메뉴 건너뛰기




Volumn 59, Issue 2, 2011, Pages 180-187

In situ detection of active transglutaminases for keratinocyte type (tgase 1) and tissue type (tgase 2) using fluorescence-labeled highly reactive substrate peptides

Author keywords

Calcium; Connective tissue; Epithelium; Transglutaminase

Indexed keywords

PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; TRANSGLUTAMINASE 1; UNCLASSIFIED DRUG; FLUORESCENT DYE; GUANINE NUCLEOTIDE BINDING PROTEIN; ISOENZYME; OLIGOPEPTIDE;

EID: 79953780725     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1369/jhc.2010.957225     Document Type: Article
Times cited : (37)

References (35)
  • 1
    • 0032488822 scopus 로고    scopus 로고
    • Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes: Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers
    • Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF. 1998. Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes: detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers. J Biol Chem. 273:3452-3460.
    • (1998) J Biol Chem , vol.273 , pp. 3452-3460
    • Aeschlimann, D.1    Koeller, M.K.2    Allen-Hoffmann, B.L.3    Mosher, D.F.4
  • 2
    • 77950579354 scopus 로고    scopus 로고
    • Transglutaminase 1 preferred substrate peptide K5 is an efficient tool in diagnosis of lamellar ichthyosis
    • Akiyama M, Sakai K, Yanagi T, Fukushima S, Ihn H, Hitomi K, Shimizu H. 2010. Transglutaminase 1 preferred substrate peptide K5 is an efficient tool in diagnosis of lamellar ichthyosis. Am J Pathol. 176:1592-1599.
    • (2010) Am J Pathol , vol.176 , pp. 1592-1599
    • Akiyama, M.1    Sakai, K.2    Yanagi, T.3    Fukushima, S.4    Ihn, H.5    Hitomi, K.6    Shimizu, H.7
  • 3
    • 4143117776 scopus 로고    scopus 로고
    • The transglutaminase family: An overview
    • Beninati S, Piacentini M. 2004. The transglutaminase family: an overview. Amino Acids. 26:367-372.
    • (2004) Amino Acids , vol.26 , pp. 367-372
    • Beninati, S.1    Piacentini, M.2
  • 4
    • 17144371855 scopus 로고    scopus 로고
    • The cornified envelope: A model of cell death in the skin
    • Candi E, Schmidt R, Melino G. 2005. The cornified envelope: a model of cell death in the skin. Nat Rev Mol Cell Biol. 6:328-340.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 328-340
    • Candi, E.1    Schmidt, R.2    Melino, G.3
  • 6
    • 0029861911 scopus 로고    scopus 로고
    • Transglutaminase from rat coagulating gland secretion: Post-translational modification and activation by phosphatidic acids
    • Esposito C, Pucci P, Amoresano A, Marino G, Cozzolino A, Porta R. 1996. Transglutaminase from rat coagulating gland secretion: post-translational modification and activation by phosphatidic acids. J Biol Chem. 271:27416-27423.
    • (1996) J Biol Chem , vol.271 , pp. 27416-27423
    • Esposito, C.1    Pucci, P.2    Amoresano, A.3    Marino, G.4    Cozzolino, A.5    Porta, R.6
  • 7
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: An enigmatic enzyme with diverse functions
    • Fesus L, Piacentini M. 2002. Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem Sci. 27: 534-539.
    • (2002) Trends Biochem Sci , vol.27 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 8
    • 0035150905 scopus 로고    scopus 로고
    • A simple assay and histochemical localization of transglutaminase activity using a derivative of green fluorescent protein as substrate
    • Furutani Y, Kato A, Notoya M, Ghoneim MA, Hirose S. 2001. A simple assay and histochemical localization of transglutaminase activity using a derivative of green fluorescent protein as substrate. J Histochem Cytochem. 49:247-258.
    • (2001) J Histochem Cytochem , vol.49 , pp. 247-258
    • Furutani, Y.1    Kato, A.2    Notoya, M.3    Ghoneim, M.A.4    Hirose, S.5
  • 9
    • 0035980007 scopus 로고    scopus 로고
    • Evolution of transglutaminase genes: Identification of a transglutaminase gene cluster on human chromosome 15q15
    • Grenard P, Bates MK, Aeschlimann D. 2001. Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. J Biol Chem. 276:33066-33078.
    • (2001) J Biol Chem , vol.276 , pp. 33066-33078
    • Grenard, P.1    Bates, M.K.2    Aeschlimann, D.3
  • 10
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • Griffin M, Casadio R, Bergamini CM. 2002. Transglutaminases: nature's biological glues. Biochem J. 368:377-396.
