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Thromb Haemost 1994; 71(04): 402-415
DOI: 10.1055/s-0038-1642451
DOI: 10.1055/s-0038-1642451
Review Article
Transglutaminases: Protein Cross-Linking Enzymes in Tissues and Body Fluids
Further Information
Publication History
Received: 09 November 1993
Accepted after revision: 12 January 1994
Publication Date:
06 July 2018 (online)
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References
- 1 Kanaji T, Ozaki H, Takao T, Kawajiri FI, Ide H, Motoki M, Shimonishi Y. Primary structure of microbial transglutaminase from Streptoverticillium sp. strain s-8112. J Biol Chem 1993; 268: 11565-72
- 2 Folk JE, Finlayson JS. The ∈-(γ-glutamyl)lysine cross-link and the catalytic role of transglutaminases. Adv Protein Chem 1977; 31: 1-133
- 3 Lorand L, Conrad SM. Transglutaminases. Mol Cell Biochem 1984; 58: 9-35
- 4 Folk JE, Cole PW, Mullooly JP. Mechanism of action of guinea pig liver transglutaminase: The metal-dependent hydrolysis of p-nitrophenyl acetate; further observations on the role of metal in enzyme activation. J Biol Chem 1967; 242: 2615-21
- 5 Gorman JJ, Folk JE. Structural features of glutamine substrates for transglutaminases: Specificities of human plasma factor XIIIa and the guinea pig liver enzyme toward synthetic peptides. J Biol Chem 1981; 256: 2712-5
- 6 Gorman JJ, Folk JE. Structural features of glutamine substrates for transglutaminases: Role of extended interactions in the specificity of human plasma factor XIIIa and the guinea pig liver enzyme. J Biol Chem 1984; 259: 9007-10
- 7 Aeschlimann D, Paulsson M, Mann K. Identification of Gin726 in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes. J Biol Chem 1992; 267: 11316-21
- 8 Shainoff JR, Urbanic DA, Di Bello PM. Immunoelectrophoretic characterizations of the cross-linking of fibrinogen and fibrin by factor XHIa and tissue transglutaminase. J Biol Chem 1991; 266: 6429-37
- 9 Fésus L, Metsis ML, Muszbek L, Koteliansky VE. Transglutaminase-sensitive glutamine residues of human plasma fibronectin revealed by studying its proteolytic fragments. Eur J Biochem 1986; 154: 371-4
- 10 Carrell NA, Erickson HP, McDonagh J. Electron microscopy and hydrodynamic properties of factor XIII subunits. J Biol Chem 1989; 264: 551-6
- 11 Grundmann U, Amann E, Zettlmeissl G, Küpper HA. Characterization of cDNA coding for human factor XIIIa. Proc Natl Acad Sci USA 1986; 83: 8024-8
- 12 Ichinose A, Hendrickson LE, Fujikawa K, Davie EW. Amino acid sequence of the a-subunit of human factor XIII. Biochemistry 1986; 25: 6900-6
- 13 Takahashi N, Takahashi Y, Putnam FW. Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta. Proc Natl Acad Sci USA 1986; 83: 8019-23
- 14 Takagi T, Doolittle RF. Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin. Biochemistry 1974; 13: 750-6
- 15 Greenberg CS, Birckbichler PJ, Rice RH. Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues. FASEB J 1991; 5: 3071-7
- 16 Weisberg LJ, Shiu DT, Conkling PR, Shuman MA. Identification of normal human peripheral blood monocytes and liver as sites of synthesis of coagulation factor XIII a-chain. Blood 1987; 70: 579-82
