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CTSH (cathepsin H)

Written2007-09Zala Jevnikar, Janko Kos
Faculty of Pharmacy, University of Ljubljana, Ljubljana, Slovenia

(Note : for Links provided by Atlas : click)

Identity

Alias_namesCPSB
Alias_symbol (synonym)ACC-4
ACC-5
ACC4
ACC5
Other aliasDKFZp686B24257
EC 3.4.22.16
MGC1519
aleurain
minichain
HGNC (Hugo) CTSH
LocusID (NCBI) 1512
Atlas_Id 40206
Location 15q25.1  [Link to chromosome band 15q25]
Location_base_pair Starts at 78921750 and ends at 78945098 bp from pter ( according to hg19-Feb_2009)  [Mapping CTSH.png]
Fusion genes
(updated 2016)
CTSH (15q25.1) / CTSH (15q25.1)CTSH (15q25.1) / PI4KA (22q11.21)CTSH (15q25.1) / RASGRF1 (15q25.1)
CTSH (15q25.1) / SYNE1 (6q25.1)

DNA/RNA

Description The gene for human cathepsin H is located on chromosome 15q24-q25 and contains 12 exons spanning over 23 kb of genomic sequences. The junctions between the exons and 11 introns conform to the GT-AG rule. The preproenzyme transcript length is 1005 bp.
Transcription The cathepsin H gene has a TATA- and CAAT-less promoter and upstretream of exon 1 only one GC box was detected, suggesting the presence of one more exon. Two different forms of cathepsin H cDNA, the full-length form (CTSH) and a truncated form with deletion of 12 amino acids at the signal peptide region (CTSHdelta10-21), were identified in prostate tissues and cancer cell lines.

Protein

 
  Richardson diagram of cathepsin H structure: a-helixes are shown in red and ß -sheets in green. Catalytic residues are shown in ball-and-stick representation: Cys141 in yellow, His281 in purple and Asn301 in pink. Carbohydrates are shown as CPK spheres in yellow. The mini chain is shown in grey (MEROPS: the peptidase database - C01.040).
Description Cathepsin H belongs to the superfamily of papain-like cysteine proteases. It is synthesized as a preproenzyme of 335 amino acid residues with a calculated Mr of 37 403. It is proteolytically processed to an active single chain, i.e. mature form within the endosomes/lysosomes. A unique feature of this enzyme is that it acts as both an aminopeptidase and an endopeptidase although the latter activity is much lower than the former activity. Sequencing data revealed that in addition to the heavy and light chains, which are typically found in a number of mammalian papain-like cysteine proteases, cathepsin H contains also an octapeptide EPQNCSAT originating from the propeptide, termed the mini-chain. It was shown that the mini-chain is disulfide linked to Cys205 of the main body of the enzyme and involved in the aminopeptidase activity of the enzyme. It was concluded that the mini-chain plays a key role in substrate recognition, and that the carbohydrate residues attached to the body of the enzyme are involved in the positioning the mini-chain in the active-site cleft. Procathepsin H has three potential carbohydrate binding sites. Glycosilation has been confirmed on Asn230 and on the mini-chain Asn101 of the mature enzyme. The recombinant form of human cathepsin H lacking the mini-chain was shown to be an endopeptidase. Cathepsin H hidrolyzes endopeptidase substrates such as Bz-Arg+NHNap, Bz-Arg+NHMec, Bz-Phe-Val-Arg+NHMec, and acts on Pro-Gly+Phe and Pro-Arg+NHNap much like a dipeptidyl-peptidase. It was shown to cleave several proteins preferring hydrophobic residues at P2 and P3, however the endopeptidase activity of the enzyme is limited. Collagen and laminin, for instance, were not degraded by cathepsin H. Naturally occurring inhibitors of cathepsin H are the cystatins, a2-macroglobulin and antigens from mouse cytotoxic lymphocytes CTLA-2ß.
Expression Cathepsin H expression is ubiquitous, with very high expression in the kidney. There is growing evidence that the expression of cathepsin H is increased in diseases including breast, colorectal and prostate carcinoma, melanoma and gliomas. In contrast, decreased cathepsin H expression has been reported in squamous cell carcinoma of the head and neck. Other studies have found a higher cathepsin H expression in well-differentiated pancreatic cancer cells compared with less well-differentiated cancer cells.
Localisation Cathepsin H is located manly at the endosomal-lysosomal compartments. Only 10 % of the enzyme is secreted. It has been shown that substantial concentrations of cathepsin H circulate in the blood.
Function Cathepsin H is one of the lysosomal cysteine proteinases, which are involved in intracellular protein degradation. It is one of the few noncomplement proteases that cleave native C5 to generate the potent chemotaxin C5a. Cathepsin H was detected in extracellular compartments of atherosclerotic plaques. Although the pathogenic potential of cathepsin H in the development of the late, unstable plaque is quite evident, there is the possibility that this protease may play a role in early atherogenesis. Furthermore, it was found that cathepsin H could contribute to the transformation of LDL in monocyte-derived foam cells. Recently the enzyme was shown to be essential in one of the processing steps of hydrophobic surfactant-associated protein C.
Cathepsin H is overexpressed in different tumour cells. However, the role of cathepsin H in tumour progression is not well understood. A possible function of cathepsin H in tumour progression is its ability to degrade fibrinogen and fibronectin, suggesting that, along with other proteases, cathepsin H may be involved in the destruction of extracellular matrix components leading to cancer proliferation, migration, and metastasis.
Homology Cathepsins H exhibit a high degree of sequence homology to cathepsin B and other cysteine proteinases of the C1 (papain) family.

