelial cells acquire a ... ...

Abstract	The growth of new blood vessels is a dynamic yet highly regulated process that depends on coordinated signaling by growth factor and cell adhesion receptors. As part of the molecular program regulating angiogenesis, endothelial cells acquire a proliferative and invasive phenotype but also show increased susceptibility to apoptotic stimuli. Integrins are the principle adhesion receptors used by endothelial cells to interact with their extracellular microenvironment, and integrin-mediated interactions play a critical role in regulating cell proliferation, migration, and survival. Alterations in the repertoire and?or activity of integrins, as well as the availability and structural property of their ligands, regulate the vascular cell during the growth or repair of blood vessels.
MeSH term(s)	Animals ; Blood Vessels/anatomy & histology ; Blood Vessels/physiology ; Cell Survival ; Clinical Trials as Topic ; Endothelial Cells/cytology ; Endothelial Cells/metabolism ; Endothelium, Vascular/cytology ; Endothelium, Vascular/metabolism ; Extracellular Matrix/metabolism ; Fibrin/metabolism ; Humans ; Integrins/genetics ; Integrins/metabolism ; Matrix Metalloproteinases/metabolism ; Mitogen-Activated Protein Kinases/metabolism ; Neovascularization, Physiologic ; Plasminogen/metabolism ; Urokinase-Type Plasminogen Activator/metabolism
Chemical Substances	Integrins ; Fibrin (9001-31-4) ; Plasminogen (9001-91-6) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Urokinase-Type Plasminogen Activator (EC 3.4.21.73) ; Matrix Metalloproteinases (EC 3.4.24.-)
Language	English
Publishing date	2004
Publishing country	United States
Document type	Journal Article ; Review
ISSN	1557-8933 ; 0070-2153
ISSN (online)	1557-8933
ISSN	0070-2153
DOI	10.1016/S0070-2153(04)64009-9
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