- 17 Poon MC, Russell JA, Low S, Sinclair GD, Jones AR, Blahey W, Ruether BA, Hoar DI. Hemopoietic origin of factor XIII a-subunits in platelets, monocytes and plasma. Evidence from bone marrow transplantation studies. J Clin Invest 1989; 84: 787-92
- 18 Tharaud C, Ribet AM, Costes C, Gaillardin C. Secretion of human blood coagulation factor-XIIIa by the yeast Yarrowia-Lipolytica. Gene 1992; 121: 111-9
- 19 Ichinose A, McMullen BA, Fujikawa K, Davie EW. Amino acid sequence of the b-subunit of human factor XIII, a protein composed of ten repetitive segments. Biochemistry 1986; 25: 4633-8
- 20 Ichinose A, Bottenus RE, Davie EW. Structure of transglutaminases. J Biol Chem 1990; 265: 13411-4
- 21 Lozier J, Takahashi N, Putnam FW. Complete amino acid sequence of human plasma ß2-glycoprotein I. Proc Natl Acad Sci USA 1984; 81: 3640-4
- 22 Bottenus RE, Ichinose A, Davie EW. Nucleotide sequence of the gene for the b-subunit of human factor XIII. Biochemistry 1990; 29: 11195-209
- 23 Gentile V, Saydak M, Chiocca EA, Akande O, Birckbichler PJ, Lee KN, Stein JP, Davies PJA. Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases. J Biol Chem 1991; 266: 478-83
- 24 Nakanishi K, Nara K, Hagiwara H, Aoyama Y, Ueno H, Hirose S. Cloning and sequence analysis of cDNA clones for bovine aortic-endothelial-cell transglutaminase. Eur J Biochem 1991; 202: 15-21
- 25 Ikura K, Nasu T, Yokota H, Tsuchiya Y, Sasaki R, Chiba H. Amino acid sequence of guinea pig liver transglutaminase from its cDNA sequence. Biochemistry 1988; 27: 2898-905
- 26 Weraarchakul-Boonmark N, Jeong JM, Murthy SNP, Engel JD, Lorand L. Cloning and expression of chicken erythrocyte transglutaminase. Proc Natl Acad Sci USA 1992; 89: 9804-8
- 27 Folk JE, Cole PW. Mechanism of action of guinea pig liver transglutaminase: Purification and properties of the enzyme; identification of a functional cysteine essential for activity. J Biol Chem 1966; 241: 5518-25
- 28 Boothe RL, Folk JE. A reversible, calcium-dependent, copper-catalyzed inactivation of guinea pig liver transglutaminase. J Biol Chem 1969; 244: 399-405
- 29 Ikura K, Yokota H, Sasaki R, Chiba H. Determination of amino- and carboxyl-terminal sequences of guinea pig liver transglutaminase: Evidence for amino-terminal processing. Biochemistry 1989; 28: 2344-8
- 30 Ikura K, Tsuchiya Y, Sasaki R, Chiba H. Expression of guinea - pig liver transglutaminase cDNA in Escherichia Coli: Amino-terminal Nα-acetyl group is not essential for catalytic function of transglutaminase. Eur J Biochem 1990; 187: 705-11
- 31 Muesch A, Hartmann E, Rohde K, Rubartelli A, Sitia R, Rapoport TA. A novel pathway for secretory proteins?. TIBS 1990; 15: 86-8
- 32 Aeschlimann D, Paulsson M. Cross-linking of laminin-nidogen complexes by tissue transglutaminase: A novel mechanism for basement membrane stabilization. J Biol Chem 1991; 266: 15308-17
- 33 Aeschlimann D, Wetterwald A, Fleisch H, Paulsson M. Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes. J Cell Biol 1993; 120: 1461-70
- 34 Barsigian C, Stem AM, Martinez J. Tissue (type II) transglutaminase covalently incorporates itself, fibrinogen, or fibronectin into high molecular weight complexes on the extracellular surface of isolated hepatocytes. J Biol Chem 1991; 266: 22501-9
