Full text data of CASP14
CASP14
[Confidence: low (only semi-automatic identification from reviews)]
Caspase-14; CASP-14; 3.4.22.-; Caspase-14 subunit p19; Caspase-14 subunit p10; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Caspase-14; CASP-14; 3.4.22.-; Caspase-14 subunit p19; Caspase-14 subunit p10; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P31944
ID CASPE_HUMAN Reviewed; 242 AA.
AC P31944; O95823; Q3SYC9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2001, sequence version 2.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Caspase-14;
DE Short=CASP-14;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=Caspase-14 subunit p19;
DE Contains:
DE RecName: Full=Caspase-14 subunit p10;
DE Flags: Precursor;
GN Name=CASP14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11062009; DOI=10.1006/bbrc.2000.3698;
RA Eckhart L., Ban J., Fischer H., Tschachler E.;
RT "Caspase-14: analysis of gene structure and mRNA expression during
RT keratinocyte differentiation.";
RL Biochem. Biophys. Res. Commun. 277:655-659(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=12181750; DOI=10.1038/sj.cdd.4401061;
RA Pistritto G., Jost M., Srinivasula S.M., Baffa R., Poyet J.-L.,
RA Kari C., Lazebnik Y., Rodeck U., Alnemri E.S.;
RT "Expression and transcriptional regulation of caspase-14 in simple and
RT complex epithelia.";
RL Cell Death Differ. 9:995-1006(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 68-74; 137-147 AND 154-162.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11175259; DOI=10.1038/sj.cdd.4400785;
RA Lippens S., Kockx M., Knaapen M., Mortier L., Polakowska R.,
RA Verheyen A., Garmyn M., Zwijsen A., Formstecher P., Huylebroeck D.,
RA Vandenabeele P., Declercq W.;
RT "Epidermal differentiation does not involve the pro-apoptotic
RT executioner caspases, but is associated with caspase-14 induction and
RT processing.";
RL Cell Death Differ. 7:1218-1224(2000).
RN [6]
RP PROTEIN SEQUENCE OF 153-163, PROTEOLYTIC PROCESSING, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12200134; DOI=10.1016/S0006-291X(02)02015-6;
RA Chien A.J., Presland R.B., Kuechle M.K.;
RT "Processing of native caspase-14 occurs at an atypical cleavage site
RT in normal epidermal differentiation.";
RL Biochem. Biophys. Res. Commun. 296:911-917(2002).
CC -!- FUNCTION: Believed to be a non-apoptotic caspase which is involved
CC in epidermal differentiation. Seems to play a role in keratinocyte
CC differentiation and cornification. Probably regulates maturation
CC of the epidermis by proteolytically processing filaggrin (By
CC similarity).
CC -!- SUBUNIT: Complex of unprocessed caspase-14 and processed 19 kDa
CC (p19) and 10 kDa (p10) subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes of adult skin
CC suprabasal layers (from spinous layers to the stratum granulosum
CC and stratum corneum) (at protein level). Expressed in
CC keratinocytes of hair shaft and sebaceous glands (at protein
CC level). In psoriatic skin only expressed at very low levels.
CC -!- INDUCTION: In undifferentiated keratinocytes under postconfluency
CC growth conditions (in vitro).
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF097874; AAD16173.1; -; mRNA.
DR EMBL; BC069541; AAH69541.1; -; mRNA.
DR EMBL; BC103868; AAI03869.1; -; mRNA.
DR EMBL; BC103869; AAI03870.1; -; mRNA.
DR PIR; JC7517; JC7517.
DR RefSeq; NP_036246.1; NM_012114.2.
DR UniGene; Hs.466057; -.
DR ProteinModelPortal; P31944; -.
DR SMR; P31944; 28-241.
DR IntAct; P31944; 4.
DR STRING; 9606.ENSP00000221740; -.
DR BindingDB; P31944; -.
DR ChEMBL; CHEMBL5991; -.
DR MEROPS; C14.018; -.
