Bikunin - Not just a plasma proteinase inhibitor

International Journal of Biochemistry and Cell Biology

Volumn 32, Issue 2, 2000, Pages 125-137

  Fries, Erik ^a   Blom, Anna M ^b  

^a UPPSALA UNIVERSITY   (Sweden)

^b LUND UNIVERSITY   (Sweden)

Author keywords

Bikunin; Calcium blocker; Inflammation; Inter inhibitor; Proteinase inhibitor

Indexed keywords

BLOOD CLOTTING FACTOR 10A; CALCIUM; CALCIUM CHANNEL BLOCKING AGENT; CELL SURFACE PROTEIN; INTER ALPHA TRYPSIN INHIBITOR; KALLIKREIN; PLASMIN; PROTEIN SUBUNIT; PROTEINASE INHIBITOR; ULINASTATIN;

BLOOD CLOTTING; CALCIUM CELL LEVEL; CELL GROWTH; COMPLEX FORMATION; ENZYME INHIBITION; GENE EXPRESSION; GENETIC ORGANIZATION; HUMAN; INFLAMMATION; METASTASIS; MOLECULAR WEIGHT; NEPHROLITHIASIS; NONHUMAN; PLASMA CLEARANCE; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW; TISSUE DISTRIBUTION;

EID: 0033987191     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(99)00125-9     Document Type: Article

References (117)