- 35 Kojima S, Nara K, Rifkin DB. Requirement for transglutaminase in the activation of latent transforming growth factor-(β in bovine endothelial cells. J Cell Biol 1993; 121: 439-48
- 36 Clarke DD, Mycek MJ, Neidle A, Waelsch H. The incorporation of amines into protein. Arch Biochem Biophys 1959; 79: 338-54
- 37 Phillips MA, Stewart BE, Qin Q, Chakravarty R, Floyd EE, Jetten AM, Rice RH. Primary structure of keratinocyte transglutaminase. Proc Natl Acad Sci USA 1990; 87: 9333-7
- 38 Kim HC, Idler WW, Kim IG, Han JH, Chung SI, Steinert PM. The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones. I Biol Chem 1991; 266: 536-9
- 39 Chakravarty R, Rice RH. Acylation of keratinocyte transglutaminase by palmitic and myristic acids in the membrane anchorage region. J Biol Chem 1989; 264: 625-9
- 40 Rice RH, Rong X, Chakravarty R. Proteolytic release of keratinocyte transglutaminase. Biochem J 1990; 265: 351-7
- 41 Chakravarty R, Rong X, Rice RH. Phorbol ester-stimulated phosphorylation of keratinocyte transglutaminase in the membrane anchorage region. Biochem J 1990; 271: 25-30
- 42 Kim IG, Gorman JJ, Park SC, Chung SI, Steinert PM. The deduced sequence of the novel protransglutaminase E (TGase 3) of human and mouse. J Biol Chem 1993; 268: 12682-90
- 43 Wilson EM, French FS. Biochemical homology between rat dorsal prostate and coagulating gland. J Biol Chem 1980; 255: 10946-53
- 44 Ho KC, Quarmbv VE, French FS, Wilson EM. Molecular cloning of rat prostate transglutaminase cDNA: The major androgen-regulated protein- DP1 of rat dorsal prostate and coagulating gland. J Biol Chem 1992; 267: 12660-7
- 45 Seitz J, Keppler C, Hiintemann S, Rausch U, Aumüller G. Purification and molecular characterization of a secretory transglutaminase from coagulating gland of the rat. Biochim Biophys Acta 1991; 1078: 139-46
- 46 Seitz J, Keppler C, Rausch U, Aumiiller G. Immunohistochemistry of secretory transglutaminase from rodent prostate. Histochemistry 1990; 93: 525-30
- 47 Aumüller G, Steinhoff M, Keppler C, Rapoport CT, Seitz J. Secretory transglutaminase of rat coagulating gland: Characterization, mechanism of exocytosis and hormonal regulation. 3rd international conference on transglutaminases and protein cross-linking reactions. 1992. abstr 11. Samuel Roberts Noble Foundation Ardmore Oklahoma; USA:
- 48 Korsgren C, Lawler J, Lambert S, Speicher D, Cohen CM. Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2. Biochemistry 1990; 87: 613-7
- 49 Cohen CM, Dotimas E, Korsgren C. Human erythrocyte membrane protein band 4.2 (pallidin). Semin Hematol 1993; 30: 119-37
- 50 Risinger MA, Dotimas EM, Cohen CM. Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated. J Biol Chem 1992; 267: 5680-5
- 51 Sung LPA, Chien S, Fan YS, Lin CC, Lambert K, Zhu LY, Lam JS, Chang LS. Human erythrocyte protein-4.2: Isoform expression, differential splicing, and chromosomal assignment. Blood 1992; 79: 2763-70
- 52 Tokunaga F, Yamada M, Miyata T, Ding YL, Hiranaga-Kawabata M, Muta T, Iwanaga S. Limulus hemocyte transglutaminase: Its purification and characterization, and identification of the intracellular substrates. J Biol Chem 1993; 268: 252-61
- 53 Tokunaga F, Muta T, Iwanaga S, Ichinose A, Davie EW, Kuma KI, Miyata T. Limulus hemocyte transglutaminase: cDNA-cloning, amino acid sequence, and tissue localization. J Biol Chem 1993; 268: 262-8