DR DMDM; 12231007; -.
DR PaxDb; P31944; -.
DR PeptideAtlas; P31944; -.
DR PRIDE; P31944; -.
DR DNASU; 23581; -.
DR Ensembl; ENST00000221740; ENSP00000221740; ENSG00000105141.
DR Ensembl; ENST00000427043; ENSP00000393417; ENSG00000105141.
DR GeneID; 23581; -.
DR KEGG; hsa:23581; -.
DR UCSC; uc010dzv.2; human.
DR CTD; 23581; -.
DR GeneCards; GC19P015160; -.
DR HGNC; HGNC:1502; CASP14.
DR HPA; CAB010059; -.
DR MIM; 605848; gene.
DR neXtProt; NX_P31944; -.
DR PharmGKB; PA26085; -.
DR eggNOG; NOG327631; -.
DR HOGENOM; HOG000231878; -.
DR HOVERGEN; HBG050804; -.
DR InParanoid; P31944; -.
DR KO; K04401; -.
DR OMA; CVTKARE; -.
DR OrthoDB; EOG7VQJDT; -.
DR PhylomeDB; P31944; -.
DR GeneWiki; Caspase_14; -.
DR GenomeRNAi; 23581; -.
DR NextBio; 46186; -.
DR PMAP-CutDB; P31944; -.
DR PRO; PR:P31944; -.
DR ArrayExpress; P31944; -.
DR Bgee; P31944; -.
DR CleanEx; HS_CASP14; -.
DR Genevestigator; P31944; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045095; C:keratin filament; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR011600; Pept_C14_caspase.
DR InterPro; IPR001309; Pept_C14_ICE_p20.
DR InterPro; IPR016129; Pept_C14_ICE_p20_AS.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR015917; Pept_C14A_p45_core.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; FALSE_NEG.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Differentiation;
KW Direct protein sequencing; Hydrolase; Nucleus; Protease;
KW Reference proteome; Thiol protease; Zymogen.
FT PROPEP 1 ? Potential.
FT /FTId=PRO_0000004652.
FT CHAIN ? 152 Caspase-14 subunit p19.
FT /FTId=PRO_0000004653.
FT CHAIN 153 242 Caspase-14 subunit p10.
FT /FTId=PRO_0000004654.
FT ACT_SITE 89 89 By similarity.
FT ACT_SITE 132 132 By similarity.
SQ SEQUENCE 242 AA; 27680 MW; E539FB7E8DD808A2 CRC64;
MSNPRSLEEE KYDMSGARLA LILCVTKARE GSEEDLDALE HMFRQLRFES TMKRDPTAEQ
FQEELEKFQQ AIDSREDPVS CAFVVLMAHG REGFLKGEDG EMVKLENLFE ALNNKNCQAL
RAKPKVYIIQ ACRGEQRDPG ETVGGDEIVM VIKDSPQTIP TYTDALHVYS TVEGYIAYRH
DQKGSCFIQT LVDVFTKRKG HILELLTEVT RRMAEAELVQ EGKARKTNPE IQSTLRKRLY
LQ
//
ID CASPE_HUMAN Reviewed; 242 AA.
AC P31944; O95823; Q3SYC9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2001, sequence version 2.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Caspase-14;
DE Short=CASP-14;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=Caspase-14 subunit p19;
DE Contains:
DE RecName: Full=Caspase-14 subunit p10;
DE Flags: Precursor;
GN Name=CASP14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11062009; DOI=10.1006/bbrc.2000.3698;
RA Eckhart L., Ban J., Fischer H., Tschachler E.;
RT "Caspase-14: analysis of gene structure and mRNA expression during
RT keratinocyte differentiation.";
RL Biochem. Biophys. Res. Commun. 277:655-659(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=12181750; DOI=10.1038/sj.cdd.4401061;
RA Pistritto G., Jost M., Srinivasula S.M., Baffa R., Poyet J.-L.,
RA Kari C., Lazebnik Y., Rodeck U., Alnemri E.S.;
RT "Expression and transcriptional regulation of caspase-14 in simple and
RT complex epithelia.";
RL Cell Death Differ. 9:995-1006(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 68-74; 137-147 AND 154-162.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel
RT protein database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11175259; DOI=10.1038/sj.cdd.4400785;
RA Lippens S., Kockx M., Knaapen M., Mortier L., Polakowska R.,
RA Verheyen A., Garmyn M., Zwijsen A., Formstecher P., Huylebroeck D.,
RA Vandenabeele P., Declercq W.;
RT "Epidermal differentiation does not involve the pro-apoptotic
RT executioner caspases, but is associated with caspase-14 induction and
RT processing.";
RL Cell Death Differ. 7:1218-1224(2000).
