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Article: New Azo Derivatives of Ethanol Lignin: Synthesis, Structure, and Photosensitive Properties.

Borovkova, Valentina S / Malyar, Yuriy N / Vasilieva, Natalia Yu / Skripnikov, Andrey M / Ionin, Vladislav A / Sychev, Valentin V / Golubkov, Viktor A / Taran, Oxana P

Materials (Basel, Switzerland)

2023 Volume 16, Issue 4

Abstract: Water-soluble azo derivatives of lignin were synthesized by the azo coupling reaction using organosolv ethanol lignin and diazonium salts based on sulfanilic acid and p-nitroaniline. The structure of azo derivatives of lignin were studied by nuclear ... ...

Abstract	Water-soluble azo derivatives of lignin were synthesized by the azo coupling reaction using organosolv ethanol lignin and diazonium salts based on sulfanilic acid and p-nitroaniline. The structure of azo derivatives of lignin were studied by nuclear magnetic resonance, Fourier-transform infrared spectroscopy, and gel permeation chromatography. It was found that the azobenzene bonds formed in the azo coupling reaction of macromolecules impart the photosensitive properties to the synthesized polymers via cis-trans photoisomerization of the diazobenzene group. It was shown experimentally that the synthesized polymers exhibited good solubility both in the aqueous media in a wide (2-12) pH range and in DMSO and THF organic solvents, which opens up new prospects for their application.
Language	English
Publishing date	2023-02-11
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2487261-1
ISSN	1996-1944
ISSN	1996-1944
DOI	10.3390/ma16041525
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Article ; Online: Downstream signaling and genome-wide regulatory effects of PTK7 pseudokinase and its proteolytic fragments in cancer cells.

Golubkov, Vladislav S / Strongin, Alex Y

Cell communication and signaling : CCS

2014 Volume 12, Page(s) 15

Abstract: Background: The full-length membrane protein tyrosine kinase 7 (PTK7) pseudokinase, an important component of the planar cell polarity and the Wnt canonical and non-canonical pathways, is a subject of step-wise proteolysis in cells and tissues. The ... ...

Abstract	Background: The full-length membrane protein tyrosine kinase 7 (PTK7) pseudokinase, an important component of the planar cell polarity and the Wnt canonical and non-canonical pathways, is a subject of step-wise proteolysis in cells and tissues. The proteolysis of PTK7 involves membrane type-matrix metalloproteinase (MT1-MMP), members of the Disintegrin Domain and Metalloproteinase (ADAM) family, and γ-secretase. This multi-step proteolysis results in the generation of the digest fragments of PTK7. These fragments may be either liberated into the extracellular milieu or retained on the plasma membrane or released into the cytoplasm and then transported into the nucleus. Results: We employed the genome-wide transcriptional and kinome array analyses to determine the role of the full-length membrane PTK7 and its proteolytic fragments in the downstream regulatory mechanisms, with an emphasis on the cell migration-related genes and proteins. Using fibrosarcoma HT1080 cells stably expressing PTK7 and its mutant and truncated species, the structure of which corresponded to the major PTK7 digest fragments, we demonstrated that the full-length membrane 1-1070 PTK7, the N-terminal 1-694 soluble ectodomain fragment, and the C-terminal 622-1070 and 726-1070 fragments differentially regulate multiple genes and signaling pathways in our highly invasive cancer cell model. Immunoblotting of the selected proteins were used to validate the results of our high throughput assays. Conclusions: Our results suggest that PTK7 levels need to be tightly controlled to enable migration and that the anti-migratory effect of the full-length membrane PTK7 is linked to the down-regulation of multiple migration-related genes and to the activation of the Akt and c-Jun pathway. In turn, the C-terminal fragments of PTK7 act predominantly via the RAS-ERK and CREB/ATF1 pathway and through the up-regulation of cadherin-11. In general, our data correlate well with the distinct functionality of the full-length receptor tyrosine kinases and their respective intracellular domain (ICD) proteolytic fragments.
MeSH term(s)	Cell Adhesion Molecules/metabolism ; Cell Line, Tumor ; Cell Movement ; Fibrosarcoma/genetics ; Fibrosarcoma/metabolism ; Gene Expression Regulation, Neoplastic ; Genome, Human ; Humans ; Peptide Fragments/metabolism ; Proteolysis ; Receptor Protein-Tyrosine Kinases/metabolism ; Signal Transduction ; Transcriptome
Chemical Substances	Cell Adhesion Molecules ; Peptide Fragments ; PTK7 protein, human (EC 2.7.10.1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1)
Language	English
Publishing date	2014-03-11
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1478-811X
ISSN (online)	1478-811X
DOI	10.1186/1478-811X-12-15
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Article ; Online: Insights into ectodomain shedding and processing of protein-tyrosine pseudokinase 7 (PTK7).

