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Article ; Online: Nitrosylation of tissue transglutaminase enhances fibroblast migration and regulates MMP activation.

Kurt-Celep, İnci / Nihan Kilinc, Ayse / Griffin, Martin / Telci, Dilek

Matrix biology : journal of the International Society for Matrix Biology

2021 Volume 105, Page(s) 1–16

Abstract: In wound healing, the TG2 enzyme plays a dual functional role. TG2 has been shown to regulate extracellular matrix (ECM) stabilization by its transamidase activity while increasing cell migration by acting as a cell adhesion molecule. In this process, ... ...

Abstract	In wound healing, the TG2 enzyme plays a dual functional role. TG2 has been shown to regulate extracellular matrix (ECM) stabilization by its transamidase activity while increasing cell migration by acting as a cell adhesion molecule. In this process, nitric oxide (NO) plays a particularly important role by nitrosylation of free cysteine residues on TG2, leading to the irreversible inactivation of the catalytic activity. In this study, transfected fibroblasts expressing TG2 under the control of the tetracycline-off promoter were treated with NO donor S-nitroso-N-acetyl penicillamine (SNAP) to analyze the interplay between NO and TG2 in the regulation of cell migration/invasion as well as TGF-β1-dependent MMP activation. Our results demonstrated that inhibition of TG2 cross-linking activity by SNAP promoted the migration and invasion capacity of fibroblasts by hindering TG2-mediated TGF-β1 activation. While the inhibition of TG2 activity by NO downregulated the biosynthesis and activity of MMP-2 and MMP-9, that of MMP-1a and MMP-13 was shown to be upregulated in a TGF-β1-dependent manner under the same conditions. In the presence of SNAP, interaction of TG2 with its cell surface binding partners Integrin-β1 and Syndecan-4 was reduced, which was paralleled by an increase in TG2 and PDGF association. These findings suggests that migratory phenotype of fibroblasts can be regulated by the interplay between nitric oxide and TG2 activity.
MeSH term(s)	Cell Movement ; Fibroblasts/metabolism ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism ; Protein Glutamine gamma Glutamyltransferase 2 ; Transglutaminases/genetics ; Transglutaminases/metabolism
Chemical Substances	Protein Glutamine gamma Glutamyltransferase 2 (EC 2.3.2.13) ; Transglutaminases (EC 2.3.2.13) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2021-11-09
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1183793-7
ISSN	1569-1802 ; 0945-053X
ISSN (online)	1569-1802
ISSN	0945-053X
DOI	10.1016/j.matbio.2021.10.005
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Article ; Online: Transglutaminase 2: a novel therapeutic target for idiopathic pulmonary fibrosis using selective small molecule inhibitors.

Fell, Shaun / Wang, Zhuo / Blanchard, Andy / Nanthakumar, Carmel / Griffin, Martin

Amino acids

2021 Volume 53, Issue 2, Page(s) 205–217

Abstract: This study investigates the effects of a site-directed TG2-selective inhibitor on the lung myofibroblast phenotype and ECM deposition to elucidate TG2 as a novel therapeutic target in idiopathic pulmonary fibrosis (IPF)-an incurable progressive fibrotic ... ...