1. Bauer J., Reich Z. Über die antitryptische Wirkung des Harns. Med. Klin. 46:1909;1744-1746.
2. Dillard G.H.L. The trypsin inhibitor of the urine in health and disease. J. Lab. Clin. Med. 36:1950;266-271.
3. Balduyck M., Hayem A., Kerckaert J.P., Mizon C., Mizon J. Isolation of human urinary trypsin inhibitor. Biochem. Biophys. Res. Commun. 109:1982;1247-1255.
4. Shulman N.R. A proteolytic inhibitor with anti-coagulant activity separated from human urine and plasma. J. Biol. Chem. 213:1955;655-671.
5. Ødum L., Ingwersen S. Electrophoretic investigations of acid-stable proteinase-inhibitory activity in human serum. Hoppe-Seyler's Z. Physiol. Chem. 364:1983;1671-1677.
6. Laroui S., Balduyck M., Mizon C., Selloum L., Mizon J. Plasma proteins immunologically related to inter-α-trypsin inhibitor. Biochim. Biophys. Acta. 953:1988;263-268.
7. Sugiki M., Sumi H., Maruyama M., Yoshida E., Mihara H. Clearance and distribution of acid-stable trypsin inhibitor (ASTI). Enzyme. 42:1989;31-38.
8. Hochstrasser K., Bretzel G., Feuth H., Hilla W., Lempart K. The inter-α-trypsin inhibitor as precursor of the acid-stable proteinase inhibitors in human serum and urine. Hoppe-Seyler's Z. Physiol. Chem. 357:1976;153-162.
9. Hochstrasser K., Wachter E. Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-α-inhibitor, I: determination of the amino-acid sequence of the antitryptic domain by solid-phase Edman degradation. Hoppe-Seyler's Z. Physiol. Chem. 360:1979;1285-1296.
10. Faarvagn H.J. Urinary trypsin inhibitor in man (mingin). Scand. J. Clin. Lab. Inv. 17:1965;1-78.
11. 1-microglobulin in human urine. Clin. Chim. Acta. 227:1994;195-200.
12. Gebhard W., Hochstrasser K., Fritz H., Enghild J.J., Pizzo S.V., Salvesen G. Structure of inter-α-inhibitor (inter-α-trypsin inhibitor) and pre-α-inhibitor: current state and proposition of a new terminology. Biol. Chem. Hoppe-Seyler. 371:1990;13-22.
13. Wachter E., Hochstrasser K. Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-α-trypsin inhibitor, IV: the amino acid sequence of the human urinary trypsin inhibitor isolated by affinity chromatography. Hoppe-Seyler's Z. Physiol. Chem. 362:1981;1351-1355.
14. Chirat F., Balduyck M., Mizon C., Laroui S., Sautiere P., Mizon J. A chondroitin-sulfate chain is located on serine-10 of the urinary trypsin inhibitor. Int. J. Biochem. 23:1991;1201-1203.
15. Tanaka Y., Maehara S., Sumi H., Toki N., Moriyama S., Sasaki K. Purification and partial characterization of two forms of urinary trypsin inhibitor. Biochim. Biophys. Acta. 705:1982;192-199.
16. 1-microglobulin: co-expression in liver with the light chain of inter-α-trypsin inhibitor. Biochim. Biophys. Acta. 1130:1992;63-67.
17. 1-microglobulin/bikunin precursor (AMBP) gene expression during amphibian metamorphosis. Dev. Genes Evol. 206:1997;355-362.
18. 1-microglobulin/bikunin mRNA: cloning of a cDNA from plaice (Pleuronectes platessa). Comp. Bioch. Physiol. 108B:1994;275-281.
19. Xu Y., Carr P.D., Guss J.M., Ollis D.L. The crystal structure of bikunin from the inter-α-inhibitor complex: a serine poteinase inhibitor with two Kunitz domains. J. Mol. Biol. 276:1998;955-966.
20. Swaim M.W., Pizzo S.V. Modification of the tandem reactive centres of human inter-α-trypsin inhibitor with butanedione and cis-dichlorodiammineplatinum (II). Biochem. J. 254:1988;171-178.
21. Kjellén L., Lindahl U. Proteoglycans: structures and interactions. Annu. Rev. Biochem. 60:1991;443-475.
22. Toyoda H., Kobayashi S., Sakamoto S., Toida T., Imanari T. Structural analysis of a low-sulfated chondroitin sulfate chain in human urinary trypsin inhibitor. Biol. Pharm. Bull. 16:1993;945-947.
23. Yamada S., Oyama M., Kinugasa H., Nakagawa T., Kawasaki T., Nagasawa S., Khoo K.H., Morris H.R., Dell A., Sugahara K. The sulphated carbohydrate-protein linkage region isolated from chondroitin-4-sulphate chains of inter-α-trypsin inhibitor in human plasma. Glycobiology. 5:1995;335-341.