Golubkov, Vladislav S / Strongin, Alex Y

The Journal of biological chemistry

2012 Volume 287, Issue 50, Page(s) 42009–42018

Abstract: The membrane PTK7 pseudokinase, a component of both the canonical and noncanonical/planar cell polarity Wnt pathways, modulates cell polarity and motility in biological processes as diverse as embryo development and cancer cell invasion. To determine the ...

Abstract	The membrane PTK7 pseudokinase, a component of both the canonical and noncanonical/planar cell polarity Wnt pathways, modulates cell polarity and motility in biological processes as diverse as embryo development and cancer cell invasion. To determine the individual proteolytic events and biological significance of the ectodomain shedding in the PTK7 function, we used highly invasive fibrosarcoma HT1080 cells as a model system. Current evidence suggested a likely link between PTK7 shedding and cell invasion in our HT1080 cell model system. We also demonstrated that in HT1080 cells the cleavage of the PTK7 ectodomain by an ADAM proteinase was coupled with the membrane type-1 matrix metalloproteinase (MT1-MMP) cleavage of the PKP(621)↓LI site in the seventh Ig-like domain of PTK7. Proteolytic cleavages led to the generation of two soluble, N-terminal and two matching C-terminal, cell-associated fragments of PTK7. This proteolysis was a prerequisite for the intramembrane cleavage of the C-terminal fragments of PTK7 by γ-secretase. γ-Secretase cleavage was predominantly followed by the efficient decay of the resulting C-terminal PTK7 fragment via the proteasome. In contrast, in HT1080 cells, which overexpressed the C-terminal PTK7 fragment, the latter readily entered the nucleus. Our data imply that therapeutic inhibition of PTK7 shedding may be used to slow cancer progression.
MeSH term(s)	ADAM Proteins/genetics ; ADAM Proteins/metabolism ; Active Transport, Cell Nucleus/genetics ; Amyloid Precursor Protein Secretases/genetics ; Amyloid Precursor Protein Secretases/metabolism ; Cell Adhesion Molecules/genetics ; Cell Adhesion Molecules/metabolism ; Cell Line, Tumor ; Fibrosarcoma/enzymology ; Fibrosarcoma/genetics ; Fibrosarcoma/pathology ; Humans ; Matrix Metalloproteinase 14/genetics ; Matrix Metalloproteinase 14/metabolism ; Neoplasm Invasiveness ; Protein Structure, Tertiary ; Proteolysis ; Receptor Protein-Tyrosine Kinases/genetics ; Receptor Protein-Tyrosine Kinases/metabolism ; Solubility
Chemical Substances	Cell Adhesion Molecules ; PTK7 protein, human (EC 2.7.10.1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; ADAM Proteins (EC 3.4.24.-) ; Matrix Metalloproteinase 14 (EC 3.4.24.80)
Language	English
Publishing date	2012-10-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M112.371153
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Article ; Online: Proteolysis-driven oncogenesis.

Golubkov, Vladislav S / Strongin, Alex Y

Cell cycle (Georgetown, Tex.)

2007 Volume 6, Issue 2, Page(s) 147–150

Abstract: An elevated expression of matrix metalloproteinases (MMPs) has been correlated with the growth and metastasis of preexisting tumors. The latest data, however, suggest that MMPs, by promoting genomic instability, are directly involved in the early stages ... ...

