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MST1 (macrophage stimulating 1 (hepatocyte growth factor-like))

Written2013-05Makiko Kawaguchi, Hiroaki Kataoka
Section of Oncopathology, Regenerative Biology, Department of Pathology, Faculty of Medicine, University of Miyazaki, Japan

(Note : for Links provided by Atlas : click)

Identity

Alias_namesD3F15S2
HGFL
DNF15S2
hepatocyte growth factor-like
Alias_symbol (synonym)MSP
NF15S2
Other alias
HGNC (Hugo) MST1
LocusID (NCBI) 4485
Atlas_Id 44411
Location 3p21.31  [Link to chromosome band 3p21]
Location_base_pair Starts at 49683947 and ends at 49688763 bp from pter ( according to hg19-Feb_2009)  [Mapping MST1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
MST1 (3p21.31) / SRRD (22q12.1)MST1L (1p36.13) / MST1 (3p21.31)

DNA/RNA

 
  Structure of the human MST1 gene.
Description Total length: 4817 bp; mRNA product length: 2348 bp.
Transcription The human MST1 gene structure consists of 18 exons and 17 introns spanning 4817 bp. One transcript of 2348 bps mRNA encode for 711 amino acid.
Pseudogene There are no known pseudogenes.

Protein

Note MSP was originally identified by E.J. Leonard as a serum protein that activates murine resident peritoneal macrophages (Skeel et al., 1991). The specific receptor for MSP is recepteur d'origine nantais (RON) tyrosine kinase, a member of the MET proto-oncogene family (Wang et al., 2002).
 
  Schematic representations of the domain structures of pro-MSP and mature MSP proteins. After proteolytic cleavage at the Arg483-Val484 bond, pro-MSP is converted to mature MSP and acquires its biological activity. Mature MSP is composed of α-chain (53 kDa) and β-chain (30 kDa) linked by a disulfide bond. The α-chain contains PAN/APPLE-like domain, followed by four kringle domains, and the β-chain has a serine protease (peptidase S1)-like domain. SP, signal peptide; PAN, PAN/APPLE-like domain; K1-K4, Kringle domain1-4.
Description The human MSP has the highest amino acid sequence similarity (45%) to human hepatocyte growth factor (HGF), hence its name "hepatocyte growth factor-like protein (HGFL)". MSP is a glycoprotein belonging to a plasminogen-related growth factor family. It is secreted as a single-chain precursor protein (pro-MSP), which has no biological activity (Wang et al., 2002). Pro-MSP becomes active after cleavage at the Arg483-Val484 bond by specific trypsin-like serine proteases such as hepatocyte growth factor activator (HGFA), ST14 (matriptase), hepsin (transmembrane protease, serine 1; TMPRSS1), TMPRSS11D (Human airway trypsin-like protease; HAT), clotting factor XIIa, clotting factor XIa, and serum kallikrein (Wang et al., 2002; Kawaguchi et al., 2009; Bhatt et al., 2007; Ganesan et al., 2011; Orikawa et al., 2012). Among them, HGFA is a physiological serum activator of MSP at site of tissue injury, and ST14/matriptase likely has significant roles in activation of MSP/RON signaling on the cell surface as a cellular activator. In respiratory epithelial cells, TMPRSS11D/HAT serves as an efficient activator of MSP. In addition, hepsin may have a role in cancer cells. After cleavage of pro-MSP, MSP β-chain binds to its specific receptor tyrosine kinase RON, which results in autophosphorylation within its kinase catalytic domain, leading to the initiation of multiple signaling pathways including Ras/mitogen-activated protein kinase, phosphatidylinositol 3-kinase, c-Jun amino terminal kinase, β-catenin and nuclear factor-kappaB (NF-κB) (Wang et al., 2002; Kretschmann et al., 2010).
Expression MSP transcripts are present in the liver and, to a lesser amount, in adrenal glands, lungs, kidney, placenta and pancreas (Yoshimura et al., 1993; Ganesan et al., 2011).
Localisation MSP is synthesized and secreted mainly by hepatocytes as a biologically inactive single-chain precursor form and circulate as a plasma protein. The concentration of pro-MSP in the plasma is about 2-5 nM (Wang et al., 2002). Pro-MSP is activated by trypsin-like serum serine proteases such as HGFA, clotting factor XIIa, clotting factor XIa, serum kallikrein. On the cell surface, this activation can be processed by membrane-anchored serine proteases such as ST14/matriptase, hepsin and TMPRSS11D/HAT.
Function MSP was originally identified as a serum protein that activates resident macrophages, such as induction of shape change and motility, enhanced chemotaxis in response to complement factor C5a (Wang et al., 2002). However, its biological effects are not restricted to macrophages. MSP promotes proliferation and migration of various epithelial cells and microglia (Kretschmann et al., 2010; Suzuki et al., 2008), increases ciliary motility of nasal epithelial cells (Sakamoto et al., 1997), stimulates the bone resorbing activity of osteoclasts (Kurihara et al., 1996), and stimulates sperm motility (Ohshiro et al., 1996). To date, many studies have suggested that MSP/RON signaling pathway plays roles in various pathophysiological conditions such as inflammation, wound healing, and cancer. Gene knockout studies revealed that MSP is not essential for embryogenesis, fertility (Bezerra et al., 1998).

