Kininogens, Kinins and Kinships

Werner Müller-Esterl

doi:10.1055/s-0038-1646516

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1989; 61(01): 002-006
DOI: 10.1055/s-0038-1646516

Review Article

Schattauer GmbH Stuttgart

Kininogens, Kinins and Kinships

Werner Müller-Esterl

The Department of Clinical Chemistry and Clinical Biochemistry, University of Munich, Munich, FRG

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Abstract

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References

References
1 Furie B, Furie BC. The molecular basis of blood coagulation. Cell 1988; 53: 505-518
2 Iwaarden Fvan, Bouma BN. Role of high molecular weight in contact activation. Sem Thromb Hemostas 1987; 13: 15-24
3 Kaplan AP, Silverberg M. The coagulation-kinin pathway of human plasma. Blood 1987; 70: 1-15
4 Müller-Esterl W, Iwanaga S, Nakanishi S. Kininogens revisited. Trends Biochem Sci 1986; 11: 336-339
5 Müller-Esterl W. Novel functions of kininogens. Semin Thromb Hemostas 1987; 13: 115-26
6 Chao J, Swain C, Chao S, Xiong W, Chao L. Tissue distribution and kininogen gene expression after acute-phase inflammation. Biochim Biophys Acta 1988; 329-339
7 Proud D, Perkins M, Pierce JV, Yates KN, Highet PF, Herring PL, Mangkornkanok M, Mark M, Bahu R, Carone F, Pisano JJ. Characterization and localization of human renal kininogen. J Biol Chem 1981; 10634-10639
8 Figueroa CD, MacIver AG, Mackenzie JC, Bhoola KD. Localisation of immunoreactive kininogen and tissue kallikrein in the human nephron. Histochemistry 1988; 89: 437-442
9 Schmaier AH, Zuckerberg A, Silverman C, Kuchibothla J, Tuszynski GP, Colman RW. High molecular weight kininogen: a secreted platelet protein. J Clin Invest 1983; 71: 1477-1489
10 Schmaier AH, Smith PM, Purdon AD, White JG, Colman RW. High molecular weight kininogen: localization in the unstimulated and activated platelet and activation by a platelet calpain(s). Blood 1986; 67: 119-130
11 van Iwaarden F, de Groot PG, Sixma JJ, Berrettini M, Bouma BN. High-molecular weight kininogen is present in cultured human endothelial cells - localization, isolation and characterization. Blood 1988; 71: 1268-1276
12 van Iwaarden F, de Groot PG, Bouma BN. The binding of high-molecular weight kininogen tocultured human endothelial cells. J Biol Chem 1988; 263: 4698-4703
13 Shimada T, Kato H, Iwanaga S. Accelerating effect of zinc ions on the surface-mediated activation of factor XI and prekallikrein. J Biochem 1987; 102: 913-921
14 Greengard JS, Griffin JH. Receptors for high molecular weight kininogen on stimulated washed human platelets. Biochemistry 1984; 23: 6863-6869
15 Elliott DF, Lewis GP, Horton EW. The structure of bradykinin - a plasma kinin from ox blood. Biochem Biophys Res Commun 1960; 3: 87-91
16 Boisonnas RA, Guttmann S, Jaquenoud PA, Konzett H, Sturmer E. Synethesis and biological activity of peptides related to bradykinin. Experientia 1960; 16: 326
17 Mindroiu T, Scicli G, Perini F, Carretero OA, Scicli AG. Identification of a new kinin in human urine. J Biol Chem 1986; 261: 7407-7411
18 Kato H, Matsumuara Y, Maeda H. Isolation and identification of hydroxyproline analogues of bradykinin in human urine. FEBS Lett 1988; 232: 252-254
19 Maier M, Ressert G, Jerabek I, Lottspeich F, Binder BR. Identification of (hydroxyproline³)-lysyl-bradykinin released from human kininogens by human urinary kallikrein. FEBS Lett 1988; 232: 395-398
20 Sasaguri M, Ikeda M, Ideishi M, Arakawa K. Identification of (hydroxyproline³)-lysyl-bradykinin released from human plasma protein by kallikrein. Biochem Biophys Res Commun 1988; 150: 511-516
21 Mindroiu T, Carretero OA, Proud D, Walz D, Scicli AG. A new kinin moiety in human plasma kininogens. Biochem Biophys Res Commun 1988; 152: 519-526