Mutations

Germinal Not yet reported
Somatic Not yet reported

Implicated in

Note
  
Entity Colorectal cancer
Prognosis Protein levels of cathepsin H were measured by ELISA in preoperative sera from 324 patients with colorectal cancer. The level of cathepsin H was significantly increased in patient sera, the median level was 8.4 ng/mL versus 2.1 ng/mL in 90 healthy blood donors (p < 0.0001). In survival analysis a significant difference was found between the group of patients with low cathepsin H (first tertile) who had a poor prognosis and the remaining patients (p = 0.03). The risk of patients was further stratified when cathepsin H levels were combined with carcinoembryonic antigen (CEA). Patients with high CEA and low cathepsin H had the highest risk of death with a hazard ratio of 2.72 (95% CI 1.73-4.28), p < 0.0001.The prognostic information of cathepsin H differs from that of the related cathepsins B and L and suggest different roles during the progression of malignant disease.
  
  
Entity Melanoma
Prognosis The level of cathepsin H was determined in the sera of 43 patients with metastatic melanoma, in 54 patients with treated cutaneous melanoma with no evidence of metastatic disease, and in 30 healthy blood donors, using quantitative ELISA. The levels were significantly higher within the group of metastatic melanoma patients compared with the healthy controls with a median of 13.7 versus 4.9 ng/ml (P < 0.0001). Cathepsin H was also significantly increased within the group of melanoma patients with no metastasis, with a median of 9.6 ng/ml. The serum level was increased in patients showing no response to the chemoimmunotherapy as compared to the level in responders. Metastatic melanoma patients with high content of cathepsin H experienced significantly shorter overall survival rates than the patients with low levels of the enzyme (Cat H: P < 0.006 and relative risk, 2.4, using median as cut-off value).
  
  
Entity Head and neck carcinoma
Prognosis To estimate the prognostic value of cathepsins H in head and neck carcinoma, its concentration was measured in cytosols of primary tumours and adjacent normal tissue from 21 patients. Cathepsin H concentration was higher in normal tissue (p = 0.001) than in tumour tissue and in laryngeal than in non-laryngeal normal and tumour tissues. Disease-free survival was poor in patients with lower concentrations of cathepsin H in tumour tissue (p = 0.055).
  
  
Entity Bladder cell transitional cell carcinoma
Note Using spectrofluorometric assay, catalytic activity of cathepsin H was measured in human bladder cell lines (HCV29, normal; RT4, well differentiated; J82, poorly differentiated) and in noncancerous and cancerous tissue samples (n = 20) of transitional cell carcinoma. In comparison to the intracellular activity of cathepsin H in the poorly differentiated cell line J82, the intracellular activity in the normal cell line HCV29 was significantly greater (P <0.05), independent of stage or grade. In contrast, the portion of cathepsin H released from cell line J82 into the supernatant, revealed higher values than that from cell line HCV29. In cancerous bladder tissue, the level of cathepsin H was significantly greater than in the matched normal tissue (P <0.05).
  