24. Sjöberg E.M., Fries E. One of the major sulphated proteins secreted by rat hepatocytes contains low-sulphated chondroitin sulphate. Biochem. J. 272:1990;113-118.
25. Sjöberg E.M., Fries E. Biosynthesis of bikunin (urinary trypsin inhibitor) in rat hepatocytes. Arch. Biochem. Biophys. 295:1992;217-222.
26. Yamada S., Oyama M., Yuki Y., Kato K., Sugahara K. The uniform galactose 4-sulfate structure in the carbohydrate-protein linkage region of human urinary trypsin inhibitor. Eur. J. Biochem. 233:1995;687-693.
27. Toyoda H., Ikey T., Demachi Y., Toida T., Imanari T. Structural analysis of the N-linked oligosaccharides from human urinary trypsin inhibitor. Chem. Pharm. Bull. 40:1992;2882-2884.
28. Enghild J.J., Salvesen G., Thøgersen I.B., Valnickova Z., Pizzo S.V., Hefta S.A. Presence of the protein-glycosaminoglycan-protein covalent cross-link in the inter-α-related proteinase inhibitor heavy chain 2/bikunin. J. Biol. Chem. 268:1993;8711-8716.
29. Y. Yuki, K. Nomura, M. Kirihara, M. Shimomura, H. Hiratani, R. Nishimura, K. Kato, Charge isomers of urinary bikunin (trypsin inhibitor), Biochim. Biophys. Acta 1203 (1993) 298-303.
30. Lindström K.E., Blom A., Johnsson E., Haraldsson B., Fries E. High glomerular permeability of bikunin despite similarity in charge and hydrodynamic size to serum albumin. Kidney Int. 51:1997;1053-1058.
31. Slota A., Sjöquist M., Wogast M., Alston-Smith J., Fries E. Bikunin in rat plasma, lymph and bile. Biol. Chem. Hoppe-Seyler. 375:1994;127-133.
32. Chan P., Risler J.L., Raguenez G., Salier J.P. The three heavy-chain precursors for the inter-α-inhibitor family in mouse: new members of the multicopper oxidase protein group with differential transcription in liver and brain. Biochem. J. 306:1995;505-512.
33. Salier J.P., Rouet P., Raguenez G., Daveau M. The inter-α-inhibitor family: from structure to regulation. Biochem. J. 315:1996;1-9.
34. Bost F., Diarra-Mehrpour M., Martin J.-P. Inter-α-trypsin inhibitor proteoglycan family. Eur. J. Biochem. 252:1998;339-346.
35. Ødum L., Hansen-Nord G., Byrjalsen I. Human inter-α-trypsin inhibitor and immunologically related inhibitors investigated by quantitative immunoelectrophoresis. II. Pathological conditions. Clin. Chim. Acta. 162:1987;189-198.
36. Blom A., Pertoft H., Fries E. Inter-α-inhibitor is required for the formation of the hyaluronan-containing coat on fibroblasts and mesothelial cells. J. Biol. Chem. 270:1995;9698-9701.
37. Thøgersen I.B., Enghild J.J. Biosynthesis of bikunin proteins in the human carcinoma cell line HepG2 and in primary human hepatocytes. J. Biol. Chem. 270:1995;18700-18709.
38. Enghild J.J., Salvesen G., Hefta S.A., Thøgersen I.B., Rutherfurd S., Pizzo S.V. Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-α-inhibitor. J. Biol. Chem. 266:1991;747-751.
39. Morelle W., Capon C., Balduyck M., Sautiere P., Kouach M., Michalski C., Fournet B., Mizon J. Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-α-trypsin inhibitor. Eur. J. Biochem. 221:1994;881-888.
40. Kaumeyer J.F., Polazzi J.O., Kotick M.P. The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-α-trypsin inhibitor also encodes α-1-microglobulin (protein HC). Nucleic Acids Res. 14:1986;7839-7850.
41. 1-microglobulin. Trends Biochem. Sci. 15:1990;240-243.
42. Hosaka M., Nagahama M., Kim W., Watanabe T., Hatsuzawa K., Nakayama K. Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalysed by furin within the constitutive secretory pathway. J. Biol. Chem. 266:1991;12127-12130.
43. Bratt T., Olsson H., Sjöberg E.M., Jergil B., Åkerström B. Cleavage of the αl-microglobulin-bikumin precursor is localized to the Golgi apparatus of rat liver cells. Biochim. Biophys. Acta. 1157:1993;147-154.
