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Article ; Online: Conditioned Medium of Mesenchymal Stromal Cells: A New Class of Therapeutics.

Bogatcheva, N V / Coleman, M E

2019 Volume 84, Issue 11, Page(s) 1375–1389

Abstract: Mesenchymal stromal cell (MSCs) represent a class of biologics with the prospects for employment as immunomodulatory, tissue-protective, and regenerative therapeutics. In parallel with cellular therapy, cell-free therapy based on MSC-secreted bioactive ... ...

Abstract	Mesenchymal stromal cell (MSCs) represent a class of biologics with the prospects for employment as immunomodulatory, tissue-protective, and regenerative therapeutics. In parallel with cellular therapy, cell-free therapy based on MSC-secreted bioactive factors is being actively developed. MSCs secrete a variety of protein, peptide, RNA, and lipid mediators which can be concentrated, frozen, or even lyophilized without loss of activity, which gives them a certain advantage over cellular products requiring liquid nitrogen storage and infrastructure to revive frozen cells. This review (i) describes currently conducted clinical trials of cell-free products containing MSC secretome; (ii) summarizes main approaches to the generation and characterization of conditioned media concentrates and extracellular vesicle isolates; (iii) analyzes a variety of preclinical studies where effectiveness of secretome products has been shown; and (iv) summarizes current knowledge about secretome bioactive components obtained by analysis of in vivo models testing the therapeutic potential of the MSC secretome.
MeSH term(s)	Acute Kidney Injury/pathology ; Acute Kidney Injury/prevention & control ; Animals ; Arthritis/pathology ; Arthritis/prevention & control ; Bone Marrow Cells/cytology ; Culture Media, Conditioned/chemistry ; Culture Media, Conditioned/pharmacology ; Drug Evaluation, Preclinical ; Exosomes/metabolism ; Lung Injury/pathology ; Lung Injury/prevention & control ; Mesenchymal Stem Cells/cytology ; Mesenchymal Stem Cells/metabolism
Chemical Substances	Culture Media, Conditioned
Language	English
Publishing date	2019-11-29
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1109-5
ISSN	1608-3040 ; 0006-2979 ; 0320-9717
ISSN (online)	1608-3040
ISSN	0006-2979 ; 0320-9717
DOI	10.1134/S0006297919110129
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Article ; Online: Inhibition of autocrine HGF maturation overcomes cetuximab resistance in colorectal cancer.

Jones, Vivian Truong / Graves-Deal, Ramona / Cao, Zheng / Bogatcheva, Galina / Ramirez, Marisol A / Harmych, Sarah J / Higginbotham, James N / Sharma, Vineeta / Damalanka, Vishnu C / Wahoski, Claudia C / Joshi, Neeraj / Irudayam, Maria Johnson / Roland, Joseph T / Ayers, Gregory D / Liu, Qi / Coffey, Robert J / Janetka, James W / Singh, Bhuminder

Cellular and molecular life sciences : CMLS

2024 Volume 81, Issue 1, Page(s) 28

Abstract: Although amplifications and mutations in receptor tyrosine kinases (RTKs) act as bona fide oncogenes, in most cancers, RTKs maintain moderate expression and remain wild-type. Consequently, cognate ligands control many facets of tumorigenesis, including ... ...