- 54 Singer MA, Hortsch M, Goodman CS, Bentley D. Annulin, a protein expressed at limb segment boundaries in the grasshopper embryo, is homologous to protein cross-linking transglutaminases. Dev Biol 1992; 154: 143-59
- 55 Ichinose A, Davie EW. Characterization of the gene for the a-subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor. Proc Natl Acad Sci USA 1988; 85: 5829-33
- 56 Kim IG, McBride OW, Wang M, Kim SY, Idler WW, Steinert PM. Structure and organization of the human transglutaminase-1 gene. J Biol Chem 1992; 267: 7710-7
- 57 Phillips MA, Stewart BE, Rice RH. Genomic structure of keratinocyte transglutaminase. J Biol Chem 1992; 267: 2282-6
- 58 Korsgren C, Cohen CM. Organization of the gene for human erythrocyte membrane protein 4.2: Structural similarities with the gene for the a-subunit of factor XIII. Proc Natl Acad Sci USA 1991; 88: 4840-4
- 59 Chiocca EA, Davies PJA, Stein JP. The molecular basis of retinoic acid action. J Biol Chem 1988; 263: 11584-9
- 60 Moore WTJ, Murtaugh MP, Davies PJA. Retinoic acid-induced expression of tissue transglutaminase in mouse peritoneal macrophages. J Biol Chem 1984; 259: 12794-802
- 61 Nara K, Nakanishi K, Hagiwara H, Wakita KI, Kojima S, Hirose S. Retinol-induced morphological changes of cultured bovine endothelial cells are accompanied by a marked increase in transglutaminase. J Biol Chem 1989; 264: 19308-12
- 62 Piacentini M, Ceru MP, Dini L, Dirao M, Piredda L, Thomazy V, Davies PJA, Fésus L. In vivo and in vitro induction of tissue transglutaminase in rat hepatocytes by retinoic acid. Biochim Biophys Acta 1992; 1135: 171-9
- 63 Gentile V, Thomazy V, Piacentini M, Fésus L, Davies PJA. Expression of tissue transglutaminase in Balb-c 3T3 fibroblasts: Effects on cellular morphology and adhesion. J Cell Biol 1992; 119: 463-74
- 64 Davies PJA, Gentile V, Saydak M, Thomazy V, Gil D, Chandraratna R. Retinoid-receptor-regulated expression of tissue transglutaminase. 3rd international conference on transglutaminases and protein cross-linking reactions. 1992. Samuel Roberts Noble Foundation Ardmore Oklahoma; USA: abstr 4.
- 65 Verma AK, Shoemaker A, Simsiman R, Denning M, Zachman RD. Expression of retinoic acid nuclear receptors and tissue transglutaminase is altered in various tissues of rats fed a vitamin-A-deficient diet. J Nutr 1992; 122: 2144-52
- 66 Suto N, Ikura K, Shinagawa R, Sasaki R. Identification of promoter region of guinea pig liver transglutaminase gene. Biochim Biophys Acta 1993; 1172: 319-22
- 67 Suto N, Ikura K, Sasaki R. Expression induced by interleukin-6 of tissue- type transglutaminase in human hepatoblastoma HepG2 cells. J Biol Chem 1993; 268: 7469-73
- 68 Byrd JC, Lichti U. Two types of transglutaminase in the PC12 pheochromocytoma cell line. J Biol Chem 1987; 262: 11699-705
- 69 Kruh J. Effects of sodium butyrate, a new pharmacological agent, on cells in culture. Mol Cell Biochem 1982; 42: 65-82
- 70 Tanaka H, Shinki T, Takito J, Jin CH, Suda T. Transglutaminase is involved in the fusion of mouse alveolar macrophages induced by 1α,25-dihydroxyvitamin D3 . Exp Cell Res 1991; 192: 165-72