Abstract	An elevated expression of matrix metalloproteinases (MMPs) has been correlated with the growth and metastasis of preexisting tumors. The latest data, however, suggest that MMPs, by promoting genomic instability, are directly involved in the early stages of cell transformation from normalcy to malignancy and in incipient cancer. Here, we discuss these novel findings and present a novel concept of a proteolysis-driven oncogenesis. We have placed the emphasis of our review on the membrane type-1 matrix metalloproteinase (MT1-MMP)-induced chromosome instability which leads to the transition from normalcy to malignancy.
MeSH term(s)	Animals ; Chromosomal Instability ; Humans ; Hydrolysis ; Matrix Metalloproteinase 1/genetics ; Matrix Metalloproteinase 1/metabolism ; Neoplasms/enzymology ; Neoplasms/genetics ; Neoplasms/pathology
Chemical Substances	Matrix Metalloproteinase 1 (EC 3.4.24.7)
Language	English
Publishing date	2007-01-12
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2146183-1
ISSN	1551-4005 ; 1538-4101 ; 1554-8627
ISSN (online)	1551-4005
ISSN	1538-4101 ; 1554-8627
DOI	10.4161/cc.6.2.3706
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Article ; Online: Intradomain cleavage of inhibitory prodomain is essential to protumorigenic function of membrane type-1 matrix metalloproteinase (MT1-MMP) in vivo.

Golubkov, Vladislav S / Chernov, Andrei V / Strongin, Alex Y

The Journal of biological chemistry

2011 Volume 286, Issue 39, Page(s) 34215–34223

Abstract: Invasive cancers use pericellular proteolysis to breach the extracellular matrix and basement membrane barriers and invade the surrounding tissue. Proinvasive membrane type-1 matrix metalloproteinase (MT1-MMP) is the primary mediator of proteolytic ... ...

Abstract	Invasive cancers use pericellular proteolysis to breach the extracellular matrix and basement membrane barriers and invade the surrounding tissue. Proinvasive membrane type-1 matrix metalloproteinase (MT1-MMP) is the primary mediator of proteolytic events on the cancer cell surface. MT1-MMP is synthesized as a zymogen. The latency of MT1-MMP is maintained by its N-terminal inhibitory prodomain. In the course of MT1-MMP activation, the R(108)RKR(111) ↓ Y(112) prodomain sequence is processed by furin. The intact prodomain released by furin alone, however, is a potent inhibitor of the emerging MT1-MMP enzyme. Evidence suggests that the prodomain undergoes intradomain cleavage at the PGD ↓ L(50) site followed by the release of the degraded prodomain by furin cleavage that finalizes the two-step activation event. These cleavages, only if combined, cause the activation of MT1-MMP. The significance of the intradomain cleavage in the protumorigenic program of MT1-MMP, however, remained unidentified. To identify this important parameter, in our current study, we used the cells that expressed the wild-type prodomain-based fluorescent biosensor and the mutant biosensor with the inactivated PGD↓L(50) cleavage site (L50D mutant) and also the cells with the enforced expression of the wild-type and L50D mutant MT1-MMP. Using cell-based tests, orthotopic breast cancer xenografts in mice, and genome-wide transcriptional profiling of cultured cells and tumor xenografts, we demonstrated that the intradomain cleavage of the PGD ↓ L(50) sequence of the prodomain is essential for the protumorigenic function of MT1-MMP. Our results emphasize the importance of the intradomain cleavages resulting in the inactivation of the respective inhibitory prodomains not only for MT1-MMP but also for other MMP family members.
MeSH term(s)	Amino Acid Substitution ; Animals ; Breast Neoplasms/enzymology ; Breast Neoplasms/genetics ; Cell Line, Tumor ; Enzyme Activation/genetics ; Female ; Furin/genetics ; Furin/metabolism ; Humans ; Matrix Metalloproteinase 14/genetics ; Matrix Metalloproteinase 14/metabolism ; Mice ; Mice, Nude ; Mutation, Missense ; Neoplasm Invasiveness ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Neoplasm Transplantation ; Transplantation, Heterologous
Chemical Substances	Neoplasm Proteins ; FURIN protein, human (EC 3.4.21.75) ; Furin (EC 3.4.21.75) ; MMP14 protein, human (EC 3.4.24.80) ; Matrix Metalloproteinase 14 (EC 3.4.24.80)
Language	English
Publishing date	2011-08-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.264036
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Article ; Online: Potential relation of aberrant proteolysis of human protein tyrosine kinase 7 (PTK7) chuzhoi by membrane type 1 matrix metalloproteinase (MT1-MMP) to congenital defects.