22 Maeda H, Matsumura Y, Kato H. Purification and identification of hydroxyprolyl³-bradykinin is ascitic fluid from a patient with gastric cancer. J Biol Chem 1988; 263: 16051-4
23 Kishimura H, Yasuhara T, Yoshida H, Nakajima T. Vespakinin-M, a novel bradykinin analogue containing hydroxyproline in the venom of Vespa mandarinia Smith. Chem Pharm Bull 1976; 24: 2896-2897
24 Erspamer V, Yasuhara T, Nakajima T. The new vasoactive peptides in amphibian skin. Adv Exp Med Biol 1979; 120 A 7-13
25 Rhoads RE, Udenfriend S. Substrate specificity of collagen proline hydroxylase: hydroxylation of a specific proline residue in bradykinin. Arch Biochem Biophys 1969; 133: 108-111
26 McGee JO, Rhoads RE, Udenfriend S. The substrate recognition site of collagen proline hydroxylase: the hydroxylation of -X-Pro-Gly- sequences in bradykinin analogs and other peptides. Arch Biochem Biophys 1971; 144: 343-351
27 Enjyoji K, Kato H. Hydroxyprolyl³-bradykinin in high molecular weight kininogen: presence in human and monkey kininogens, but not in kininogens from bovine, rat, rabbit, guineas pig, and mouse plasma. FEBS Lett 1988; 238: 1-4
28 Ohkubo I, Kurachi K, Takasawa T, Shiowaka H, Sasaki M. Isolation of a human cDNA for α₂-thiol proteinase inhibitor and its identity with low molecular weight kininogen. Biochemistry 1984; 23: 5691-5697
29 Sueyoshi T, Enjyoji K, Shimada T, Kato H, Iwanaga S, Bando Y, Kominami E, Katunuma N. A new function of kininogens as thiol proteinase inhibitors: inhibition of papain and cathepsins B, H and L by bovine, rat and human plasma kininogens. FEBS Lett 1985; 182: 193-195
30 Müller-Esterl W, Fritz H, Machleidt W, Ritonja A, Brzin J, Kotnik M, Turk V, Kellermann J, Lottspeich F. Human plasma kininogens are identical with α₂-cysteine proteinase inhibitors. Evidence from immunological, enzymological and sequence data FEBS Lett 1985; 182: 310-314
31 Kitamura N, Kitagawa H, Fukushima D, Takagaki Y, Miyata T, Nakanishi S. Structural organization of the human kininogen gene and a model for its evolution. J Biol Chem 1985; 260: 8610-8697
31a Kellermann J, Lottspeich F, Henschen A, Müller-Esterl W. Completion of the primary structure of human high-molecular-mass kininogen. The amino acid sequence of the entire heavy chain and evidence for its evolution by gene triplication Eur J Biochem 1986; 154: 471-478
32 Salvesen G, Parker C, Abrahamson M, Grubb A, Barrett AJ. Human low-M_r kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine pro- teinases. Biochem J 1986; 234: 429-434
33 Vogel R, Assfalg-Machleidt I, Esterl A, Machleidt W, Müller-Esterl W. Proteinase-sensitive regions in the heavy chain of low molecular weight kininogen map to the interdomain junctions. J Biol Chem 1988; 263: 12661-12668
34 Müller-Esterl W, Fritz H, Kellermann J, Lottspeich F, Machleidt W, Turk V. Genealogy of mammalian cysteine proteinase inhibitorsCommon evolutionary origin of stefins, cystatins and kininogens. FEBS Lett 1985; 191: 221-226
35 Kellermann J, Thelen C, Lottspeich F, Henschen A, Vogel R, Müller-Esterl W. Arrangement of the disulphide bridges in human low-M_rkininogen. Biochem J 1987; 247: 15-21
36 Barrett AJ, Fritz H, Grubb A, Isemura S, Järvinen M, Katunuma N, Machleidt W, Müller-Esterl W, Sasaki M, Turk V. Nomenclature and classification of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin. Biochem J 1986; 236: 312
36a Barrett AJ. The cystatins: a new class of peptidase inhibitors. Trends Biochem Sci 1987; 12: 193-196
37 Koide T, Odani S. Histidine-rich glycoprotein is evolutionary related to the cystatin superfamily Presence of two cystatin domains in the N-terminal region. FEBS Lett 1987; 216: 17-21