Abstract	This study investigates the effects of a site-directed TG2-selective inhibitor on the lung myofibroblast phenotype and ECM deposition to elucidate TG2 as a novel therapeutic target in idiopathic pulmonary fibrosis (IPF)-an incurable progressive fibrotic disease. IPF fibroblasts showed increased expression of TG2, α smooth muscle actin (αSMA) and fibronectin (FN) with increased extracellular TG2 and transforming growth factor β1 (TGFβ1) compared to normal human lung fibroblasts (NHLFs) which do not express αSMA and express lower levels of FN. The myofibroblast phenotype shown by IPF fibroblasts could be reversed by selective TG2 inhibition with a reduction in matrix FN and TGFβ1 deposition. TG2 transduction or TGFβ1 treatment of NHLFs led to a comparable phenotype to that of IPF fibroblasts which was reversible following selective TG2 inhibition. Addition of exogenous TG2 to NHLFs also induced the myofibroblast phenotype by a mechanism involving TGFβ1 activation which could be ameliorated by selective TG2 inhibition. SMAD3-deleted IPF fibroblasts via CRISPR-cas9 genome editing, showed reduced TG2 protein levels following TGFβ1 stimulation. This study demonstrates a key role for TG2 in the induction of the myofibroblast phenotype and shows the potential for TG2-selective inhibitors as therapeutic agents for the treatment of fibrotic lung diseases like IPF.
MeSH term(s)	Actins/genetics ; Actins/metabolism ; Enzyme Inhibitors/pharmacology ; Fibronectins/genetics ; Fibronectins/metabolism ; GTP-Binding Proteins/antagonists & inhibitors ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism ; Humans ; Idiopathic Pulmonary Fibrosis/drug therapy ; Idiopathic Pulmonary Fibrosis/genetics ; Idiopathic Pulmonary Fibrosis/metabolism ; Myofibroblasts/drug effects ; Myofibroblasts/metabolism ; Smad3 Protein/genetics ; Smad3 Protein/metabolism ; Transforming Growth Factor beta1/genetics ; Transforming Growth Factor beta1/metabolism ; Transglutaminases/antagonists & inhibitors ; Transglutaminases/genetics ; Transglutaminases/metabolism
Chemical Substances	ACTA2 protein, human ; Actins ; Enzyme Inhibitors ; Fibronectins ; SMAD3 protein, human ; Smad3 Protein ; TGFB1 protein, human ; Transforming Growth Factor beta1 ; transglutaminase 2 (EC 2.3.2.-) ; Transglutaminases (EC 2.3.2.13) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2021-01-21
Publishing country	Austria
Document type	Journal Article
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-020-02938-w
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Article ; Online: Biochemical and Functional Characterization of the Three Zebrafish Transglutaminases 2.

Lisetto, Manuel / Fattorini, Mariagiulia / Lanza, Andrea / Gerdol, Marco / Griffin, Martin / Wang, Zhuo / Ferrara, Fortunato / Sblattero, Daniele

International journal of molecular sciences

2023 Volume 24, Issue 15

Abstract: Transglutaminase 2 (TG2) is a multifunctional protein widely distributed in various tissues and involved in many physiological and pathological processes. However, its actual role in biological processes is often controversial as TG2 shows different ... ...

Abstract	Transglutaminase 2 (TG2) is a multifunctional protein widely distributed in various tissues and involved in many physiological and pathological processes. However, its actual role in biological processes is often controversial as TG2 shows different effects in these processes depending on its localization, cell type, or experimental conditions. We characterized the enzymatic and functional properties of TG2 proteins expressed in Danio rerio (zebrafish) to provide the basis for using this established animal model as a reliable tool to characterize TG2 functions in vivo. We confirmed the existence of three genes orthologous to human TG2 (zTGs2) in the zebrafish genome and their expression and function during embryonic development. We produced and purified the zTGs2s as recombinant proteins and showed that, like the human enzyme, zTGs2 catalyzes a Ca
MeSH term(s)	Animals ; Humans ; Apoptosis/genetics ; Catalysis ; Cell Adhesion ; Fibroblasts ; Gene Expression ; HEK293 Cells ; Phylogeny ; Protein Conformation ; Protein Glutamine gamma Glutamyltransferase 2/chemistry ; Protein Glutamine gamma Glutamyltransferase 2/classification ; Protein Glutamine gamma Glutamyltransferase 2/genetics ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Zebrafish/genetics ; Zebrafish/metabolism ; Zebrafish Proteins/chemistry ; Zebrafish Proteins/classification ; Zebrafish Proteins/genetics
Chemical Substances	Protein Glutamine gamma Glutamyltransferase 2 (EC 2.3.2.13) ; Recombinant Proteins ; TGM2 protein, human ; Zebrafish Proteins
Language	English
Publishing date	2023-07-27
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms241512041
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Article: Transglutaminase 2: a novel therapeutic target for idiopathic pulmonary fibrosis using selective small molecule inhibitors