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 11
    • 0033607637 scopus 로고    scopus 로고
    • Transglutaminase type 1 and its cross-linking activity are concentrated at adherens junctions in simple epithelial cells
    • Hiiragi T, Sasaki H, Nagafuchi A, Sabe H, Shen SC, Matsuki M, Yamanishi K, Tsukita S. 1999. Transglutaminase type 1 and its cross-linking activity are concentrated at adherens junctions in simple epithelial cells. J Biol Chem. 274:34148-34154.
    • (1999) J Biol Chem , vol.274 , pp. 34148-34154
    • Hiiragi, T.1    Sasaki, H.2    Nagafuchi, A.3    Sabe, H.4    Shen, S.C.5    Matsuki, M.6    Yamanishi, K.7    Tsukita, S.8
  • 12
    • 25144501535 scopus 로고    scopus 로고
    • Transglutaminase in skin epidermis
    • Hitomi K. 2005. Transglutaminase in skin epidermis. Eur J Dermatol. 15:313-319.
    • (2005) Eur J Dermatol , vol.15 , pp. 313-319
    • Hitomi, K.1
  • 13
    • 69949094931 scopus 로고    scopus 로고
    • A specific colorimetric assay for measuring transglutaminase 1 and factor XIII activities
    • Hitomi K, Kitamura M, Perez Alea M, Ceylon I, Thomas V, El Alaoui S. 2009. A specific colorimetric assay for measuring transglutaminase 1 and factor XIII activities. Anal Biochem. 394:281-283.
    • (2009) Anal Biochem , vol.394 , pp. 281-283
    • Hitomi, K.1    Kitamura, M.2    Perez Alea, M.3    Ceylon, I.4    Thomas, V.5    El Alaoui, S.6
  • 14
    • 62949246332 scopus 로고    scopus 로고
    • Preferred substrate sequences for transglutaminase 2: Screening using a phagedisplayed peptide library
    • Hitomi K, Kitamura M, Sugimura Y. 2009. Preferred substrate sequences for transglutaminase 2: screening using a phagedisplayed peptide library. Amino Acids. 36:619-624.
    • (2009) Amino Acids , vol.36 , pp. 619-624
    • Hitomi, K.1    Kitamura, M.2    Sugimura, Y.3
  • 16
    • 0034924217 scopus 로고    scopus 로고
    • Physiopathology and regulation of factor XIII
    • Ichinose A. 2001. Physiopathology and regulation of factor XIII. Thromb Haemost. 86:57-65.
    • (2001) Thromb Haemost , vol.86 , pp. 57-65
    • Ichinose, A.1
  • 17
    • 32844458075 scopus 로고    scopus 로고
    • Role of protein modification mediated by transglutaminase 2 in human viral diseases
    • Jeon JH, Kim IG. 2006. Role of protein modification mediated by transglutaminase 2 in human viral diseases. Front Biosci. 11:221-231.
    • (2006) Front Biosci , vol.11 , pp. 221-231
    • Jeon, J.H.1    Kim, I.G.2
  • 18
    • 0036715005 scopus 로고    scopus 로고
    • Epithelial barrier function: Assembly and structural features of the cornified cell envelop
    • Kalinin AE, Kajava AV, Steinert PM. 2002. Epithelial barrier function: assembly and structural features of the cornified cell envelop. BioEssays. 24:789-800.
    • (2002) BioEssays , vol.24 , pp. 789-800
    • Kalinin, A.E.1    Kajava, A.V.2    Steinert, P.M.3
  • 19
    • 0038607621 scopus 로고    scopus 로고
    • Use of a new adhesive film for the preparation of multi-purpose fresh-frozen sections from hard tissues, wholeanimals, insects and plants
    • Kawamoto T. 2003. Use of a new adhesive film for the preparation of multi-purpose fresh-frozen sections from hard tissues, wholeanimals, insects and plants. Arch Histrol Cytol. 66:123-143.
    • (2003) Arch Histrol Cytol , vol.66 , pp. 123-143
    • Kawamoto, T.1
  • 20
    • 0034043852 scopus 로고    scopus 로고
    • A method for preparing 2- to 50-μm-thick fresh frozen section of large samples and undecalcified hard tissues
    • Kawamoto T, Shimizu M. 2000. A method for preparing 2- to 50-μm-thick fresh frozen section of large samples and undecalcified hard tissues. Histochem Cell Biol. 113:331-339.
    • (2000) Histochem Cell Biol , vol.113 , pp. 331-339
    • Kawamoto, T.1    Shimizu, M.2
  • 21
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand L, Graham RM. 2003. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol. 4:140-156.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 23
    • 62949150350 scopus 로고    scopus 로고
    • Biological and therapeutic significance of tissue transglutaminase in pancreatic cancer
    • Mehta K. 2009. Biological and therapeutic significance of tissue transglutaminase in pancreatic cancer. Amino Acids. 36: 709-716.