Abstract	Although amplifications and mutations in receptor tyrosine kinases (RTKs) act as bona fide oncogenes, in most cancers, RTKs maintain moderate expression and remain wild-type. Consequently, cognate ligands control many facets of tumorigenesis, including resistance to anti-RTK therapies. Herein, we show that the ligands for the RTKs MET and RON, HGF and HGFL, respectively, are synthesized as inactive precursors that are activated by cellular proteases. Our newly generated HGF/HGFL protease inhibitors could overcome both de novo and acquired cetuximab resistance in colorectal cancer (CRC). Conversely, HGF overexpression was necessary and sufficient to induce cetuximab resistance and loss of polarity. Moreover, HGF-induced cetuximab resistance could be overcome by the downstream MET inhibitor, crizotinib, and upstream protease inhibitors. Additionally, HAI-1, an endogenous inhibitor of HGF proteases, (i) was downregulated in CRC, (ii) exhibited increased genomic methylation that correlated with poor prognosis, (iii) HAI-1 expression correlated with cetuximab response in a panel of cancer cell lines, and (iv) exogenous addition of recombinant HAI-1 overcame cetuximab resistance in CC-HGF cells. Thus, we describe a targetable, autocrine HAI-1/Protease/HGF/MET axis in cetuximab resistance in CRC.
MeSH term(s)	Humans ; Cetuximab/pharmacology ; Signal Transduction ; Proto-Oncogene Proteins c-met/genetics ; Proto-Oncogene Proteins c-met/metabolism ; Drug Resistance, Neoplasm/genetics ; Colorectal Neoplasms/drug therapy ; Colorectal Neoplasms/genetics ; Colorectal Neoplasms/metabolism ; Protease Inhibitors/pharmacology ; Peptide Hydrolases/metabolism ; Cell Line, Tumor ; Hepatocyte Growth Factor/genetics ; Hepatocyte Growth Factor/metabolism ; Hepatocyte Growth Factor/pharmacology
Chemical Substances	Cetuximab (PQX0D8J21J) ; Proto-Oncogene Proteins c-met (EC 2.7.10.1) ; Protease Inhibitors ; Peptide Hydrolases (EC 3.4.-) ; HGF protein, human ; Hepatocyte Growth Factor (67256-21-7)
Language	English
Publishing date	2024-01-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-023-05071-5
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Article: [THE DEVELOPMENT OF IMMUNE ENZYME AND IMMUNE CHROMATOGRAPHIC MONOCLONAL TEST-SYSTEM FOR DETECTING TULAREMIA AGENT].

Eremkin, A V / Elagin, G D / Petchenkin, D V / Fomenkov, O O / Bogatcheva, N V / Kitmanov, A A / Kuklina, G V / Tikhvinskaya, O V

Klinicheskaia laboratornaia diagnostika

2016 Volume 61, Issue 3, Page(s) 184–187

Abstract: The immune enzyme and immunochromatographic test-systems for detecting tularemia agent were developed on the basis of selected set of monoclonal antibodies having immunochemical activity to antigens Francisella tularensis. The evaluation of sensitivity ... ...

Abstract	The immune enzyme and immunochromatographic test-systems for detecting tularemia agent were developed on the basis of selected set of monoclonal antibodies having immunochemical activity to antigens Francisella tularensis. The evaluation of sensitivity and specificity of developed test-systems demonstrated that samples provided detection of strains of F. tularensis in concentration from 5.0 x 105 mkxcm-3 to 1.0 x 106 mkxcm-3 and gave no false positive results in analysis of heterologous microorganisms in concentration of 1.0 x 108 mkxcm-3.
MeSH term(s)	Animals ; Antibodies, Bacterial/chemistry ; Antibodies, Monoclonal, Murine-Derived/chemistry ; Chromatography, Affinity/methods ; Enzyme-Linked Immunosorbent Assay/methods ; Francisella tularensis ; Humans ; Mice ; Sensitivity and Specificity ; Tularemia/diagnosis
Chemical Substances	Antibodies, Bacterial ; Antibodies, Monoclonal, Murine-Derived
Language	Russian
Publishing date	2016-08-08
Publishing country	Russia (Federation)
Document type	Journal Article
ZDB-ID	1155086-7
ISSN	0869-2084
ISSN	0869-2084
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Article: INSL3/LGR8 role in testicular descent and cryptorchidism.