44. Bourguignon J., Diarra M.M., Thiberville L., Bost F., Sesboüé R., Martin J.P. Human pre-α-trypsin inhibitor-precursor heavy chain. CDNA and deduced amino-acid sequence. Eur. J. Biochem. 212:1993;771-776.
45. Thuveson M., Fries E. Intracellular proteolytic processing of the heavy chain of rat pre-α-inhibitor. J. Biol. Chem. 274:1999;6741-6746.
46. Diarra-Mehrpour M., Bourguignon J., Sesboüé R., Salier J.P., Leveillard T., Martin J.P. Structural analysis of the human inter-α-trypsin inhibitor light-chain gene. Eur. J. Biochem. 191:1990;131-139.
47. 1-microglobulin-bikunin gene. Biol. Chem. Hoppe-Seyler. 371:1990;1185-1196.
48. 1-microglobulin/bikunin mRNA transcripts. Mol. Marine Biol. Biotech. 4:1995;105-109.
49. 1-microglobulin/bikunin gene. J. Biol. Chem. 267:1992;20765-20773.
50. 1-microglobulin/bikunin precursor. Biochem. J. 334:1998;577-584.
51. 1-microglobulin/HI-30 reveals developmental and tissue-specific expression of two variant messenger ribonucleic acids. Biochim. Biophys. Acta. 1088:1991;47-56.
52. Salier J.P., Chan P., Raguenez G., Zwingman T., Erickson R.P. Developmentally regulated transcription of the four liver-specific genes for inter-α-inhibitor family in mouse. Biochem. J. 296:1993;85-91.
53. 1-microglobulin mRNA in the rat. J. Biol. Chem. 261:1986;15070-15074.
54. Thomas T., Southwell B.R., Schreiber G., Jaworowski A. Plasma protein synthesis and secretion in the visceral yolk sac of the fetal rat: gene expression, protein synthesis and secretion. Placenta. 11:1990;413-430.
55. Trefz G., Streit B., Justus C.W., Ebert W., Kramer M.D. Establishment of an enzyme-linked immuno-sorbent assay for urinary trypsin inhibitor by using a monoclonal antibody. J. Immunoassay. 12:1991;347-369.
56. Chawla R.K., Miller F.W., Lawson D.H., Nixon D.W. Urinary cancer-related protein EDCl and serum inter-α-trypsin inhibitor in breast cancer. Tumor Biol. 5:1984;351-363.
57. Chawla R.K., Lawson D.H., Ahmad M., Travis J. Cancer-related urinary proteinase inhibitor, EDCl: a new method for its isolation and evidence for multiple forms. J. Cell. Biochem. 50:1992;227-236.
58. Kuwajima S., Matsui T., Kitahashi S., Kishida T., Noda T., Izumi Y., Naka K., Okuda K. Automated measurement of trypsin inhibitor in urine with a centrifugal analyzer: comparison with other acute phase reactants. Clin. Biochem. 23:1990;167-171.
59. Sugiki M., Maruyama M., Yoshida E., Sumi H., Mihara H. Acid-stable protease inhibitor in chronic phase of carrageenan-induced inflammation in rats. Inflammation. 15:1991;281-289.
60. Franck C., Pedersen J.Z. Trypsin-inhibitory activities of acid-stable fragments of the inter-α-inhibitor in inflammatory and uraemic conditions. Scand. J. Clin. Lab. Invest. 43:1983;151-155.
61. Liony C., Sesbüé R., Manchon N.D., Bercoff E., Delzant G., Martin J.P., Bourreille J. Inter-alpha-trypsine inhibiteur et ses dérivés dans les syndromes inflammatoires. Presse Med. 20:1991;203-206.
62. Daveau M., Rouet P., Scotte M., Faye L., Hiron M., Lebreton J.P., Salier J.P. Human inter-alpha-inhibitor family in inflammation: simultaneous synthesis of positive and negative acute-phase proteins. Biochem. J. 292:1993;485-492.
63. Daveau M., Jean L., Soury E., Olivier E., Masson S., Lyoumi S., Chan P., Hiron M., Lebreton J.P., Husson A., Jegou S., Vaudry H., Salier J.P. Hepatic and extra-hepatic transcription of inter-α-inhibitor family genes under normal or acute inflammatory conditions in rat. Arch. Biochem. Biophys. 350:1998;315-323.
64. 1-microglobulin concentrations in urine of rats during pregnancy is due to decreased tubular reabsorption. Biochim. Biophys. Acta. 1361:1997;198-202.