38 Elzanowski A, Barker WC, Hunt LT, Seibel-Ross E. Cystatin domains in α₂-HS glycoprotein and fetuin. FEBS Lett 1988; 227: 167-170
39 Lee CC, Bowman BH, Yang F. Human α₂-HS glycoprotein: the A and B chains with a connecting sequence are encoded by a single mRNA transcript. Proc Natl Acad Sci USA 1987; 84: 4403-4407
40 Sueyoshi T, Miyata T, Hashimoto N, Kato H, Hayashida H, Miyata T, Iwanaga S. Bovine high molecular weight kininogen. The amino acid sequence, positions of carbohydrate chains, and disulfide bridges in the heavy chain portion J Biol Chem 1987; 262: 2768-2779
41 Tait J, Fijikawa K. Identification of the binding site for plasma prekallikrein in human high molecular weight kininogen A region from residues 185 to 224 of the kininogen light chain retains full binding activity. J Biol Chem 1986; 261: 15396-15401
42 Tait J, Fujikawa K. Primary structure requirements for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI. J Biol Chem 1987; 262: 11651-11656
43 Kitagawa H, Kitamura N, Hayashida H, Miyata T, Nakanishi S. Differing expression patterns and evolution of the rat kininogen gene family. J Biol Chem 1987; 262: 2190-2198
44 Kakizuka A, Kitamura N, Nakanishi S. Localization of DNA sequences governing alternative mRNA production of rat kininogen genes. J Biol Chem 1988; 263: 3884-3889
45 Fung WP, Schreiber G. Structure and expression of the genes for major acute phase α₁-protein (thiostatin) and kininogen in the rat. J Biol Chem 1987; 262: 9298-9308
46 Kageyama R, Kitamura N, Ohkubo H, Nakanishi S. Differing utilization of homologous transcription initiation sites of rat K- and T- kininogen genes under inflammation conditions. J Biol Chem 1987; 262: 2345-2351
47 Gilbert W. Why genes in pieces. Nature 1978; 271: 501
48 Patthy L. Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules. Cell 1985; 41: 657-663
49 Nakanishi S. Substance P precursor and kininogen: their structures, gene organizations, and regulation. Physiol Rev 1987; 67: 1117-1142
50 Proud D, Kaplan AP. Kinin formation: mechanisms and role in inflammatory disorders. Annu Rev Immunol 1988; 6: 49-83
51 Drinkwater CC, Evans BA, Richards RI. Kallikreins, kinins and growth factor biosynthesis. Trends Biochem Sci 1988; 13: 169-172
52 MacDonald R, Margolius HS, Erdös EG. Molecular biology of tissue kallikrein. Biochem J 1988; 253: 313-321
53 Walsh PN. Platelet-mediated trigger mechanisms in the contact phase of blood coagulation. Sem Thromb Hemostas 1987; 13: 86-94
54 Okamoto H, Greenbaum LM. Isolation and structure of T-kinin. Biochem Biophys Res Commun 1983; 112: 701-708
55 Sakamoto W, Satoh F, Gotoh K, Uehara S. Ile-Ser-bradykinin (T-kinin) and Met-Ile-Ser-bradykinin (Met-T-kinin) are released from T-kininogen by an acid proteinase of granulomatous tissue in rats. FEBS Lett 1987; 219: 437-440
56 Sakajnoto W, Satoh F, Nagasawa S, Handa H. Identification of T- kinin-Leu (T-kinin containing peptide) released from T-kininogen by cathepsin D of granulomatous tissues in rats. Biochem Biophys Res Commun 1988; 150: 1199-1206
57 Kimura M, Sueyoshi T, Takada K, Tanaka K, Morita T, Iwanaga S. Isolation and characterization of ornitho-kininogen. Eur J Biochem 1987; 168: 493-501
58 Hiwasa T, Yokoyama S, Ha JM, Noguchi S, Sakiyama S. c-Ha-ras gene products are potent inhibitors of cathepsins B and L. FEBS Lett 1987; 211: 23-26
59 Hiwasa T. Internally repeated sequences in ras gene products. Biochem J 1988; 254: 621-624
60 Enjyoji K, Kato H, Hayashi I, Oh-ishi S, Iwanaga S. Purification and characterization of rat T-kininogens isolated from plasma of adjuvant- treated rats. Identification of three types of T-kininogens J Biol Chem 1988; 263: 973-979