Bogatcheva, N V / Agoulnik, A I

Reproductive biomedicine online

2005 Volume 10, Issue 1, Page(s) 49–54

Abstract: Cryptorchidism, generally referred to a failure of testicular descent into the scrotum, is the most frequent (up to 3-4% at birth) congenital anomaly in newborn boys. Cryptorchidism is closely associated with impaired fertility, and represents an ... ...

Abstract	Cryptorchidism, generally referred to a failure of testicular descent into the scrotum, is the most frequent (up to 3-4% at birth) congenital anomaly in newborn boys. Cryptorchidism is closely associated with impaired fertility, and represents an established risk factor for testicular cancer. Like other genital defects, cryptorchidism is believed to be caused by either endocrine or genetic abnormalities, or both. Recent elucidation of the molecular mechanism of the rodent testicular descent, and, in particular, the critical role of Insl3 (insulin-like 3) and its receptor Great/Lgr8 encouraged the search for naturally occurring mutations in the human homologues of these genes in the affected patient population. Genetic analysis revealed several functionally deleterious mutations in both INSL3 and GREAT/LGR8 genes. However, although some of mutations were found only in cryptorchid patients, it remains to be verified whether there is a causative link between the presence of mutations in INSL3 or GREAT/LGR8 and the undescended testis phenotype in men. The data and analysis of published studies indicate that mutations in these two genes might account for only a small portion of all cases of this disease in the human population.
MeSH term(s)	Cryptorchidism/metabolism ; Humans ; Infertility, Male/genetics ; Infertility, Male/metabolism ; Insulin/genetics ; Insulin/metabolism ; Male ; Mutation ; Proteins/genetics ; Proteins/metabolism ; Testis/anatomy & histology ; Testis/physiology
Chemical Substances	Insulin ; Leydig insulin-like protein ; Proteins
Language	English
Publishing date	2005-02-02
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2113823-0
ISSN	1472-6491 ; 1472-6483
ISSN (online)	1472-6491
ISSN	1472-6483
DOI	10.1016/s1472-6483(10)60803-6
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Article ; Online: Distinct Factors Secreted by Adipose Stromal Cells Protect the Endothelium From Barrier Dysfunction and Apoptosis

Hongyan Lu / Stephanie Merfeld-Clauss / Yameena Jawed / Keith L. March / Michael E. Coleman / Natalia V. Bogatcheva

Frontiers in Cell and Developmental Biology, Vol

2020 Volume 8

Abstract: ... apoptosis in endothelium is c-Jun N-terminal kinase (JNK)-dependent, and JNK activation is inhibited by ASC ...

Abstract	We have shown previously that adipose stromal cell (ASC)-derived conditioned media (CM) limited lung injury, endothelial barrier dysfunction, and apoptosis. Here, we used endothelial hyperpermeability and apoptosis assays to investigate how concentration processes affect endothelium-directed bioactivity of ASC-CM and to gain information on the nature of bioactive factors. Comparison of ASC-CM concentrated with differential molecular weight (MW) cutoff filters showed that endothelial barrier protection depended on the species-specific factors in ASC-CM fractionated with MW > 50 kDa. Known barrier regulators—keratin growth factor (KGF), vascular endothelial growth factor (VEGF), and hepatocyte growth factor (HGF)—were detected in ASC-CM fraction of > 100 kDa. Pretreatment of endothelial monolayers with concentrations of KGF, VEGF, and HGF detected in ASC-CM showed that only KGF and HGF protect the endothelium from barrier dysfunction. Depletion of KGF and HGF from ASC-CM attenuated ASC-CM’s ability to protect the endothelial barrier. In contrast to barrier-protective factors, apoptosis-protective factors fractionated with MW < 3 kDa and were not species-specific. Application of donors of apoptosis-mitigating gases showed that the CO donor carbon monoxide-releasing molecule 2 (CORM2) protected the endothelium from apoptosis, while the H2S donor NaSH did not. Knockdown of CO-generating heme oxygenase 1 in ASC attenuated ASC-CM’s ability to protect the endothelium from apoptosis. We have shown that tumor necrosis factor alpha (TNFα)-induced apoptosis in endothelium is c-Jun N-terminal kinase (JNK)-dependent, and JNK activation is inhibited by ASC-CM pretreatment of endothelial cells. ASC-CM from heme oxygenase 1-depleted ASC displayed attenuated ability to suppress endothelial JNK activation, suggesting that CO-mediated protection of the endothelium from apoptosis is achieved by the downregulation of the JNK pathway. Altogether, our results demonstrate that the concentration of ASC-CM with low MW cutoff ...
Keywords	ASC ; conditioned media ; endothelial cells ; barrier dysfunction ; apoptosis ; Biology (General) ; QH301-705.5
Subject code	610
Language	English
Publishing date	2020-09-01T00:00:00Z
Publisher	Frontiers Media S.A.
Document type	Article ; Online
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Article: Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins.