Inflammation
During inflammation, MSP exerts a dual function, both stimulatory and inhibitory, on macrophages. Stimulatory functions include its ability to induce macrophage spreading, migration, phagocytosis and the production of cytokines. However, MSP inhibits lipopolysaccharide-induced production of inflammatory mediators, such as inducible NO synthase, cyclooxygenase-2, and prostaglandin E2. These suppressive effects are mediated by RON-transduced signals that block LPS-induced activation of NF-κB pathways (Wang et al., 2002; Kretschmann et al., 2010).

Wound healing
MSP/RON signaling is involved at various steps of wound healing process. MSP promotes keratinocyte migration in mouse wound models and in wound healing assays in vitro. In experimental excisional wounds in rats, expression levels of MSP and RON within the wound were highest between 7 and 21 days. In a lung injury model, the function of MSP/RON appears to be necessary to suppress NF-κB activation and RON deficient mice exhibited increased lung injury and significantly decreased survival times (Kretschmann et al., 2010). However, MSP deficient mice do not show any defects in a skin wound healing model, suggesting that functional redundancies exist in the wound healing process (Bezerra et al., 1998). In a gentamicin(GM)-induced nephropathy model, MSP attenuates GM-induced inflammation and apoptosis by inhibition of the MAPKs/NF-κB signaling pathways (Lee et al., 2013).

Homology The human MSP has 45% amino acid sequence identity to hepatocyte growth factor, 43% to plasminogen and 36% to prothrombin, and 79% identity with murine and rat orthologue.

Mutations

Note Non-synonymous SNP (rs3197999, R689C) in the human MST-1 gene has been linked to inflammatory bowel disease (IBD) (Goyette et al., 2008; Latiano et al., 2010). This R689C variant impairs MSP function by reducing its affinity to RON. Recent study suggests that the rs3197999 variant in MST1 gene is also associated with primary sclerosing cholangitis (PSC) and extrahepatic cholangiocarcinoma (Melum et al., 2011; Srivastava et al., 2012; Krawczyk et al., 2013).

Implicated in

Note
  
Entity Cancer
Note Activation of RON by MSP can initiate signaling through many pathways implicated in tumor progression and metastasis. MSP activating serine proteases, such as HGFA, ST14/matriptase and hepsin are upregulated in various cancers. In addition, RON is overexpressed in many types of epithelial cancer. When MSP was activated at sites of tumors it would not only lead to activation of RON on tumor-associated macrophages, but also on the tumor cells, where RON has been shown to induce proliferation, survival, cell migration, epithelial-mesenchymal transition (EMT), invasion and metastasis. Furthermore, MSP/RON regulates M2 macrophage polarization leading to secretion of immunosuppressive cytokines as well as growth and angiogenic factors that promote the tumor progression. (Kretschmann et al., 2010).
  
  
Entity Lung cancer
Note MSP promoted liver metastasis of small cell lung cancer cells in a mouse model. Moreover, immunohistochemical analyses of liver metastases revealed that microvessel density and tumor-associated macrophages are significantly increased in lesions produced by MSP transfected cells (Sato et al., 2013).
  
  
Entity Breast cancer
Note In the MMTV-PyMT mouse breast cancer model, MSP promoted tumor growth and increased metastatic frequency. The most prominent effect of MSP expression in tumors was osteolytic metastasis to bone (Welm et al., 2007). Immunohistochemical analysis revealed that the proportion of malignant tumors (invasive ductal carcinoma) positive for MSP expression was significantly higher than that of benign tumor (Ren et al., 2012). However, there was no relationship between MSP expression and histopathological grade of the carcinoma cells.
Prognosis Breast cancer patients whose tumor overexpressed MSP/ST14/RON had significantly shorter metastasis-free survival and overall survival compared with patients whose tumors did not overexpress MSP/ST14/RON genes. Furthermore, overexpression of MSP/ST14/RON increased incidence of bone, lung, liver and brain metastases (Welm et al., 2007).
  