- 71 Liew FM, Yamanishi K. Regulation of transglutaminase-1 gene expression by 12-0-tetradecanoylphorbol-13-acetate, dexamethasone, and retinoic acid in cultured human kcratinocytes. Exp Cell Res 1992; 202: 310-5
- 72 Saunders NA, Bernacki SH, Vollberg TM, Jetten AM. Regulation of transglutaminase type I expression in squamous differentiating rabbit tracheal epithelial cells and human epidermal keratinocytes: Effects of retinoic acid and phorbol esters. Mol Endocrinol 1993; 7: 387-98
- 73 Lichti U, Ben T, Yuspa SH. Retinoic acid-induced transglutaminase in mouse epidermal cells is distinct from epidermal transglutaminase. J Biol Chem 1985; 260: 1422-6
- 74 Hold D, Mehrel T, Lichti U, Turner ML, Roop DR, Steinert PM. Characterization of human loricrm. J Biol Chem 1991; 266: 6626-36
- 75 Marvin KW, George MD, Fujimoto W, Saunders NA, Bernacki SH, Jetten AM. Cornifin, a cross-linked envelope precursor in keratinocytes that is down-regulated by reiinnids. Prnr Natl Acad Sci USA 1992; 89: 11026-30
- 76 George MD, Vollberg TM, Floyd FF, Stein IP, Jetten AM. Regulation of transglutaminase type II by transforming growth factor-pi in normal and transformed human epidermal keratinocytes. J Biol Chem 1990; 265: 11098-104
- 77 Hornyak TJ, Shafer JA. Role of calcium ion in the generation of factor XIII activity. Biochemistry 1991; 30: 6175-82
- 78 Kim HC, Lewis MS, Gorman JJ, Park SC, Girard IE, Folk JE, Chung SI. Protransglutaminase E from guinea pig skin. J Biol Chem 1990; 265: 21971-8
- 79 Chang SK, Chung SI. Cellular transglutaminase: The particulate-associated transglutaminase from chondrosarcoma and liver. J Biol Chem 1986; 261: 8112-21
- 80 Achyuthan KE, Greenberg CS. Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. J Biol Chem 1987; 262: 1901-6
- 81 Lee KN, Birckbichler PJ, Patterson Jr MK. GTP hydrolysis by guinea pig liver transglutaminase. Biochem Biophys Res Commun 1989; 162: 1370-5
- 82 Lee KN, Arnold SA, Birckbichler PJ, Patterson Jr MK, Fraij BM, Maxwell MD, Carter HA, Takeuchi Y. Chemical modification and site- directed mutagenesis of human tissue-type transglutaminase. 3rd international conference on transglutaminases and protein cross-linking reactions. 1992. Samuel Roberts Noble Foundation. Ardmore, Oklahoma; USA: abstr 22
- 83 Chen R, Doolittle RF. γ-γ Cross-linking sites in human and bovine fibrin. Biochemistry 1971; 10: 4486-91
- 84 Doolittle RF, Watt KWK, Cottrell BA, Strong DD, Riley M. The amino acid sequence of the a-chain of human fibrinogen. Nature 1979; 280: 464-8
- 85 Hornyak TJ, Shafer JA. Interactions of factor XIII with fibrin as substrate and cofactor. Biochemistry 1992; 31: 423-9
- 86 Achyuthan KE, Mary A, Greenberg CS. The binding sites on fibrin(ogen) for guinea pig liver transglutaminase are similar to those of blood coagulation factor XIII. J Biol Chem 1988; 263: 14296-301
- 87 Tamaki T, Aoki N. Cross-linking of α2-plasmin inhibitor to fibrin catalyzed by activated fibrin-stabilizing factor. J Biol Chem 1982; 257: 14767-72
- 88 Mortensen SB, Sottrup-Jensen L, Hansen HF, Rider D, Petersen TE, Magnusson S. Sequence location of a putative transglutaminase crosslinking site in human α2-macroglobulin. FEBS lett 1981; 129: 314-7
- 89 Mosher DF. Cross-linking of fibronectin to collagenous proteins. Mol Cell Biochem 1984; 58: 63-8