Golubkov, Vladislav S / Aleshin, Alexander E / Strongin, Alex Y

The Journal of biological chemistry

2011 Volume 286, Issue 23, Page(s) 20970–20976

Abstract: Membrane PTK7 pseudo-kinase plays an essential role in planar cell polarity and the non-canonical Wnt pathway in vertebrates. Recently, a new N-ethyl-N-nitrosourea-induced mutant named chuzhoi (chz) was isolated in mice. chz embryos have severe birth ... ...

Abstract	Membrane PTK7 pseudo-kinase plays an essential role in planar cell polarity and the non-canonical Wnt pathway in vertebrates. Recently, a new N-ethyl-N-nitrosourea-induced mutant named chuzhoi (chz) was isolated in mice. chz embryos have severe birth defects, including a defective neural tube, defective heart and lung development, and a shortened anterior-posterior body axis. The chz mutation was mapped to the Ala-Asn-Pro tripeptide insertion into the junction region between the fifth and the sixth Ig-like domains of PTK7. Unexpectedly, chz reduced membrane localization of the PTK7 protein. We hypothesized and then proved that the chz mutation caused an insertion of an additional membrane type 1 matrix metalloproteinase cleavage site in PTK7 and that the resulting aberrant proteolysis of chz affected the migratory parameters of the cells. It is likely that aberrations in the membrane type 1 matrix metalloproteinase/PTK7 axis are detrimental to cell movements that shape the body plan and that chz represents a novel model system for increasing our understanding of the role of proteolysis in developmental pathologies, including congenital defects.
MeSH term(s)	Abnormalities, Drug-Induced/enzymology ; Abnormalities, Drug-Induced/genetics ; Alkylating Agents/adverse effects ; Alkylating Agents/pharmacology ; Animals ; Cell Adhesion Molecules/genetics ; Cell Adhesion Molecules/metabolism ; Cell Line, Tumor ; Cell Movement/drug effects ; Cell Movement/genetics ; Cell Shape/drug effects ; Cell Shape/genetics ; Ethylnitrosourea/adverse effects ; Ethylnitrosourea/pharmacology ; Humans ; Matrix Metalloproteinase 14/genetics ; Matrix Metalloproteinase 14/metabolism ; Mice ; Mutation ; Protein Structure, Tertiary ; Receptor Protein-Tyrosine Kinases/genetics ; Receptor Protein-Tyrosine Kinases/metabolism
Chemical Substances	Alkylating Agents ; Cell Adhesion Molecules ; Mmp14 protein, mouse ; PTK7 protein, human (EC 2.7.10.1) ; Ptk7 protein, mouse (EC 2.7.10.1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; MMP14 protein, human (EC 3.4.24.80) ; Matrix Metalloproteinase 14 (EC 3.4.24.80) ; Ethylnitrosourea (P8M1T4190R)
Language	English
Publishing date	2011-04-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.237669
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Article ; Online: Protein-tyrosine pseudokinase 7 (PTK7) directs cancer cell motility and metastasis.