Gusev, N B / Bogatcheva, N V / Marston, S B

Biochemistry. Biokhimiia

2002 Volume 67, Issue 5, Page(s) 511–519

Abstract: The modern classification of small heat shock proteins (sHsp) is presented and peculiarities of their primary structure and the mechanism of formation of oligomeric complexes are described. Data on phosphorylation of sHsp by different protein kinases are ...

Abstract	The modern classification of small heat shock proteins (sHsp) is presented and peculiarities of their primary structure and the mechanism of formation of oligomeric complexes are described. Data on phosphorylation of sHsp by different protein kinases are presented and the effect of phosphorylation on oligomeric state and chaperone activity of sHsp is discussed. Intracellular location of sHsp under normal and stress conditions is described and it is emphasized that under certain condition sHsp interact with different elements of cytoskeleton. The literature concerning the effect of sHsp on polymerization of actin in vitro is analyzed. An attempt is made to compare effects of sHsp on polymerization of actin in vitro with the results obtained on living cells under normal conditions and after heat shock or hormone action. The literature concerning possible effects of sHsp on cell motility is also analyzed.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cell Movement ; Cytoskeletal Proteins/metabolism ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/metabolism ; Humans ; Muscles/physiology ; Phosphorylation ; Protein Structure, Quaternary
Chemical Substances	Cytoskeletal Proteins ; Heat-Shock Proteins
Language	English
Publishing date	2002-01-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1109-5
ISSN	1608-3040 ; 0006-2979 ; 0320-9717
ISSN (online)	1608-3040
ISSN	0006-2979 ; 0320-9717
DOI	10.1023/a:1015549725819
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Article: Role of tyrosine kinase signaling in endothelial cell barrier regulation.

Bogatcheva, Natalia V / Garcia, Joe G N / Verin, Alexander D

Vascular pharmacology

2003 Volume 39, Issue 4-5, Page(s) 201–212

Abstract: Phosphorylation of proteins on tyrosine acts as a reversible and specific trigger mechanism, forming or disrupting regulatory connections between proteins. Tyrosine kinases and phosphatases participate in multiple cellular processes, and considerable ... ...

