Mouse matriptase-2: identification, characterization and comparative mRNA expression analysis with mouse hepsin in adult and embryonic tissues

被引:70
作者
Hooper, JD [1 ]
Campagnolo, L [1 ]
Goodarzi, G [1 ]
Truong, TN [1 ]
Stuhlmann, H [1 ]
Quigley, JP [1 ]
机构
[1] Scripps Res Inst, Div Vasc Biol, Dept Cell Biol, La Jolla, CA 92037 USA
关键词
hepsin; membrane; mouse matriptase-2; serine protease;
D O I
10.1042/BJ20030390
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We report the identification and characterization of mouse matriptase-2 (m-matriptase-2), an 811-amino-acid protein composed of an N-terminal cytoplasmic domain, a membranespanning domain, two CUB (complement protein subcomponents C1r/C1s, urchin embryonic growth factor and bone morphogenetic protein 1) domains, three LDLR (low-density-lipoprWe report the identification and characterization of mouse matriptase-2 (m-matriptase-2), an 811-amino-acid protein composed of an N-terminal cytoplasmic domain, a membranespanning domain, two CUB (complement protein subcomponents Clr/Cls, urchin embryonic growth factor and bone morphogenefic protein 1) domains, three LDLR (low-densitylipoprotein receptor class A) domains and a C-terminal serineprotease domain. All m-matriptase-2 protein domain boundaries corresponded with intron/exon junctions of the encoding gene, which spans approx. 29 kb and comprises 18 exons. Matriptase-2 is highly conserved in human, mouse and rat, with the rat matriptase-2 gene (r-nialtriptase-2) predicted to encode transmembrane and soluble isoforms. Western-blot analysis indicated that m-matriptase-2 migrates close to its theoretical molecular mass of 91 kDa, and immunofluorescence analysis was consistent with the proposed surface membrane localization of this protein. Reverse-transcription PCR and in-situ-hybridization analysis indicated that m-matriptase-2 expression overlaps with the distribution of mouse hepsin (m-hepsin, a cell-surface serine protease identified in hepatoma cells) in adult tissues and duringotein receptor class A) domains and a C-terminal serineprotease domain. All m-matriptase-2 protein domain boundaries corresponded with intron/exon junctions of the encoding gene, which spans approx. 29 kb and comprises 18 exons. Matriptase-2 is highly conserved in human, mouse and rat, with the rat matriptase-2 gene (r-maltriptase-2) predicted to encode transmembrane and soluble isoforms. Western blot analysis indicated that m-matriptase-2 migrates close to its theoretical molecular mass of 91 kDa, and immunofluorescence analysis was consistent with the proposed surface membrane localization of this protein. Reverse-transcription PCR and in-situ-hybridization analysis indicated that m-matriptase-2 expression overlaps with the distribution of mouse hepsin (m-hepsin, a cell-surface serine protease identified in hepatoma cells) in adult tissues and during embryonic development. In adult tissues both are expressed at highest levels in liver, kidney and uterus. During embryogenesis m-matriptase-2 expression peaked between days 12.5 and 15.5. m-hepsin expression was biphasic, with peaks at day 7.5 to 8.5 and again between days 12.5 and 15.5. In situ hybridization of embryonic tissues indicated abundant expression of both m-matriptase-2 and m-hepsin in the developing liver and at lower levels in developing pharyngo-tympanic tubes. While m-hepsin was detected in the residual embryonic yolk sac and with lower intensity in lung, heart, gastrointestinal tract, developing kidney tubules and epithelium of the oral cavity, m-matriptase-2 was absent in these tissues, but strongly expressed within the nasal cavity by olfactory epithelial cells. Mechanistic insight into the potential role of this new transmembrane serine protease is provided by its novel expression profile in embryonic and adult mouse.
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页码:689 / 702
页数:14
相关论文
共 59 条
[1]  
Afar DEH, 2001, CANCER RES, V61, P1686
[2]   Sequence and structure-based prediction of eukaryotic protein phosphorylation sites [J].
Blom, N ;
Gammeltoft, S ;
Brunak, S .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 294 (05) :1351-1362
[3]   N-terminal processing is essential for release of epithin, a mouse type II membrane serine protease [J].
Cho, EG ;
Kim, MG ;
Kim, C ;
Kim, SR ;
Seong, IS ;
Chung, CH ;
Schwartz, RH ;
Park, D .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (48) :44581-44589
[4]   Delineation of prognostic biomarkers in prostate cancer [J].
Dhanasekaran, SM ;
Barrette, TR ;
Ghosh, D ;
Shah, R ;
Varambally, S ;
Kurachi, K ;
Pienta, KJ ;
Rubin, MA ;
Chinnaiyan, AM .
NATURE, 2001, 412 (6849) :822-826
[5]   Decrease and gain of gene expression are equally discriminatory markers for prostate carcinoma -: A gene expression analysis on total and microdissected prostate tissue [J].
Ernst, T ;
Hergenhahn, M ;
Kenzelmann, M ;
Cohen, CD ;
Bonrouhi, M ;
Weninger, A ;
Klären, R ;
Gröne, EF ;
Wiesel, M ;
Güdemann, C ;
Küster, J ;
Schott, W ;
Staehler, G ;
Kretzler, M ;
Hollstein, M ;
Gröne, HJ .
AMERICAN JOURNAL OF PATHOLOGY, 2002, 160 (06) :2169-2180
[6]   The PROSITE database, its status in 2002 [J].
Falquet, L ;
Pagni, M ;
Bucher, P ;
Hulo, N ;
Sigrist, CJA ;
Hofmann, K ;
Bairoch, A .
NUCLEIC ACIDS RESEARCH, 2002, 30 (01) :235-238
[7]  
FONSECA P, 1983, J BIOL CHEM, V258, P4516
[8]   Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase [J].
Friedrich, R ;
Fuentes-Prior, P ;
Ong, E ;
Coombs, G ;
Hunter, M ;
Oehler, R ;
Pierson, D ;
Gonzalez, R ;
Huber, R ;
Bode, W ;
Madison, EL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (03) :2160-2168
[9]   Mutations in the proenteropeptidase gene are the molecular cause of congenital enteropeptidase deficiency [J].
Holzinger, A ;
Maier, EM ;
Bück, C ;
Mayerhofer, PU ;
Kappler, M ;
Haworth, JC ;
Moroz, SP ;
Hadorn, HB ;
Sadler, JE ;
Roscher, AA .
AMERICAN JOURNAL OF HUMAN GENETICS, 2002, 70 (01) :20-25
[10]   Localization of the mosaic transmembrane serine protease corin to heart myocytes [J].
Hooper, JD ;
Scarman, AL ;
Clarke, BE ;
Normyle, JF ;
Antalis, TM .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2000, 267 (23) :6931-6937