RN [6]
RP PROTEIN SEQUENCE OF 153-163, PROTEOLYTIC PROCESSING, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12200134; DOI=10.1016/S0006-291X(02)02015-6;
RA Chien A.J., Presland R.B., Kuechle M.K.;
RT "Processing of native caspase-14 occurs at an atypical cleavage site
RT in normal epidermal differentiation.";
RL Biochem. Biophys. Res. Commun. 296:911-917(2002).
CC -!- FUNCTION: Believed to be a non-apoptotic caspase which is involved
CC in epidermal differentiation. Seems to play a role in keratinocyte
CC differentiation and cornification. Probably regulates maturation
CC of the epidermis by proteolytically processing filaggrin (By
CC similarity).
CC -!- SUBUNIT: Complex of unprocessed caspase-14 and processed 19 kDa
CC (p19) and 10 kDa (p10) subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes of adult skin
CC suprabasal layers (from spinous layers to the stratum granulosum
CC and stratum corneum) (at protein level). Expressed in
CC keratinocytes of hair shaft and sebaceous glands (at protein
CC level). In psoriatic skin only expressed at very low levels.
CC -!- INDUCTION: In undifferentiated keratinocytes under postconfluency
CC growth conditions (in vitro).
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF097874; AAD16173.1; -; mRNA.
DR EMBL; BC069541; AAH69541.1; -; mRNA.
DR EMBL; BC103868; AAI03869.1; -; mRNA.
DR EMBL; BC103869; AAI03870.1; -; mRNA.
DR PIR; JC7517; JC7517.
DR RefSeq; NP_036246.1; NM_012114.2.
DR UniGene; Hs.466057; -.
DR ProteinModelPortal; P31944; -.
DR SMR; P31944; 28-241.
DR IntAct; P31944; 4.
DR STRING; 9606.ENSP00000221740; -.
DR BindingDB; P31944; -.
DR ChEMBL; CHEMBL5991; -.
DR MEROPS; C14.018; -.
DR DMDM; 12231007; -.
DR PaxDb; P31944; -.
DR PeptideAtlas; P31944; -.
DR PRIDE; P31944; -.
DR DNASU; 23581; -.
DR Ensembl; ENST00000221740; ENSP00000221740; ENSG00000105141.
DR Ensembl; ENST00000427043; ENSP00000393417; ENSG00000105141.
DR GeneID; 23581; -.
DR KEGG; hsa:23581; -.
DR UCSC; uc010dzv.2; human.
DR CTD; 23581; -.
DR GeneCards; GC19P015160; -.
DR HGNC; HGNC:1502; CASP14.
DR HPA; CAB010059; -.
DR MIM; 605848; gene.
DR neXtProt; NX_P31944; -.
DR PharmGKB; PA26085; -.
DR eggNOG; NOG327631; -.
DR HOGENOM; HOG000231878; -.
DR HOVERGEN; HBG050804; -.
DR InParanoid; P31944; -.
DR KO; K04401; -.
DR OMA; CVTKARE; -.
DR OrthoDB; EOG7VQJDT; -.
DR PhylomeDB; P31944; -.
DR GeneWiki; Caspase_14; -.