Abstract	Phosphorylation of proteins on tyrosine acts as a reversible and specific trigger mechanism, forming or disrupting regulatory connections between proteins. Tyrosine kinases and phosphatases participate in multiple cellular processes, and considerable evidence now supports a role for tyrosine phosphorylation in vascular permeability. A semipermeable barrier between the vascular compartment and the interstitium is maintained by the integrity of endothelial monolayer, controlling movement of fluids, macromolecules and leucocytes. Barrier function is regulated by the adjustment of paracellular gaps between endothelial cells (ECs) by two antagonistic forces, centripetal cytoskeletal tension and opposing cell-cell and cell-matrix adhesion forces. Both cytoskeletal filaments and adhesion sites are intimately linked in complex machinery which is regulated by multiple signaling events including protein phosphorylation and/or protein translocation to specific intracellular positions. Tyrosine kinases occupy key positions in the mechanism controlling cell responses mediated through various cell surface receptors, which use tyrosine phosphorylation to transduce extracellular signal.
MeSH term(s)	Animals ; Cell Adhesion Molecules/metabolism ; Cell Membrane Permeability/physiology ; Cytoskeleton/physiology ; Endothelium, Vascular/enzymology ; Endothelium, Vascular/metabolism ; Endothelium, Vascular/physiology ; Humans ; Intercellular Junctions/physiology ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Signal Transduction/physiology
Chemical Substances	Cell Adhesion Molecules ; Protein-Tyrosine Kinases (EC 2.7.10.1)
Language	English
Publishing date	2003-04-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	2082846-9
ISSN	1537-1891 ; 1537-1891 ; 1879-3649
ISSN (online)	1537-1891
ISSN	1537-1891 ; 1879-3649
DOI	10.1016/s1537-1891(03)00009-0
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Article: Molecular mechanisms of thrombin-induced endothelial cell permeability.

Bogatcheva, N V / Garcia, J G N / Verin, A D

Biochemistry. Biokhimiia

2002 Volume 67, Issue 1, Page(s) 75–84

Abstract: Confluent endothelium serves as a selective barrier between the vascular space of blood vessels and underlying tissues. Compromised barrier function of the endothelium in response to inflammation mediators, such as thrombin, is accompanied by reversible ... ...

Abstract	Confluent endothelium serves as a selective barrier between the vascular space of blood vessels and underlying tissues. Compromised barrier function of the endothelium in response to inflammation mediators, such as thrombin, is accompanied by reversible cell rounding and interendothelial gap formation. Endothelial barrier integrity substantially depends on the cytoskeleton, which ensures actin stress fiber formation and via actomyosin-driven contraction regulates cell shape and adhesion. Recent studies have shown the sequence of events that mediate signal transduction in endothelial cells. Binding of thrombin with its receptor initiates activation of heterotrimeric G-proteins, which, in turn, entails a decrease in cAMP level in the cell, increase in intracellular Ca2+ and diacylglycerol concentration, and activation of the small G-protein Rho. Phosphorylation of myosin light chains as a result of activation of myosin light chain kinase and inactivation of myosin phosphatases stimulates stress fiber formation and triggers actomyosin contraction. In addition, thrombin-induced rearrangement in the endothelial cytoskeleton is regulated by Ca2+/calmodulin-dependent protein kinase, protein kinase C, and tyrosine protein kinases. This review focuses on presently known biochemical mechanisms of cell response to thrombin and their role in endothelial barrier dysfunction.
MeSH term(s)	Animals ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cyclic AMP/metabolism ; Diglycerides/metabolism ; Endothelium/metabolism ; Endothelium, Vascular/metabolism ; Humans ; Inositol 1,4,5-Trisphosphate/metabolism ; Myosin Light Chains/metabolism ; Myosins/metabolism ; Permeability ; Phosphorylation ; Protein Kinase C/metabolism ; Protein-Tyrosine Kinases/metabolism ; Thrombin/metabolism
Chemical Substances	Diglycerides ; Myosin Light Chains ; Inositol 1,4,5-Trisphosphate (85166-31-0) ; Cyclic AMP (E0399OZS9N) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Protein Kinase C (EC 2.7.11.13) ; Calcium-Calmodulin-Dependent Protein Kinases (EC 2.7.11.17) ; Thrombin (EC 3.4.21.5) ; Myosins (EC 3.6.4.1) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2002-01-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
ZDB-ID	1109-5
ISSN	1608-3040 ; 0006-2979 ; 0320-9717
ISSN (online)	1608-3040
ISSN	0006-2979 ; 0320-9717
DOI	10.1023/a:1013904231324
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Article: Interaction of smooth muscle calponin with phospholipids.