Fell, Shaun / Wang, Zhuo / Blanchard, Andy / Nanthakumar, Carmel / Griffin, Martin

Amino acids. 2021 Feb., v. 53, no. 2

2021

Abstract	This study investigates the effects of a site-directed TG2-selective inhibitor on the lung myofibroblast phenotype and ECM deposition to elucidate TG2 as a novel therapeutic target in idiopathic pulmonary fibrosis (IPF)—an incurable progressive fibrotic disease. IPF fibroblasts showed increased expression of TG2, α smooth muscle actin (αSMA) and fibronectin (FN) with increased extracellular TG2 and transforming growth factor β1 (TGFβ1) compared to normal human lung fibroblasts (NHLFs) which do not express αSMA and express lower levels of FN. The myofibroblast phenotype shown by IPF fibroblasts could be reversed by selective TG2 inhibition with a reduction in matrix FN and TGFβ1 deposition. TG2 transduction or TGFβ1 treatment of NHLFs led to a comparable phenotype to that of IPF fibroblasts which was reversible following selective TG2 inhibition. Addition of exogenous TG2 to NHLFs also induced the myofibroblast phenotype by a mechanism involving TGFβ1 activation which could be ameliorated by selective TG2 inhibition. SMAD3-deleted IPF fibroblasts via CRISPR-cas9 genome editing, showed reduced TG2 protein levels following TGFβ1 stimulation. This study demonstrates a key role for TG2 in the induction of the myofibroblast phenotype and shows the potential for TG2-selective inhibitors as therapeutic agents for the treatment of fibrotic lung diseases like IPF.
Keywords	CRISPR-Cas systems ; actin ; fibroblasts ; fibronectins ; genome ; humans ; lungs ; phenotype ; protein-glutamine gamma-glutamyltransferase ; pulmonary fibrosis ; smooth muscle ; therapeutics
Language	English
Dates of publication	2021-02
Size	p. 205-217.
Publishing place	Springer Vienna
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-020-02938-w
Database	NAL-Catalogue (AGRICOLA)

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Article: Corrigendum:

Pinton, Giulia / Wang, Zhuo / Balzano, Cecilia / Missaglia, Sara / Tavian, Daniela / Boldorini, Renzo / Fennell, Dean A / Griffin, Martin / Moro, Laura

Frontiers in oncology

2022 Volume 12, Page(s) 1081632

Abstract: This corrects the article DOI: 10.3389/fonc.2021.678447.]. ...

Abstract	[This corrects the article DOI: 10.3389/fonc.2021.678447.].
Language	English
Publishing date	2022-11-23
Publishing country	Switzerland
Document type	Published Erratum
ZDB-ID	2649216-7
ISSN	2234-943X
ISSN	2234-943X
DOI	10.3389/fonc.2022.1081632
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Article ; Online: Transglutaminase 2 maintains a colorectal cancer stem phenotype by regulating epithelial-mesenchymal transition.

Ayinde, Oluseyi / Wang, Zhuo / Pinton, Giulia / Moro, Laura / Griffin, Martin

Oncotarget

2019 Volume 10, Issue 44, Page(s) 4556–4569

Abstract: Transglutaminase 2 (TG2), a multifunctional protein, is reported in regulating the cancer stem cell (CSC) phenotype in various cancers. Our previous work suggested the link between TG2 and Epithelial-Mesenchymal Transition (EMT) in colorectal cancer (CRC) ...