  
Entity Pancreatic cancer
Note MSP-induced activation of RON leads to enhanced L3.6pl pancreatic cancer cell migration and invasion. RON activation also induced morphological spindle-shape change and altered expression of E-cadherin (Camp et al., 2007). MSP strongly induced phosphorylation and nuclear translocation of ribosomal S6 kinases (RSK)-2, a downstream signaling protein of the Ras-Erk1/2 pathway. RSK-2 expressing L3.6pl pancreatic cancer cell shows EMT-like phenotypic changes after MSP stimulation (Ma et al., 2011).
  
  
Entity Merkel cell carcinoma
Note Tissue samples from 14 cases of Merkel cell carcinoma were used for immunohistochemical analysis. Nine cases out of 14 were positive for MSP and 9 cases out of 14 cases were positive for RON. Normal Merkel cells were negative for MSP and RON, suggesting MSP/RON signaling could play a role in tumorigenesis of MCC (Nagahama et al., 2011).
  
  
Entity Knee osteoarthritis (OA)
Note By using glycoproteomic approach, MSP was found as a prognostic factor for knee OA (Fukuda et al., 2012). In situ hybridization confirmed that abundant MSP mRNA expression was observed in the synovial tissues from OA knee.
Prognosis Higher plasma MSP level was associated with the progression of knee OA.
  

Bibliography

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Citation

This paper should be referenced as such :
Kawaguchi, M ; Kataoka, H
MST1 (macrophage stimulating 1 (hepatocyte growth factor-like))
Atlas Genet Cytogenet Oncol Haematol. 2013;17(12):828-832.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/MST1ID44411ch3p21.html