Golubkov, Vladislav S / Prigozhina, Natalie L / Zhang, Yong / Stoletov, Konstantin / Lewis, John D / Schwartz, Phillip E / Hoffman, Robert M / Strongin, Alex Y

The Journal of biological chemistry

2014 Volume 289, Issue 35, Page(s) 24238–24249

Abstract: It is well established that widely expressed PTK7 is essential for vertebrate tissue morphogenesis. In cancer, the functionality of PTK7 is selectively regulated by membrane type-1 matrix metalloproteinase (MT1-MMP), ADAMs (a disintegrin domain and ... ...

Abstract	It is well established that widely expressed PTK7 is essential for vertebrate tissue morphogenesis. In cancer, the functionality of PTK7 is selectively regulated by membrane type-1 matrix metalloproteinase (MT1-MMP), ADAMs (a disintegrin domain and metalloproteinases), and γ-secretase proteolysis. Here, we established that the full-length membrane PTK7, its Chuzhoi mutant with the two functional MT1-MMP cleavage sites, and its L622D mutant with the single inactivated MT1-MMP cleavage site differentially regulate cell motility in a two-dimensional versus three-dimensional environment. We also demonstrated that in polarized cancer cells, the levels of PTK7 expression and proteolysis were directly linked to the structure and kinetics of cell protrusions, including lamellipodia and invadopodia. In the functionally relevant and widely accepted animal models of metastasis, mouse and chick embryo models, both the overexpression and knock-out of PTK7 in HT1080 cells abrogated metastatic dissemination. Our analysis of human tissue specimens confirmed intensive proteolysis of PTK7 in colorectal cancer tumors, but not in matching normal tissue. Our results provide convincing evidence that both PTK7 expression and proteolysis, rather than the level of the cellular full-length PTK7 alone, contribute to efficient directional cell motility and metastasis in cancer.
MeSH term(s)	Animals ; Cell Adhesion Molecules/metabolism ; Cell Line, Tumor ; Cell Movement ; Chick Embryo ; Fibrosarcoma/enzymology ; Fibrosarcoma/pathology ; Humans ; Matrix Metalloproteinase 14/metabolism ; Neoplasm Metastasis ; Proteolysis ; Receptor Protein-Tyrosine Kinases/metabolism
Chemical Substances	Cell Adhesion Molecules ; PTK7 protein, human (EC 2.7.10.1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; Matrix Metalloproteinase 14 (EC 3.4.24.80)
Language	English
Publishing date	2014-07-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M114.574459
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Article ; Online: Identification of Annexin A4 as a hepatopancreas factor involved in liver cell survival.

Zhang, Danhua / Golubkov, Vladislav S / Han, Wenlong / Correa, Ricardo G / Zhou, Ying / Lee, Sunyoung / Strongin, Alex Y / Dong, P Duc Si

Developmental biology

2014 Volume 395, Issue 1, Page(s) 96–110

Abstract: To gain insight into liver and pancreas development, we investigated the target of 2F11, a monoclonal antibody of unknown antigen, widely used in zebrafish studies for labeling hepatopancreatic ducts. Utilizing mass spectrometry and in vivo assays, we ... ...