DR GenomeRNAi; 23581; -.
DR NextBio; 46186; -.
DR PMAP-CutDB; P31944; -.
DR PRO; PR:P31944; -.
DR ArrayExpress; P31944; -.
DR Bgee; P31944; -.
DR CleanEx; HS_CASP14; -.
DR Genevestigator; P31944; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045095; C:keratin filament; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR011600; Pept_C14_caspase.
DR InterPro; IPR001309; Pept_C14_ICE_p20.
DR InterPro; IPR016129; Pept_C14_ICE_p20_AS.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR015917; Pept_C14A_p45_core.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; FALSE_NEG.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Differentiation;
KW Direct protein sequencing; Hydrolase; Nucleus; Protease;
KW Reference proteome; Thiol protease; Zymogen.
FT PROPEP 1 ? Potential.
FT /FTId=PRO_0000004652.
FT CHAIN ? 152 Caspase-14 subunit p19.
FT /FTId=PRO_0000004653.
FT CHAIN 153 242 Caspase-14 subunit p10.
FT /FTId=PRO_0000004654.
FT ACT_SITE 89 89 By similarity.
FT ACT_SITE 132 132 By similarity.
SQ SEQUENCE 242 AA; 27680 MW; E539FB7E8DD808A2 CRC64;
MSNPRSLEEE KYDMSGARLA LILCVTKARE GSEEDLDALE HMFRQLRFES TMKRDPTAEQ
FQEELEKFQQ AIDSREDPVS CAFVVLMAHG REGFLKGEDG EMVKLENLFE ALNNKNCQAL
RAKPKVYIIQ ACRGEQRDPG ETVGGDEIVM VIKDSPQTIP TYTDALHVYS TVEGYIAYRH
DQKGSCFIQT LVDVFTKRKG HILELLTEVT RRMAEAELVQ EGKARKTNPE IQSTLRKRLY
LQ
//
MIM
605848
*RECORD*
*FIELD* NO
605848
*FIELD* TI
*605848 CASPASE 14, APOPTOSIS-RELATED CYSTEINE PROTEASE; CASP14
*FIELD* TX
DESCRIPTION
read more
CASP14 belongs to the evolutionarily conserved caspase family. Caspases
are cysteinyl aspartate-specific proteinases, many of which play a
central role in apoptosis (Van de Craen et al., 1998). See CASP1
(147678) for additional background information on caspases.
CLONING
Using database searches for caspase sequences, Van de Craen et al.
(1998) identified CASP14 in human genomic sequence data and cloned both
human and mouse CASP14 cDNAs. By Northern blot and RT-PCR analyses, Van
de Craen et al. (1998) detected Casp14 expression in mouse skin and
developing mouse embryos (embryonic day 7, 15, 16, and 17). Expression
generally increased during maturation of the mouse embryo but dropped
temporarily to an undetectable level around embryonic day 11 to 12. The
authors suggested that Casp14 may play a role in ontogenesis and skin
physiology.
Eckhart et al. (2000) cloned a full-length CASP14 cDNA encoding a
242-amino acid protein with potential AP1 (165160) and KLF4 (602253)
interaction sites. They identified 2 CASP14 transcripts, designated
CASP14a and CASP14b, that differ in the C terminus due to a shifted open
reading frame. Use of an alternative splice acceptor site within intron
5 results in a 74-nucleotide insertion in CASP14b. CASP14b lacks
homology with the caspase consensus sequence and does not have a
counterpart in mouse. In situ hybridization analysis detected CASP14
within the epidermis, in hair follicles, and in the cells of the
sebaceous glands, with highest expression in the keratogenous zone and
the inner root sheeth of the hair follicle and in the peripheral cells
of the sebaceous glands.
Using immunohistochemical analysis, Denecker et al. (2007) confirmed
that mouse Casp14 was expressed only in cornifying epithelia, such as
the epidermis and Hassall bodies, and in forestomach, which is cornified
like epidermis.