- 90 Lynch GW, Slayter HS, Miller BE, McDonagh J. Characterization of thrombospondin as a substrate for factor XIII transglutaminase. J Biol Chem 1987; 262: 1772-8
- 91 Sane DC, Moser TL, Pippen AMM, Parker CJ, Achyuthan KE, Greenberg CS. Vitronectin is a substrate for transglutaminases. Biochem Biophys Res Commun 1988; 157: 115-20
- 92 Skorstengaard K, Halkier T, Hojrup P, Mosher D. Sequence location of a putative transglutaminase cross-linking site in human vitronectin. FEBS Lett 1990; 262: 269-74
- 93 Borth W, Chang V, Bishop P, Harpel PC. Lipoprotein(a) is a substrate for factor XIIIa and tissue transglutaminase. J Biol Chem 1991; 266: 18149-53
- 94 Francis RT, McDonagh J, Mann KG. Factor V is a substrate for the trans-amidase factor XIIIa. J Biol Chem 1986; 261: 9787-92
- 95 Hada M, Kaminski M, Bockenstedt P, McDonagh J. Covalent crosslinking of von Willebrand factor to fibrin. Blood 1986; 68: 95-101
- 96 Jensen PH, Lorand L, Ebbesen P, Gliemann J. Type 2 plasminogen- activator inhibitor is a substrate for trophoblast transglutaminase and factor XIIIa: Transglutaminase-catalyzed cross-linking to cellular and extracellular structures. Eur J Biochcm 1993; 214: 141-6
- 97 Grinnell F, Feld M, Winter I. Fibroblast adhesion to fibrinogen and fihrin substrata: Requirement for cold-insoluble globulin (plasma fibronectin). Cell 1980; 19: 517-25
- 98 Barry ELR, Mosher DF. Binding and degradation of blood coagulation factor XIII by cultured fibroblasts. J Biol Chem 1990; 265: 9302-7
- 99 Barry ELR, Mosher DF. Factor XIIIa-mediated cross-linking of fibronectin in fibroblast cell layers. J Biol Chem 1989; 264: 4179-85
- 100 Quade BI, McDonald JA. Fibronectin's amino-terminal matrix assembly site is located within the 29-kDa amino-terminal domain containing five type I repeats. J Biol Chem 1988; 263: 19602-9
- 101 Lorand L, Losowsky MS, Miloszewski KJM. Human factor XIII: Fibrinstabilizing factor. Prog Hemostas Thromb 1980; 5: 245-90
- 102 Board P, Coggan M, Miloszewski K. Identification of a point mutation in factor-XIII a-subunit deficiency. Blood 1992; 80: 937-41
- 103 Fukue H, Anderson K, McPhedran P, Clyne L, McDonagh J. A unique factor XIII inhibitor to a fibrin-binding site on factor XIIIa. Blood 1992; 79: 65-74
- 104 Thomazy V, Fésus L. Differential expression of tissue transglutaminase in human cells. Cell Tissue Res 1989; 255: 215-24
- 105 Le Mosy EK, Erickson HP, Beyer WF, Radek JT, Jeong JM, Murthy SNP, Lorand L. Visualization of purified fibronectin-transglutaminase complexes. J Biol Chem 1992; 267: 7880-5
- 106 Bowness JM, Folk JE, Timpl R. Identification of a substrate site for liver transglutaminase on the aminopropeptide of type III collagen. J Biol Chem 1987; 262: 1022-4
- 107 Prince CW, Dickie D, Krumdieck CL. Osteopontin, a substrate for transglutaminase and factor XIII activity. Biochem Biophys Res Commun 1991; 177: 1205-10
- 108 Barsigian C, Fellin FM, Jain A, Martinez J. Dissociation of fibrinogen and fibronectin binding from transglutaminase-mediated cross-linking at the hepatocyte surface. J Biol Chem 1988; 263: 14015-22
- 109 Tyrrell DJ, Sale WS, Slife CW. Fibronectin is a component of the sodium dodecyl sulfate-insoluble transglutaminase substrate. J Biol Chem 1988; 263: 8464-9