Bogatcheva, N V / Gusev, N B

FEBS letters

1995 Volume 371, Issue 2, Page(s) 123–126

Abstract: ... in the short (13 kDa) N-terminal chymotryptic peptide of calponin. The apparent dissociation constant ...

Abstract	Analyzing the primary structure we predicted that calponin may interact with phospholipids. In order to check this suggestion we investigated the interaction of calponin with phospholipids by ultracentrifugation, light scattering, vesicles leakage and differential scanning calorimetry. In agreement with our prediction calponin interacts with acidic phospholipids and the phospholipid-binding site was located in the short (13 kDa) N-terminal chymotryptic peptide of calponin. The apparent dissociation constant of calponin-phospholipids complex was less than 0.2 microM and calmodulin competes with phospholipids for calponin binding. Although the interaction of calponin with phospholipids decreases at high ionic strength, calponin binds phospholipids even in the presence of 100-150 mM of the salt. Under certain conditions calponin induced leakage of phospholipid vesicles and affected the cooperativity of lipid phase transition. It is concluded that both electrostatic and hydrophobic interactions provide for calponin-phospholipid complex formation.
MeSH term(s)	Animals ; Binding Sites ; Binding, Competitive ; Calcium-Binding Proteins/metabolism ; Calcium-Binding Proteins/pharmacology ; Calmodulin/metabolism ; Calmodulin/pharmacology ; Calorimetry, Differential Scanning ; Chymotrypsin/metabolism ; Ducks ; Gizzard, Avian/chemistry ; Hydrogen-Ion Concentration ; Light ; Liposomes/metabolism ; Microfilament Proteins ; Muscle, Smooth/chemistry ; Osmolar Concentration ; Peptide Fragments/metabolism ; Phospholipids/metabolism ; Scattering, Radiation ; Ultracentrifugation ; Calponins
Chemical Substances	Calcium-Binding Proteins ; Calmodulin ; Liposomes ; Microfilament Proteins ; Peptide Fragments ; Phospholipids ; Chymotrypsin (EC 3.4.21.1)
Language	English
Publishing date	1995-09-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/0014-5793(95)00868-a
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Article: Computer-assistant prediction of phospholipid binding sites of caldesmon and calponin.

Bogatcheva, N V / Gusev, N B

FEBS letters

1995 Volume 363, Issue 3, Page(s) 269–272

Abstract: ... phospholipid binding sites is located in the sequence 628-658 [Bogatcheva et al. (1994) FEBS Lett. 342, 176 ...

Abstract	The primary structure of smooth muscle caldesmon and calponin was screened for the presence of amphiphilic alpha-helices which can participate in the formation of protein-lipid contacts. Only one caldesmon segment (residues 645-660) having a predominantly alpha-helical structure and high hydrophobic moment satisfies all criteria for a surface-seeking helix and is predicted to be involved in the caldesmon-phospholipid interaction. This prediction agrees with experimental results indicating that one of the caldesmon-phospholipid binding sites is located in the sequence 628-658 [Bogatcheva et al. (1994) FEBS Lett. 342, 176]. Two segments of calponin (residues 45-55 and 85-95) exhibit high hydrophobic moments and the sequence 85-95 is characterized by a high probability of alpha-helix formation. This may suggest that at least one of these segments could facilitate the calponin-phospholipid interaction and that calponin, as with many other actin binding proteins, is able to interact with membranes.
MeSH term(s)	Binding Sites ; Calcium-Binding Proteins/metabolism ; Calmodulin-Binding Proteins/metabolism ; Microfilament Proteins ; Muscle Proteins/metabolism ; Phospholipids/metabolism ; Protein Structure, Secondary ; Software ; Solubility ; Calponins
Chemical Substances	Calcium-Binding Proteins ; Calmodulin-Binding Proteins ; Microfilament Proteins ; Muscle Proteins ; Phospholipids
Language	English
Publishing date	1995-04-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/0014-5793(95)00328-7
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