Abstract	Transglutaminase 2 (TG2), a multifunctional protein, is reported in regulating the cancer stem cell (CSC) phenotype in various cancers. Our previous work suggested the link between TG2 and Epithelial-Mesenchymal Transition (EMT) in colorectal cancer (CRC). Here we demonstrate the importance of TG2 in CSC development in human CRC cell lines HCT116 and SW620. CRC spheroid cells showed increased CSC characteristics over their monolayer cells with increased expression of CD44 and over expression of Oct3/4, Sox2 and Nanog. They also showed increased EMT and invasiveness, and enhanced expression of TG2. TG2 inhibition by its selective inhibitor 1-155 reduced both spheroid formation and invasive potential of the spheroid cells. β-catenin, a mediator of stem cell maintenance, was overexpressed in the spheroid cells and could be attenuated by TG2 inhibition. Spheroid cells possessed increased angiogenesis stimulating ability via overexpression of Vascular Endothelial Growth Factor (VEGF). Increased VEGF was present in the culture media from spheroid cells when compared to monolayer cultures which could be reduced by selective inhibition by 1-155. Stemness and malignancy in the colorectal spheroid cells was associated with increased TG2, EMT, β-catenin and VEGF. Here we demonstrate that inhibiting TG2 reduces both stemness and angiogenic stimulating activity in CRC.
Language	English
Publishing date	2019-07-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.27062
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Tissue transglutaminase induces Epithelial-Mesenchymal-Transition and the acquisition of stem cell like characteristics in colorectal cancer cells.

Ayinde, Oluseyi / Wang, Zhuo / Griffin, Martin

Oncotarget

2017 Volume 8, Issue 12, Page(s) 20025–20041

Abstract: Human colon cancer cell lines (CRCs) RKO, SW480 and SW620 were investigated for TG2 involvement in tumour advancement and aggression. TG2 expression correlated with tumour advancement and expression of markers of epithelial-mesenchymal transition (EMT). ... ...

Abstract	Human colon cancer cell lines (CRCs) RKO, SW480 and SW620 were investigated for TG2 involvement in tumour advancement and aggression. TG2 expression correlated with tumour advancement and expression of markers of epithelial-mesenchymal transition (EMT). The metastatic cell line SW620 showed high TG2 expression compared to the primary tumour cell lines SW480 and RKO and could form tumour spheroids under non- adherent conditions. TG2 manipulation in the CRCs by shRNA or TG2 transduction confirmed the relationship between TG2 and EMT. TGFβ1 expression in CRC cells, and its level in the cell medium and extracellular matrix was increased in primary tumour CRCs overexpressing TG2 and could regulate TG2 expression and EMT by both canonical (RKO) and non-canonical (RKO and SW480) signalling. TGFβ1 regulation was not observed in the metastatic SW620 cell line, but TG2 knockdown or inhibition in SW620 reversed EMT. In SW620, TG2 expression and EMT was associated with increased presence of nuclear β-catenin which could be mediated by association of TG2 with the Wnt signalling co-receptor LRP5. TG2 inhibition/knockdown increased interaction between β-catenin and ubiquitin shown by co-immunoprecipitation, suggesting that TG2 could be important in β-catenin regulation. β-Catenin and TG2 was also upregulated in SW620 spheroid cells enriched with cancer stem cell marker CD44 and TG2 inhibition/knockdown reduced the spheroid forming potential of SW620 cells. Our data suggests that TG2 could hold both prognostic and therapeutic significance in colon cancer.
MeSH term(s)	Apoptosis ; Biomarkers, Tumor/genetics ; Biomarkers, Tumor/metabolism ; Cell Proliferation ; Colorectal Neoplasms/enzymology ; Colorectal Neoplasms/pathology ; Epithelial-Mesenchymal Transition ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation, Neoplastic ; Humans ; Neoplastic Stem Cells/metabolism ; Neoplastic Stem Cells/pathology ; Transforming Growth Factor beta1/genetics ; Transforming Growth Factor beta1/metabolism ; Transglutaminases/metabolism ; Tumor Cells, Cultured ; Wnt Signaling Pathway ; beta Catenin/genetics ; beta Catenin/metabolism
Chemical Substances	Biomarkers, Tumor ; TGFB1 protein, human ; Transforming Growth Factor beta1 ; beta Catenin ; transglutaminase 2 (EC 2.3.2.-) ; Transglutaminases (EC 2.3.2.13) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2017-03-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.15370
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Article ; Online: The role of TG2 in regulating S100A4-mediated mammary tumour cell migration.