  
Entity Lung cancer
Note A transgenic mouse model of lung cancer was utilized to identify markers of early lung tumours in humans. Immunohistochemical analyses identified cathepsin H as being consistently elevated in the murine lung tumours compared to non-tumour bearing transgenic lung tissue surrounding the tumour. Importantly, the elevation was observed in early stage, indicating its ability to detect early lung lesions that would be amenable to surgical resection.
  
  
Entity Glioma
Note Cathepsin H activity was determined in normal brain tissue and tumour tissue extracts. The activity of cathepsin H was twofold higher in low grade glioma, fourfold higher in anaplastic astrocytoma and eightfold higher in glioblastoma than in normal brain tissue. Cathepsin H antibody inhibited the invasion of glioblastoma cell lines through Matrigel®. These data suggest that the tumour-specific increase in antigen may be a useful independent marker of tumour progression in central nervous system neoplasms.
  
  
Entity Cervical carcinoma
Note The expression of cathepsin H in cervical carcinoma cell lines and tissue was found to be down-regulated compared to normal tissue, using cDNA arrays.
  
  
Entity Joint diseases
Note The level of cathepsin H was determined in synovial fluids and sera of patients with inflammatory and metabolic joint diseases, using quantitative ELISA. Cathepsin H was not found in normal sera (values below 3 micrograms/l), but was measurable in patients' synovial fluids. The highest values of cathepsin H were measured in synovial fluids of patients with undifferentiated arthritis. There is yet no clear correlation between the quantity of the enzyme released in synovia and the clinical diagnosis or the stage of disease.
  
  
Entity Alzheimer's disease
Note Cultured fibroblasts from patients affected by Alzheimer's disease (AD) exhibited alterations of the enzyme transketolase. Abnormalities (dubbed alkaline band) consisted of enzyme forms having unusually high pl and were proposed as a marker of the disease in living patients. Human cathepsin H was shown to partially induce an Alzheimer-like transketolase pattern and cleave normal transketolase to a 35 kDa fragment as spontaneously occurring in Alzheimer's disease fibroblasts. The explanation of transketolase abnormalities could be an imbalance of proteolysis in Alzheimer's disease fibroblasts due to a relative increase/derangement of cysteine proteinases, including cathepsin H.
  

Bibliography

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PMID 2329322
 
Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function.
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PMID 9493267
 
Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis.
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PMID 2759235
 
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PMID 8771190
 
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Citation

This paper should be referenced as such :
Jevnikar, Z ; Kos, J
CTSH (cathepsin H)
Atlas Genet Cytogenet Oncol Haematol. 2008;12(2):130-133.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/CTSHID40206ch15q25.html