- 110 Zatloukal K, Fésus L, Denk H, Tarcsa E, Spurej G, Bock G. High amount of ∈-(γ-glutamyl)lysine cross-links in Mallory bodies. Lab Invest 1992; 66: 774-7
- 111 Upchurch HF, Conway E, Patterson Jr MK, Maxwell MD. Localization of cellular transglutaminase on the extracellular matrix after wounding: Characteristics of the matrix bound enzyme. J Cell Physiol 1991; 149: 375-82
- 112 Eitan S, Schwartz M. A transglutaminase that converts interleukin-2 into a factor cytotoxic to oligodendrocytes. Science 1993; 261: 106-8
- 113 Takashi R. A novel actin label: A fluorescent probe at glutamine-41 and its consequences. Biochemistry 1988; 27: 938-43
- 114 Ando Y, Imamura S, Owada MK, Kannagi R. Calcium-induced intracellular cross-linking of lipocortin I by tissue transglutaminase in A431 cells. J Biol Chem 1991; 266: 1101-8
- 115 Green H. The keratinocyte as differentiated cell type. Harvey Led 1979; 74: 101-39
- 116 Fésus L, Davies PJA, Piacentini M. Apoptosis: Molecular mechanisms in programmed cell death. Eur J Cell Biol 1991; 56: 170-7
- 117 Fésus L, Thomazy V, Falus A. Induction and activation of tissue transglutaminase during programmed cell death. FEBS Lett 1987; 224: 104-8
- 118 Berbers GAM, Feenstra RW, Van Den Bos R, Hoekman WA, Bloemendal H, De Jong WW. Lens transglutaminase selects specific (β-crystallin sequences as substrate. Proc Natl Acad Sci USA 1984; 81: 7017-20
- 119 Lorand L, Velasco PT, Murthy SNP, Wilson J, Parameswaran KN. Isolation of transglutaminase-reactive sequences from complex biological systems: A prominent lysine donor sequence in bovine lens. Proc Natl Acad Sci USA 1992; 89: 11161-3
- 120 Groenen PJTA, Bloemendal H, De Jong WW. The carboxyl-terminal lysine of αβ-crystallin is an amine-donor substrate for tissue transglutaminase. Eur J Biochem 1992; 205: 671-4
- 121 Wiebe RI, Tarr AH, Bowness JM. Increased transglutaminase in the aortas of cholesterol-fed rabbits: Occurence of buffer soluble and insoluble forms and an inhibitor. Biochem Cell Biol 1991; 69: 821-7
- 122 Weinberg JB, Pippen AMM, Greenberg CS. Extravascular fibrin formation and dissolution in synovial tissue of patients with osteoarthritis and rheumatoid arthritis. Arthritis and Rheumatism 1991; 34: 996-1005
- 123 Cordella-Miele E, Miele L, Mukherjee AB. A novel transglutaminase-mediated posttranslational modification of phospholipase A 2dramatically increases its catalytic activity. J Biol Chem 1990; 265: 17180-8
- 124 Zettergren JG, Peterson LL, Wuepper KD. Keratolinin: The soluble substrate of epidermal transglutaminase from human and bovine tissue. Proc Natl Acad Sci USA 1984; 81: 238-42
- 125 Simon M, Green H. The glutamine residues reactive in transglutaminase-catalyzed cross-linking of involucrin. J Biol Chem 1988; 263: 18093-8
- 126 Eckert RL, Yaffe MB, Crish JF, Murthy S, Rorke EA, Welter JF. Involucrin: Structure and role in envelope assembly. J Invest Dermatol 1993; 100: 613-7
- 127 Kvedar JC, Manabe M, Phillips SB, Ross BS, Baden HP. Characterization of sciellin, a precursor to the cornified envelope of human keratinocytes. Differentiation 1992; 49: 195-204
- 128 Takahashi M, Tezuka T, Katunuma N. Phosphorylated cystatin a is a natural substrate of epidermal transglutaminase for formation of skin cornified envelope. FEBS Lett 1992; 308: 79-82