Wang, Zhuo / Griffin, Martin

PloS one

2013 Volume 8, Issue 3, Page(s) e57017

Abstract: The importance of S100A4, a Ca(2+)-binding protein, in mediating tumour cell migration, both intracellularly and extracellularly, is well documented. Tissue transglutaminase (TG2) a Ca(2+)-dependent protein crosslinking enzyme, has also been shown to ... ...

Abstract	The importance of S100A4, a Ca(2+)-binding protein, in mediating tumour cell migration, both intracellularly and extracellularly, is well documented. Tissue transglutaminase (TG2) a Ca(2+)-dependent protein crosslinking enzyme, has also been shown to enhance cell migration. Here by using the well characterised non-metastatic rat mammary R37 cells (transfected with empty vector) and highly metastatic KP1 cells (R37 cells transfected with S100A4), we demonstrate that inhibition of TG2 either by TG2 inhibitors or transfection of cells with TG2 shRNA block S100A4-accelerated cell migration in the KP1cells and in R37 cells treated with exogenous S100A4. Cell migration was also blocked by the treatment with the non-cell permeabilizing TG2 inhibitor R294, in the human breast cancer cell line MDA-MB-231 (Clone 16, which has a high level of TG2 expression). Inhibition was paralleled by a decrease in S100A4 polymer formation. In vitro co-immunoprecipitation and Far Western blotting assays and cross-linking assays showed not only the direct interaction between TG2 and S100A4, but also confirmed S100A4 as a substrate for TG2. Using specific functional blocking antibodies, a targeting peptide and a recombinant protein as a competitive treatment, we revealed the involvement of syndecan-4 and α5β1 integrin co-signalling pathways linked by activation of PKCα in this TG2 and S100A4-mediated cell migration. We propose a mechanism for TG2-regulated S100A4-related mediated cell migration, which is dependent on TG2 crosslinking.
MeSH term(s)	Animals ; Cell Line, Tumor ; Cell Migration Inhibition/drug effects ; Cell Movement/drug effects ; Enzyme Inhibitors/pharmacology ; GTP-Binding Proteins/antagonists & inhibitors ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation, Neoplastic/drug effects ; Integrin alpha5beta1/genetics ; Integrin alpha5beta1/metabolism ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Mammary Neoplasms, Animal/genetics ; Mammary Neoplasms, Animal/metabolism ; Peptides/pharmacology ; Protein Kinase C-alpha/genetics ; Protein Kinase C-alpha/metabolism ; RNA, Small Interfering/genetics ; Rats ; S100 Calcium-Binding Protein A4 ; S100 Proteins/genetics ; S100 Proteins/metabolism ; Signal Transduction/drug effects ; Syndecan-4/genetics ; Syndecan-4/metabolism ; Transglutaminases/antagonists & inhibitors ; Transglutaminases/genetics ; Transglutaminases/metabolism
Chemical Substances	Enzyme Inhibitors ; Integrin alpha5beta1 ; Isoenzymes ; Peptides ; RNA, Small Interfering ; S100 Calcium-Binding Protein A4 ; S100 Proteins ; S100a4 protein, rat ; Sdc4 protein, rat ; Syndecan-4 ; transglutaminase 2 (EC 2.3.2.-) ; Transglutaminases (EC 2.3.2.13) ; Protein Kinase C-alpha (EC 2.7.11.13) ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2013-03-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0057017
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Article: CDKN2A

Pinton, Giulia / Wang, Zhuo / Balzano, Cecilia / Missaglia, Sara / Tavian, Daniela / Boldorini, Renzo / Fennell, Dean A / Griffin, Martin / Moro, Laura

Frontiers in oncology

2021 Volume 11, Page(s) 678447

Abstract: Malignant pleural mesothelioma is an aggressive cancer, heterogeneous in its presentation and behaviour. Despite an increasing knowledge about molecular markers and their diagnostic and prognostic value, they are not used as much as they might be for ... ...