External links

Nomenclature
HGNC (Hugo)CTSH   2535
Cards
AtlasCTSHID40206ch15q25
Entrez_Gene (NCBI)CTSH  1512  cathepsin H
AliasesACC-4; ACC-5; ACC4; ACC5; 
CPSB
GeneCards (Weizmann)CTSH
Ensembl hg19 (Hinxton)ENSG00000103811 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000103811 [Gene_View]  chr15:78921750-78945098 [Contig_View]  CTSH [Vega]
ICGC DataPortalENSG00000103811
TCGA cBioPortalCTSH
AceView (NCBI)CTSH
Genatlas (Paris)CTSH
WikiGenes1512
SOURCE (Princeton)CTSH
Genetics Home Reference (NIH)CTSH
Genomic and cartography
GoldenPath hg38 (UCSC)CTSH  -     chr15:78921750-78945098 -  15q25.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)CTSH  -     15q25.1   [Description]    (hg19-Feb_2009)
EnsemblCTSH - 15q25.1 [CytoView hg19]  CTSH - 15q25.1 [CytoView hg38]
Mapping of homologs : NCBICTSH [Mapview hg19]  CTSH [Mapview hg38]
OMIM116820   
Gene and transcription
Genbank (Entrez)AF426247 AF426248 AI057198 AK026152 AK130158
RefSeq transcript (Entrez)NM_001319137 NM_004390 NM_148979
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)CTSH
Cluster EST : UnigeneHs.148641 [ NCBI ]
CGAP (NCI)Hs.148641
Alternative Splicing GalleryENSG00000103811
Gene ExpressionCTSH [ NCBI-GEO ]   CTSH [ EBI - ARRAY_EXPRESS ]   CTSH [ SEEK ]   CTSH [ MEM ]
Gene Expression Viewer (FireBrowse)CTSH [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1512
GTEX Portal (Tissue expression)CTSH
Protein : pattern, domain, 3D structure
UniProt/SwissProtP09668   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP09668  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP09668
Splice isoforms : SwissVarP09668
Catalytic activity : Enzyme3.4.22.16 [ Enzyme-Expasy ]   3.4.22.163.4.22.16 [ IntEnz-EBI ]   3.4.22.16 [ BRENDA ]   3.4.22.16 [ KEGG ]   
PhosPhoSitePlusP09668
Domaine pattern : Prosite (Expaxy)THIOL_PROTEASE_ASN (PS00640)    THIOL_PROTEASE_CYS (PS00139)    THIOL_PROTEASE_HIS (PS00639)   
Domains : Interpro (EBI)Pept_asp_AS    Pept_cys_AS    Pept_his_AS    Peptidase_C1A    Peptidase_C1A_C    Prot_inhib_I29   
Domain families : Pfam (Sanger)Inhibitor_I29 (PF08246)    Peptidase_C1 (PF00112)   
Domain families : Pfam (NCBI)pfam08246    pfam00112   
Domain families : Smart (EMBL)Inhibitor_I29 (SM00848)  Pept_C1 (SM00645)  
Conserved Domain (NCBI)CTSH
DMDM Disease mutations1512
Blocks (Seattle)CTSH
PDB (SRS)1BZN   
PDB (PDBSum)1BZN   
PDB (IMB)1BZN   
PDB (RSDB)1BZN   
Structural Biology KnowledgeBase1BZN   
SCOP (Structural Classification of Proteins)1BZN   
CATH (Classification of proteins structures)1BZN   
SuperfamilyP09668
Human Protein AtlasENSG00000103811
Peptide AtlasP09668
HPRD00288
IPIIPI00297487   IPI00375426   IPI00922584   IPI00981006   IPI00982176   IPI00980422   
Protein Interaction databases
DIP (DOE-UCLA)P09668
IntAct (EBI)P09668
FunCoupENSG00000103811
BioGRIDCTSH
STRING (EMBL)CTSH
ZODIACCTSH
Ontologies - Pathways
QuickGOP09668
Ontology : AmiGOP-body  metanephros development  T cell mediated cytotoxicity  adaptive immune response  immune response-regulating signaling pathway  endopeptidase activity  aminopeptidase activity  cysteine-type endopeptidase activity  cysteine-type endopeptidase activity  serine-type endopeptidase activity  protein binding  extracellular region  extracellular space  lysosome  cytosol  proteolysis  proteolysis  apoptotic process  activation of cysteine-type endopeptidase activity involved in apoptotic process  peptidase activity  peptidase activity  cysteine-type peptidase activity  positive regulation of cell proliferation  cysteine-type endopeptidase activator activity involved in apoptotic process  positive regulation of gene expression  positive regulation of epithelial cell migration  neuropeptide catabolic process  bradykinin catabolic process  positive regulation of peptidase activity  antigen processing and presentation  HLA-A specific activating MHC class I receptor activity  positive regulation of cell migration  zymogen activation  protein destabilization  response to retinoic acid  membrane protein proteolysis  secretory granule lumen  negative regulation of apoptotic process  surfactant homeostasis  intracellular membrane-bounded organelle  neutrophil degranulation  cellular protein metabolic process  positive regulation of angiogenesis  proteolysis involved in cellular protein catabolic process  dichotomous subdivision of terminal units involved in lung branching  extracellular exosome  thyroid hormone binding  ERK1 and ERK2 cascade  cellular response to thyroid hormone stimulus  alveolar lamellar body  multivesicular body lumen  tertiary granule lumen  ficolin-1-rich granule lumen  positive regulation of apoptotic signaling pathway  