External links

Nomenclature
HGNC (Hugo)MST1   7380
Cards
AtlasMST1ID44411ch3p21
Entrez_Gene (NCBI)MST1  4485  macrophage stimulating 1
AliasesD3F15S2; DNF15S2; HGFL; MSP; 
NF15S2
GeneCards (Weizmann)MST1
Ensembl hg19 (Hinxton)ENSG00000173531 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000173531 [Gene_View]  chr3:49683947-49688763 [Contig_View]  MST1 [Vega]
ICGC DataPortalENSG00000173531
TCGA cBioPortalMST1
AceView (NCBI)MST1
Genatlas (Paris)MST1
WikiGenes4485
SOURCE (Princeton)MST1
Genetics Home Reference (NIH)MST1
Genomic and cartography
GoldenPath hg38 (UCSC)MST1  -     chr3:49683947-49688763 -  3p21.31   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)MST1  -     3p21.31   [Description]    (hg19-Feb_2009)
EnsemblMST1 - 3p21.31 [CytoView hg19]  MST1 - 3p21.31 [CytoView hg38]
Mapping of homologs : NCBIMST1 [Mapview hg19]  MST1 [Mapview hg38]
OMIM142408   
Gene and transcription
Genbank (Entrez)AK222893 AK294324 AK296192 AK298396 AK298452
RefSeq transcript (Entrez)NM_020998
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)MST1
Cluster EST : UnigeneHs.512587 [ NCBI ]
CGAP (NCI)Hs.512587
Alternative Splicing GalleryENSG00000173531
Gene ExpressionMST1 [ NCBI-GEO ]   MST1 [ EBI - ARRAY_EXPRESS ]   MST1 [ SEEK ]   MST1 [ MEM ]
Gene Expression Viewer (FireBrowse)MST1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)4485
GTEX Portal (Tissue expression)MST1
Human Protein AtlasENSG00000173531-MST1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP26927   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP26927  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP26927
Splice isoforms : SwissVarP26927
PhosPhoSitePlusP26927
Domaine pattern : Prosite (Expaxy)KRINGLE_1 (PS00021)    KRINGLE_2 (PS50070)    PAN (PS50948)    TRYPSIN_DOM (PS50240)   
Domains : Interpro (EBI)HGF-like    Kringle    Kringle-like    Kringle_CS    Pan_app    Peptidase_S1_PA    Peptidase_S1A    Trypsin_dom   
Domain families : Pfam (Sanger)Kringle (PF00051)    PAN_1 (PF00024)    Trypsin (PF00089)   
Domain families : Pfam (NCBI)pfam00051    pfam00024    pfam00089   
Domain families : Smart (EMBL)KR (SM00130)  PAN_AP (SM00473)  Tryp_SPc (SM00020)  
Conserved Domain (NCBI)MST1
DMDM Disease mutations4485
Blocks (Seattle)MST1
PDB (SRS)2ASU    4QT8   
PDB (PDBSum)2ASU    4QT8   
PDB (IMB)2ASU    4QT8   
PDB (RSDB)2ASU    4QT8   
Structural Biology KnowledgeBase2ASU    4QT8   
SCOP (Structural Classification of Proteins)2ASU    4QT8   
CATH (Classification of proteins structures)2ASU    4QT8   
SuperfamilyP26927
Human Protein Atlas [tissue]ENSG00000173531-MST1 [tissue]
Peptide AtlasP26927
HPRD00798
IPIIPI00292218   IPI00922577   IPI00953627   IPI01015719   IPI00925540   IPI00925679   IPI00925898   IPI00925822   
Protein Interaction databases
DIP (DOE-UCLA)P26927
IntAct (EBI)P26927
FunCoupENSG00000173531
BioGRIDMST1
STRING (EMBL)MST1
ZODIACMST1
Ontologies - Pathways
QuickGOP26927
Ontology : AmiGOmolecular_function  serine-type endopeptidase activity  protein binding  extracellular region  extracellular space  proteolysis  biological_process  receptor tyrosine kinase binding  negative regulation of gluconeogenesis  hepatocyte growth factor receptor signaling pathway  extracellular exosome  regulation of cAMP-dependent protein kinase activity  
Ontology : EGO-EBImolecular_function  serine-type endopeptidase activity  protein binding  extracellular region  extracellular space  proteolysis  biological_process  receptor tyrosine kinase binding  negative regulation of gluconeogenesis  hepatocyte growth factor receptor signaling pathway  extracellular exosome  regulation of cAMP-dependent protein kinase activity  
Pathways : BIOCARTAMsp/Ron Receptor Signaling Pathway [Genes]   
REACTOMEP26927 [protein]
REACTOME PathwaysR-HSA-8852405 [pathway]   
NDEx NetworkMST1
Atlas of Cancer Signalling NetworkMST1
Wikipedia pathwaysMST1
Orthology - Evolution
OrthoDB4485
GeneTree (enSembl)ENSG00000173531
Phylogenetic Trees/Animal Genes : TreeFamMST1
HOVERGENP26927
HOGENOMP26927
Homologs : HomoloGeneMST1
Homology/Alignments : Family Browser (UCSC)MST1
Gene fusions - Rearrangements
Fusion : MitelmanMST1/SRRD [3p21.31/22q12.1]  
Fusion: TCGAMST1 3p21.31 SRRD 22q12.1 BRCA
Fusion Cancer (Beijing)MST1P9 [MST1]  -  3p21.31 [FUSC002005]
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerMST1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)MST1
dbVarMST1
ClinVarMST1
1000_GenomesMST1 
Exome Variant ServerMST1
ExAC (Exome Aggregation Consortium)ENSG00000173531
GNOMAD BrowserENSG00000173531
Genetic variants : HAPMAP4485
Genomic Variants (DGV)MST1 [DGVbeta]
DECIPHERMST1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisMST1 
Mutations
ICGC Data PortalMST1 
TCGA Data PortalMST1 
Broad Tumor PortalMST1
OASIS PortalMST1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICMST1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDMST1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch MST1
DgiDB (Drug Gene Interaction Database)MST1
DoCM (Curated mutations)MST1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)MST1 (select a term)
intoGenMST1
NCG5 (London)MST1
Cancer3DMST1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM142408   
Orphanet783   
MedgenMST1
Genetic Testing Registry MST1
NextProtP26927 [Medical]
TSGene4485
GENETestsMST1
Target ValidationMST1
Huge Navigator MST1 [HugePedia]
snp3D : Map Gene to Disease4485
BioCentury BCIQMST1
ClinGenMST1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD4485
Chemical/Pharm GKB GenePA31185
Clinical trialMST1
Miscellaneous
canSAR (ICR)MST1 (select the gene name)
Probes
Litterature
PubMed91 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineMST1
EVEXMST1
GoPubMedMST1
iHOPMST1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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