Abstract	Malignant pleural mesothelioma is an aggressive cancer, heterogeneous in its presentation and behaviour. Despite an increasing knowledge about molecular markers and their diagnostic and prognostic value, they are not used as much as they might be for treatment allocation. It has been recently reported that mesothelioma cells that lack BAP1 (BRCA1 Associated Protein) are sensitive to inhibition of the EZH2 (Enhancer of Zeste Homolog 2) histone methyltransferase. Since we observed strong H3K27me3 (histone H3 lysine 27 trimetylation) immunoreactivity in BAP1 wild-type mesothelioma biopsies, we decided to characterize
Language	English
Publishing date	2021-07-01
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2649216-7
ISSN	2234-943X
ISSN	2234-943X
DOI	10.3389/fonc.2021.678447
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Article ; Online: TG2, a novel extracellular protein with multiple functions.

Wang, Zhuo / Griffin, Martin

Amino acids

2012 Volume 42, Issue 2-3, Page(s) 939–949

Abstract: TG2 is multifunctional enzyme which can be secreted to the cell surface by an unknown mechanism where its Ca(2+)-dependent transamidase activity is implicated in a number of events important to cell behaviour. However, this activity may only be transient ...

Abstract	TG2 is multifunctional enzyme which can be secreted to the cell surface by an unknown mechanism where its Ca(2+)-dependent transamidase activity is implicated in a number of events important to cell behaviour. However, this activity may only be transient due to the oxidation of the enzyme in the extracellular environment including its reaction with NO probably accounting for its many other roles, which are transamidation independent. In this review, we discuss the novel roles of TG2 at the cell surface and in the ECM acting either as a transamidating enzyme or as an extracellular scaffold protein involved in cell adhesion. Such roles include its ability to act as an FN co-receptor for β integrins or in a heterocomplex with FN interacting with the cell surface heparan sulphate proteoglycan syndecan-4 leading to activation of PKCα. These different properties of TG2 involve this protein in various physiological processes, which if not regulated appropriately can also lead to its involvement in a number of diseases. These include metastatic cancer, tissue fibrosis and coeliac disease, thus increasing its attractiveness as both a therapeutic target and diagnostic marker.
MeSH term(s)	Amides/metabolism ; Calcium/metabolism ; Enzyme Activation ; Extracellular Matrix/metabolism ; GTP-Binding Proteins ; Heparan Sulfate Proteoglycans/metabolism ; Humans ; Matrix Metalloproteinases/metabolism ; Protein Kinase C-alpha/metabolism ; Structure-Activity Relationship ; Transglutaminases/chemistry ; Transglutaminases/metabolism ; Transglutaminases/physiology
Chemical Substances	Amides ; Heparan Sulfate Proteoglycans ; transglutaminase 2 (EC 2.3.2.-) ; Transglutaminases (EC 2.3.2.13) ; Protein Kinase C-alpha (EC 2.7.11.13) ; Matrix Metalloproteinases (EC 3.4.24.-) ; GTP-Binding Proteins (EC 3.6.1.-) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2012-02
Publishing country	Austria
Document type	Journal Article ; Review
ZDB-ID	1121341-3
ISSN	1438-2199 ; 0939-4451
ISSN (online)	1438-2199
ISSN	0939-4451
DOI	10.1007/s00726-011-1008-x
Database	MEDical Literature Analysis and Retrieval System OnLINE

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