Ontology : EGO-EBIP-body  metanephros development  T cell mediated cytotoxicity  adaptive immune response  immune response-regulating signaling pathway  endopeptidase activity  aminopeptidase activity  cysteine-type endopeptidase activity  cysteine-type endopeptidase activity  serine-type endopeptidase activity  protein binding  extracellular region  extracellular space  lysosome  cytosol  proteolysis  proteolysis  apoptotic process  activation of cysteine-type endopeptidase activity involved in apoptotic process  peptidase activity  peptidase activity  cysteine-type peptidase activity  positive regulation of cell proliferation  cysteine-type endopeptidase activator activity involved in apoptotic process  positive regulation of gene expression  positive regulation of epithelial cell migration  neuropeptide catabolic process  bradykinin catabolic process  positive regulation of peptidase activity  antigen processing and presentation  HLA-A specific activating MHC class I receptor activity  positive regulation of cell migration  zymogen activation  protein destabilization  response to retinoic acid  membrane protein proteolysis  secretory granule lumen  negative regulation of apoptotic process  surfactant homeostasis  intracellular membrane-bounded organelle  neutrophil degranulation  cellular protein metabolic process  positive regulation of angiogenesis  proteolysis involved in cellular protein catabolic process  dichotomous subdivision of terminal units involved in lung branching  extracellular exosome  thyroid hormone binding  ERK1 and ERK2 cascade  cellular response to thyroid hormone stimulus  alveolar lamellar body  multivesicular body lumen  tertiary granule lumen  ficolin-1-rich granule lumen  positive regulation of apoptotic signaling pathway  
Pathways : KEGGLysosome   
REACTOMEP09668 [protein]
REACTOME PathwaysR-HSA-6798695 [pathway]   
NDEx NetworkCTSH
Atlas of Cancer Signalling NetworkCTSH
Wikipedia pathwaysCTSH
Orthology - Evolution
OrthoDB1512
GeneTree (enSembl)ENSG00000103811
Phylogenetic Trees/Animal Genes : TreeFamCTSH
HOVERGENP09668
HOGENOMP09668
Homologs : HomoloGeneCTSH
Homology/Alignments : Family Browser (UCSC)CTSH
Gene fusions - Rearrangements
Fusion : MitelmanCTSH/RASGRF1 [15q25.1/15q25.1]  
Fusion: TCGACTSH 15q25.1 RASGRF1 15q25.1 BRCA LUAD
Fusion Cancer (Beijing)CTSH [15q25.1]  -  PI4KA [22q11.21]  [FUSC002568]
Fusion Cancer (Beijing)CTSH [15q25.1]  -  SYNE1 [6q25.1]  [FUSC002828]
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerCTSH [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)CTSH
dbVarCTSH
ClinVarCTSH
1000_GenomesCTSH 
Exome Variant ServerCTSH
ExAC (Exome Aggregation Consortium)CTSH (select the gene name)
Genetic variants : HAPMAP1512
Genomic Variants (DGV)CTSH [DGVbeta]
DECIPHERCTSH [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisCTSH 
Mutations
ICGC Data PortalCTSH 
TCGA Data PortalCTSH 
Broad Tumor PortalCTSH
OASIS PortalCTSH [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICCTSH  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDCTSH
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch CTSH
DgiDB (Drug Gene Interaction Database)CTSH
DoCM (Curated mutations)CTSH (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)CTSH (select a term)
intoGenCTSH
NCG5 (London)CTSH
Cancer3DCTSH(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM116820   
Orphanet3637   
MedgenCTSH
Genetic Testing Registry CTSH
NextProtP09668 [Medical]
TSGene1512
GENETestsCTSH
Target ValidationCTSH
Huge Navigator CTSH [HugePedia]
snp3D : Map Gene to Disease1512
BioCentury BCIQCTSH
ClinGenCTSH
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD1512
Chemical/Pharm GKB GenePA27033
Clinical trialCTSH
Miscellaneous
canSAR (ICR)CTSH (select the gene name)
Probes
Litterature
PubMed68 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineCTSH
EVEXCTSH
GoPubMedCTSH
iHOPCTSH
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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