Abstract	To gain insight into liver and pancreas development, we investigated the target of 2F11, a monoclonal antibody of unknown antigen, widely used in zebrafish studies for labeling hepatopancreatic ducts. Utilizing mass spectrometry and in vivo assays, we determined the molecular target of 2F11 to be Annexin A4 (Anxa4), a calcium binding protein. We further found that in both zebrafish and mouse endoderm, Anxa4 is broadly expressed in the developing liver and pancreas, and later becomes more restricted to the hepatopancreatic ducts and pancreatic islets, including the insulin producing ß-cells. Although Anxa4 is a known target of several monogenic diabetes genes and its elevated expression is associated with chemoresistance in malignancy, its in vivo role is largely unexplored. Knockdown of Anxa4 in zebrafish leads to elevated expression of caspase 8 and Δ113p53, and liver bud specific activation of Caspase 3 and apoptosis. Mosaic knockdown reveal that Anxa4 is required cell-autonomously in the liver bud for cell survival. This finding is further corroborated with mosaic anxa4 knockout studies using the CRISPR/Cas9 system. Collectively, we identify Anxa4 as a new, evolutionarily conserved hepatopancreatic factor that is required in zebrafish for liver progenitor viability, through inhibition of the extrinsic apoptotic pathway. A role for Anxa4 in cell survival may have implications for the mechanism of diabetic ß-cell apoptosis and cancer cell chemoresistance.
MeSH term(s)	Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Annexin A4/genetics ; Annexin A4/metabolism ; Apoptosis/genetics ; Base Sequence ; Caspase 3/metabolism ; Cell Survival ; Embryo, Nonmammalian/cytology ; Embryo, Nonmammalian/embryology ; Embryo, Nonmammalian/metabolism ; Gene Expression Regulation, Developmental ; Gene Knockdown Techniques ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Immunohistochemistry ; In Situ Hybridization ; Liver/cytology ; Liver/embryology ; Liver/metabolism ; Microscopy, Confocal ; Molecular Sequence Data ; Pancreas/cytology ; Pancreas/embryology ; Pancreas/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Zebrafish/genetics ; Zebrafish/metabolism ; Zebrafish Proteins/genetics ; Zebrafish Proteins/metabolism
Chemical Substances	Annexin A4 ; Zebrafish Proteins ; Green Fluorescent Proteins (147336-22-9) ; Caspase 3 (EC 3.4.22.-)
Language	English
Publishing date	2014-08-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1114-9
ISSN	1095-564X ; 0012-1606
ISSN (online)	1095-564X
ISSN	0012-1606
DOI	10.1016/j.ydbio.2014.08.025
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Article: Action of fenretinide (4-HPR) on ovarian cancer and endothelial cells.

Golubkov, Vladislav / Garcia, Agustin / Markland, Francis S

Anticancer research

2005 Volume 25, Issue 1A, Page(s) 249–253

Abstract: Background: Fenretinide (4-HPR) is a synthetic retinoid that has been reported to inhibit the growth of cancer cell lines in vitro.: Materials and methods: We examined the effect of 4-HPR on ovarian cancer (OVCAR-5) cell proliferation, viability and ... ...

Abstract	Background: Fenretinide (4-HPR) is a synthetic retinoid that has been reported to inhibit the growth of cancer cell lines in vitro. Materials and methods: We examined the effect of 4-HPR on ovarian cancer (OVCAR-5) cell proliferation, viability and invasion using standard techniques. We also examined the action of 4-HPR on the actin cytoskeleton using immunocytochemistry, and on phosphorylation of focal adhesion kinase (FAK) using immunoprecipitation and phosphotyrosine immunoblotting. We then examined the activity of 4-HPR on endothelial cells using the tube formation assay on Matrigel. Results: 4-HPR inhibited OVCAR-5 cell proliferation and viability at concentrations higher than 1 microM, with 70-90% growth inhibition at 10 microM. 4-HPR (1 microM) significantly inhibited OVCAR-5 invasion after 3 days preincubation. In view of the importance of the cytoskeleton in cell motility, we examined the action of 4-HPR on the actin cytoskeleton and on FAK phosphorylation. In OVCAR-5 cells treated with 1 mM fenretinide for 3 days, actin cytoskeleton stress fibers were disrupted and FAK tyrosine phosphorylation was elevated dose-dependently. Endothelial cells treated with 1 microM 4-HPR failed to form tubes, but formed small cellular aggregates. Conclusion: Fenretinide has anti-tumor activity by acting on the actin cytoskeleton and by regulating FAK tyrosine phosphorylation. 4-HPR also inhibits endothelial cell tube formation, a major step in angiogenesis.
MeSH term(s)	Actins/metabolism ; Angiogenesis Inhibitors/pharmacology ; Antineoplastic Agents/pharmacology ; Cell Line, Tumor ; Cell Proliferation/drug effects ; Cytoskeleton/drug effects ; Cytoskeleton/metabolism ; Endothelial Cells/cytology ; Endothelial Cells/drug effects ; Endothelial Cells/enzymology ; Female ; Fenretinide/pharmacology ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Humans ; Neoplasm Invasiveness ; Neovascularization, Pathologic/drug therapy ; Neovascularization, Pathologic/enzymology ; Neovascularization, Pathologic/pathology ; Ovarian Neoplasms/blood supply ; Ovarian Neoplasms/drug therapy ; Ovarian Neoplasms/enzymology ; Ovarian Neoplasms/pathology ; Phosphorylation/drug effects ; Protein-Tyrosine Kinases/metabolism ; Umbilical Veins/cytology
Chemical Substances	Actins ; Angiogenesis Inhibitors ; Antineoplastic Agents ; Fenretinide (187EJ7QEXL) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; 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)
Language	English
Publishing date	2005-01
Publishing country	Greece
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	604549-2
ISSN	1791-7530 ; 0250-7005
ISSN (online)	1791-7530
ISSN	0250-7005
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Article: Membrane type-1 matrix metalloproteinase (MT1-MMP) protects malignant cells from tumoricidal activity of re-engineered anthrax lethal toxin.