GENE FUNCTION
Using Northern blot and semiquantitative RT-PCR analyses, Eckhart et al.
(2000) showed that CASP14 was transcriptionally upregulated during
maintenance of confluent cultures of human epidermal keratinocytes. The
transcriptional upregulation was suppressed in the presence of a high
extracellular calcium concentration.
GENE STRUCTURE
Eckhart et al. (2000) determined that the CASP14 gene contains 7 exons.
MAPPING
Van de Craen et al. (1998) identified CASP14 sequences in a cosmid clone
assigned to chromosome 19p13.1 (GenBank GENBANK AF097874).
ANIMAL MODEL
Denecker et al. (2007) found that Casp14 -/- mice were born at the
expected mendelian ratio, were fertile and healthy, and showed long-term
survival indistinguishable from that of wildtype mice. However, the skin
of Casp14 -/- mice was shiny and lichenified. Casp14 -/- epidermis
contained significantly more alveolar keratohyalin F-granules, the
profilaggrin (135940) stores, and showed altered profilaggrin
processing. Casp14 -/- epidermis was characterized by reduced
skin-hydration levels and increased water loss, which could be explained
by aberrant filaggrin processing. The skin of Casp14 -/- mice was highly
sensitive to formation of cyclobutane pyrimidine dimers after
ultraviolet B (UVB) irradiation, leading to increased UVB-induced
apoptosis. Wildtype mice stripped of the stratum corneum were at least
as sensitive as nonstripped Casp14 -/- mice to UVB irradiation,
indicating that Casp14 controls the UBV scavenging capacity of stratum
corneum.
*FIELD* RF
1. Denecker, G.; Hoste, E.; Gilbert, B.; Hochepied, T.; Ovaere, P.;
Lippens, S.; Van den Broecke, C.; Van Damme, P.; D'Herde, K.; Hachem,
J.-P.; Borgonie, G.; Presland, R. B.; Schoonjans, L.; Libert, C.;
Vandekerckhove, J.; Gevaert, K.; Vandenabeele, P.; Declercq, W.:
Caspase-14 protects against epidermal UVB photodamage and water loss. Nature
Cell Biol. 9: 666-674, 2007.
2. Eckhart, L.; Ban, J.; Fischer, H.; Tschachler, E.: Caspase-14:
analysis of gene structure and mRNA expression during keratinocyte
differentiation. Biochem. Biophys. Res. Commun. 277: 655-659, 2000.
3. Van de Craen, M.; Van Loo, G.; Pype, S.; Van Criekinge, W.; Van
den brande, I.; Molemans, F.; Fiers, W.; Declercq, W.; Vandenabeele,
P.: Identification of a new caspase homologue: caspase-14. Cell
Death Differ. 5: 838-846, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 03/03/2008
*FIELD* CD
Dawn Watkins-Chow: 4/13/2001
*FIELD* ED
mgross: 03/03/2008
carol: 4/13/2001
*RECORD*
*FIELD* NO
605848
*FIELD* TI
*605848 CASPASE 14, APOPTOSIS-RELATED CYSTEINE PROTEASE; CASP14
*FIELD* TX
DESCRIPTION
read more
CASP14 belongs to the evolutionarily conserved caspase family. Caspases
are cysteinyl aspartate-specific proteinases, many of which play a
central role in apoptosis (Van de Craen et al., 1998). See CASP1
(147678) for additional background information on caspases.
CLONING
Using database searches for caspase sequences, Van de Craen et al.
(1998) identified CASP14 in human genomic sequence data and cloned both
human and mouse CASP14 cDNAs. By Northern blot and RT-PCR analyses, Van
de Craen et al. (1998) detected Casp14 expression in mouse skin and
developing mouse embryos (embryonic day 7, 15, 16, and 17). Expression
generally increased during maturation of the mouse embryo but dropped
temporarily to an undetectable level around embryonic day 11 to 12. The
authors suggested that Casp14 may play a role in ontogenesis and skin
physiology.