    • (2009) Amino Acids , vol.36 , pp. 709-716
    • Mehta, K.1
  • 24
    • 32844467408 scopus 로고    scopus 로고
    • Tissue transglutaminase: From biological glue to cell survival cues
    • Mehta K, Fok JY, Mangala LS. 2006. Tissue transglutaminase: from biological glue to cell survival cues. Front Biosci. 11:173-185.
    • (2006) Front Biosci , vol.11 , pp. 173-185
    • Mehta, K.1    Fok, J.Y.2    Mangala, L.S.3
  • 26
    • 33645808724 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-2 is expressed in different types of congenital ichthyosis: In vivo evidence for its cross-linking into the cornified cell envelope by transglutaminase-1
    • Oji V, Oji ME, Adamini N, Walker T, Aufenvenne K, Raghunath M, Traupe H. 2006. Plasminogen activator inhibitor-2 is expressed in different types of congenital ichthyosis: in vivo evidence for its cross-linking into the cornified cell envelope by transglutaminase-1. Br J Dermatol. 154:860-867.
    • (2006) Br J Dermatol , vol.154 , pp. 860-867
    • Oji, V.1    Oji, M.E.2    Adamini, N.3    Walker, T.4    Aufenvenne, K.5    Raghunath, M.6    Traupe, H.7
  • 27
    • 67349084359 scopus 로고    scopus 로고
    • Development of an isozyme-specific colorimetric assay for tissue transglutaminase 2 cross-linking activity
    • Perez Alea M, Kitamura M, Martin G, Thomas V, Hitomi K, El Alaoui S. 2009. Development of an isozyme-specific colorimetric assay for tissue transglutaminase 2 cross-linking activity. Anal Biochem. 389:150-156.
    • (2009) Anal Biochem , vol.389 , pp. 150-156
    • Perez Alea, M.1    Kitamura, M.2    Martin, G.3    Thomas, V.4    Hitomi, K.5    El Alaoui, S.6
  • 28
    • 34249808244 scopus 로고    scopus 로고
    • Transglutaminase 2 in neurogenerative disease
    • Ruan Q, Johnson GV. 2007. Transglutaminase 2 in neurogenerative disease. Front Biosci. 12:891-904.
    • (2007) Front Biosci , vol.12 , pp. 891-904
    • Ruan, Q.1    Johnson, G.V.2
  • 30
    • 0036715684 scopus 로고    scopus 로고
    • Coeliac disease: Dissecting a complex inflammatory disorder
    • Sollid LM. 2002. Coeliac disease: dissecting a complex inflammatory disorder. Nat Rev Immunol. 2:647-655.
    • (2002) Nat Rev Immunol , vol.2 , pp. 647-655
    • Sollid, L.M.1
  • 31
    • 54849408758 scopus 로고    scopus 로고
    • Identification of preferred substrate sequences for transglutaminase 1: Development of a novel peptide that can efficiently detect cross-linking enzyme activity in the skin
    • Sugimura Y, Hosono M, Kitamura M, Tsuda T, Yamanishi K, Maki M, Hitomi K. 2008. Identification of preferred substrate sequences for transglutaminase 1: development of a novel peptide that can efficiently detect cross-linking enzyme activity in the skin. FEBS J. 275:5667-5677.
    • (2008) FEBS J , vol.275 , pp. 5667-5677
    • Sugimura, Y.1    Hosono, M.2    Kitamura, M.3    Tsuda, T.4    Yamanishi, K.5    Maki, M.6    Hitomi, K.7
  • 32
    • 33745846379 scopus 로고    scopus 로고
    • Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: Identification of peptide substrates for TGase 2 and factor XIIIa
    • Sugimura Y, Hosono M, Wada F, Yoshimura T, Maki M, Hitomi K. 2006. Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: identification of peptide substrates for TGase 2 and factor XIIIa. J Biol Chem. 281:17699-17706.
    • (2006) J Biol Chem , vol.281 , pp. 17699-17706
    • Sugimura, Y.1    Hosono, M.2    Wada, F.3    Yoshimura, T.4    Maki, M.5    Hitomi, K.6
  • 33
    • 34547510883 scopus 로고    scopus 로고
    • Novel site-specific immobilization of functional protein using a preferred substrate sequence for transglutaminase 2
    • Sugimura Y, Ueda H, Maki M, Hitomi K. 2007. Novel site-specific immobilization of functional protein using a preferred substrate sequence for transglutaminase 2. J Biotechnol. 131:121-127.
    • (2007) J Biotechnol , vol.131 , pp. 121-127
    • Sugimura, Y.1    Ueda, H.2    Maki, M.3    Hitomi, K.4
  • 35
    • 77952780489 scopus 로고    scopus 로고
    • Imaging enzymes at work: Metabolic mapping by enzyme histochemistry
    • Van Nooden CJF. 2010. Imaging enzymes at work: metabolic mapping by enzyme histochemistry. J Histochem Cytochem. 58:481-497.
    • (2010) J Histochem Cytochem , vol.58 , pp. 481-497
    • van Nooden, C.J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.