- 129 Bradway SD, Bergey EJ, Scannapieco FA, Ramasubbu N, Zawacki S, Levine MJ. Formation of salivary-mucosal pellicle: The role of transglutaminase. Biochem J 1992; 284: 557-64
- 130 Molhuizen HOF, Alkemade HAC, Zeeuwen PLJM, De Jongh GJ, Wieringa B, Schalkwijk J. SKALP/elafm: An elastase inhibitor from cultured human keratinocytes. J Biol Chem 1993; 268: 12028-32
- 131 Thacher SM, Rice RH. Keratinocyte-specific transglutaminase of cultured human epidermal cells: Relation to cross-linked envelope formation and terminal differentiation. Cell 1985; 40: 685-95
- 132 Martinet N, Kim HC, Girard JE, Nigra TP, Strong DH, Chung SI, Folk JE. Epidermal and hair follicle transglutaminases. J Biol Chem 1988; 263: 4236-41
- 133 Lee SC, Kim IG, Marekov LN, O’Keefe EJ, Parry DAD, Steinert PM. The structure of human trichohyalin: Potential multiple roles as a functional EF-hand-like calcium-binding protein, a cornified cell envelope precursor, and an intermediate filament-associated (cross-linking) protein. J Biol Chem 1993; 268: 12164-76
- 134 Williams-Ashman HG. Transglutaminases and the clotting of mammalian seminal fluids. Mol Cell Biochem 1984; 58: 51-61
- 135 Moore JT, Hagstrom J, McCormick DJ, Harvey S, Madden B, Holicky E, Stanford DR, Wieben ED. The major clotting protein from guinea pig seminal vesicle contains eight repeats of a 24-amino acid domain. Proc Natl Acad Sci USA 1987; 84: 6712-4
- 136 Porta R, Esposito C, Metafora S, Malorni A, Pucci P, Siciliano R, Marino G. Mass spectrometric identification of the amine donor and acceptor sites in a transglutaminase protein substrate secreted from rat seminal vesicles. Biochemistry 1991; 30: 3114-20
- 137 White RA, Peters LL, Adkison LR, Korsgren C, Cohen CM, Lux SE. The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene. Nature Genetics 1992; 2: 80-3
- 138 Fink ML, Chung SI, Folk JE. γ-Glutamylamine cyclotransferase: Specificity toward ∈-(L-γ-glutamyl)-L-lysine and related compounds. Proc Natl Acad Sci USA 1980; 77: 4564-8
- 139 Kuchler K, Thorner J. Membrane translocation of proteins without hydrophobic signal peptides. Curr Opin Cell Biol 1990; 2: 617-24
- 140 Rubartelli A, Cozzolino F, Talio M, Sitia R. A novel secretory pathway for interleukin-1(β, a protein lacking a signal sequence. EMBO J 1990; 9: 1503-10
- 141 Cooper DNW, Barondes SH. Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism. J Cell Biol 1990; 110: 1681-91
- 142 Lindstedt R, Apodaca G, Barondes SH, Mostov KE, Leffler H. Apical secretion of a cytosolic protein by Madin-Darby canine kidney cells: Evidence for polarized release of an endogenous lectin by a nonclassical secretory pathway. J Biol Chem 1993; 268: 11750-7
- 143 Mignatti P, Morimoto T, Rifkin DB. Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum-Golgi complex. J Cell Physiol 1992; 151: 81-93
- 144 McNeil PL, Muthukrishnan L, Warder E, D'Amore PA. Growth factors are released by mechanically wounded endothelial cells. J Cell Biol 1989; 109: 811-22
- 145 Phillips MA, Qin Q, Mehrpouyan M, Rice RH. Keratinocyte transglutaminase membrane anchorage: Analysis of site-directed mutants. Biochemistry 1993; 32: 11057-63