Rozanov, Dmitri V / Golubkov, Vladislav S / Strongin, Alex Y

The international journal of biochemistry & cell biology

2005 Volume 37, Issue 1, Page(s) 142–154

Abstract: Protective antigen (PA) and lethal factor (LF) are the two components of anthrax lethal toxin. PA is responsible for interacting with cell receptors and for the subsequent translocation of LF inside the cell compartment. A re-engineered toxin comprised ... ...

Abstract	Protective antigen (PA) and lethal factor (LF) are the two components of anthrax lethal toxin. PA is responsible for interacting with cell receptors and for the subsequent translocation of LF inside the cell compartment. A re-engineered toxin comprised of PA and a fusion chimera LF/Pseudomonas exotoxin (FP59) is a promising choice for tumor cell surface targeting. We demonstrated, however, that in vitro in cell-free system and in cultured human colon carcinoma LoVo, fibrosarcoma HT1080 and glioma U251 cells membrane type-1 matrix metalloproteinase (MT1-MMP) cleaves both the PA83 precursor and the PA63 mature protein. Exhaustive MT1-MMP cleavage of PA83 in vitro generates several major degradation fragments with an N-terminus at Glu40, Leu48, and Gln512. In cultured cells, MT1-MMP-dependent cleavage releases the cell-bound PA83 and PA63 species from the cell surface. As a result, MT1-MMP expressing cells have less PA63 to internalize. In agreement, our observations demonstrate that MT1-MMP proteolysis of PA makes the MT1-MMP-expressing aggressive invasive cells resistant to the cytotoxic effect of a bipartite PA/FP59 toxin. We infer from our studies that synthetic inhibitors of MMPs are likely to increase the therapeutic anti-cancer effect of anthrax toxin. In addition, our study supports a unique role of furin in the activation of PA, thereby suggesting that furin inhibitors are the likely specific drugs for short-term therapy of anthrax infection.
MeSH term(s)	Antigens, Bacterial/genetics ; Antigens, Bacterial/metabolism ; Antigens, Bacterial/therapeutic use ; Bacterial Toxins/genetics ; Bacterial Toxins/metabolism ; Bacterial Toxins/therapeutic use ; Cell Line, Tumor ; Exotoxins/genetics ; Exotoxins/metabolism ; Exotoxins/therapeutic use ; Gene Expression Regulation, Neoplastic/genetics ; Humans ; Matrix Metalloproteinases, Membrane-Associated ; Metalloendopeptidases/genetics ; Metalloendopeptidases/metabolism ; Neoplasms/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism
Chemical Substances	Antigens, Bacterial ; Bacterial Toxins ; Exotoxins ; Recombinant Fusion Proteins ; anthrax toxin ; Matrix Metalloproteinases, Membrane-Associated (EC 3.4.24.-) ; Metalloendopeptidases (EC 3.4.24.-)
Language	English
Publishing date	2005-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2004.06.005
Database	MEDical Literature Analysis and Retrieval System OnLINE

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