Eckhart et al. (2000) cloned a full-length CASP14 cDNA encoding a
242-amino acid protein with potential AP1 (165160) and KLF4 (602253)
interaction sites. They identified 2 CASP14 transcripts, designated
CASP14a and CASP14b, that differ in the C terminus due to a shifted open
reading frame. Use of an alternative splice acceptor site within intron
5 results in a 74-nucleotide insertion in CASP14b. CASP14b lacks
homology with the caspase consensus sequence and does not have a
counterpart in mouse. In situ hybridization analysis detected CASP14
within the epidermis, in hair follicles, and in the cells of the
sebaceous glands, with highest expression in the keratogenous zone and
the inner root sheeth of the hair follicle and in the peripheral cells
of the sebaceous glands.
Using immunohistochemical analysis, Denecker et al. (2007) confirmed
that mouse Casp14 was expressed only in cornifying epithelia, such as
the epidermis and Hassall bodies, and in forestomach, which is cornified
like epidermis.
GENE FUNCTION
Using Northern blot and semiquantitative RT-PCR analyses, Eckhart et al.
(2000) showed that CASP14 was transcriptionally upregulated during
maintenance of confluent cultures of human epidermal keratinocytes. The
transcriptional upregulation was suppressed in the presence of a high
extracellular calcium concentration.
GENE STRUCTURE
Eckhart et al. (2000) determined that the CASP14 gene contains 7 exons.
MAPPING
Van de Craen et al. (1998) identified CASP14 sequences in a cosmid clone
assigned to chromosome 19p13.1 (GenBank GENBANK AF097874).
ANIMAL MODEL
Denecker et al. (2007) found that Casp14 -/- mice were born at the
expected mendelian ratio, were fertile and healthy, and showed long-term
survival indistinguishable from that of wildtype mice. However, the skin
of Casp14 -/- mice was shiny and lichenified. Casp14 -/- epidermis
contained significantly more alveolar keratohyalin F-granules, the
profilaggrin (135940) stores, and showed altered profilaggrin
processing. Casp14 -/- epidermis was characterized by reduced
skin-hydration levels and increased water loss, which could be explained
by aberrant filaggrin processing. The skin of Casp14 -/- mice was highly
sensitive to formation of cyclobutane pyrimidine dimers after
ultraviolet B (UVB) irradiation, leading to increased UVB-induced
apoptosis. Wildtype mice stripped of the stratum corneum were at least
as sensitive as nonstripped Casp14 -/- mice to UVB irradiation,
indicating that Casp14 controls the UBV scavenging capacity of stratum
corneum.
*FIELD* RF
1. Denecker, G.; Hoste, E.; Gilbert, B.; Hochepied, T.; Ovaere, P.;
Lippens, S.; Van den Broecke, C.; Van Damme, P.; D'Herde, K.; Hachem,
J.-P.; Borgonie, G.; Presland, R. B.; Schoonjans, L.; Libert, C.;
Vandekerckhove, J.; Gevaert, K.; Vandenabeele, P.; Declercq, W.:
Caspase-14 protects against epidermal UVB photodamage and water loss. Nature
Cell Biol. 9: 666-674, 2007.
2. Eckhart, L.; Ban, J.; Fischer, H.; Tschachler, E.: Caspase-14:
analysis of gene structure and mRNA expression during keratinocyte
differentiation. Biochem. Biophys. Res. Commun. 277: 655-659, 2000.
3. Van de Craen, M.; Van Loo, G.; Pype, S.; Van Criekinge, W.; Van
den brande, I.; Molemans, F.; Fiers, W.; Declercq, W.; Vandenabeele,
P.: Identification of a new caspase homologue: caspase-14. Cell
Death Differ. 5: 838-846, 1998.
*FIELD* CN
Patricia A. Hartz - updated: 03/03/2008
*FIELD* CD
Dawn Watkins-Chow: 4/13/2001
*FIELD* ED
mgross: 03/03/2008
carol: 4/13/2001