65. Balduyck M., Piva F., Mizon C., Maes P., Malki N., Gressier B., Michalski C., Mizon J. Human leucocyte elastase (HLE) preferentially cleaves the heavy chain H2 of inter-α-trypsin inhibitor (ITI). Biol. Chem. Hoppe-Seyler. 374:1993;895-901.
66. Hochstrasser K., Reisinger P.W.M., Albrecht G.J., Wustrow T.P.U. Proteaseinhibitoren als tumorassoziierte Wachstumsfaktoren. Laryngo-Rhino-Otol. 68:1989;51-56.
67. Faarvang H.J. Relation between pituary-adrenal system and excretion of trypsin inhibitor in urine. Proc. Exp. Biol. 98:1958;89-91.
68. Faarvang H.J., Lauritsen O.S. Relationship between serum concentration and urinary output of trypsin inhibitor after cortisone administration. Scand. J. Clin. Lab. Invest. 15:1963;483-490.
69. Shikimi T., Suzuki S. Human urinary trypsin inhibitor (Urinastatin)-like substance in mouse kidney and its relationship to mouse kidney kallikrein. Biol. Chem. Hoppe-Seyler. 371:1990;991-997.
70. Shikimi T., Suzuki S., Wessel T., Joh T.H., Hattori K., Takaori S. Human urinary trypsin inhibitor (urinastatin)-like substance in mouse liver. Life Sci. 50:1992;1399-1406.
71. Businaro R., Leali F.M., De Rg, Pompili E., Pagliari G., Menghi G., Fumagalli L. Inter-α-trypsin inhibitor-related immunoreactivity in human tissues and body fluids. Cell. Mol. Biol. 38:1992;463-471.
72. L. Ødum, Immunohistochemical investigation of inter-α-trypsin inhibitor in the urinary tract, APMIS 97 (1989) 357-360.
73. Shikimi T., Hattori K., Takaori S. Existence of a human urinary trypsin inhibitor (urinastatin)-like substance in the rat brain. Japan. J. Pharmacol. 60:1992;97-103.
74. Yoshida E., Sumi H., Maruyama M., Tsushima H., Matsuoka Y., Sugiki M., Mihara H. Distribution of acid stable trypsin inhibitor immunoreactivity in normal and malignant human tissues. Cancer. 64:1989;860-869.
75. Hochstrasser K., Niebel J., Feuth H., Lempart K. Über Abbauprodukte des Inter-α-Trypsininhibitors im Serum. Klin. Wschr. 55:1977;337-342.
76. Nishino N., Aoki K., Tokura Y., Sakaguchi S., Fujie M., Sugawara Y., Takada Y., Takada A. Measurements of urinary trypsin inhibitor in urine, plasma and cancer tissues of patients with stomach cancer. Haemostasis. 19:1989;112-119.
77. Jönsson B.M., Ohlsson K. Distribution and elimination of intravenously injected urinary trypsin inhibitor. Scand. J. Clin. Lab. Invest. 51:1991;549-557.
78. Sjöberg E.M., Blom A., Sjöquist M., Wolgast M., Alston-Smith J., Fries E. Plasma clearance of rat bikunin: evidence of receptor mediated uptake. Biochem. J. 308:1995;881-887.
79. Hochstrasser K., Feuth H., Fall J., Kemkes B. Särestabile Proteaseninhibitoren im Blutplasma bei verschiedenen Nephropathien. Klin. Wschr. 52:1974;1015-1017.
80. Balduyck M., Davril M., Mizon C., Smyrlaki M., Hayem A., Mizon J. Human urinary proteinase inhibitor: inhibitory properties and interaction with bovine trypsin. Biol. Chem. Hoppe-Seyler. 366:1985;9-14.
81. Bromke B.J., Kueppers F. The major urinary protease inhibitor: simplified purification and characterization. Biochem. Med. 27:1982;56-67.
82. Jönsson B.M., Löffler C., Ohlsson K. Human granulocyte elastase is inhibited by the urinary trypsin inhibitor. Hoppe-Seyler's Z. Physiol. Chem. 363:1982;1167-1175.
83. Albrecht G.J., Hochstrasser K., Salier J.P. Elastase inhibition by the inter-α-trypsin inhibitor and derived inhibitors of man and cattle. Hoppe-Seyler's Z. Physiol. Chem. 364:1983;1703-1708.
84. Hochstrasser K., Albrecht G.J., Schönberger ÖL, Wachter E. Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-α-trypsin inhibitor, VIII. Characterization of the bovine inhibitor as double-headed trypsin-elastase inhibitor. Hoppe-Seyler's Z. Physiol. Chem. 364:1983;1689-1696.
85. Lambin P., Fine J.M., Steinbuch M. Inhibition of plasmin by a small molecular weight inhibitor derived from human inter-α-inhibitor. Thromb. Res. 13:1978;563-568.
86. Fritz H., Heimburger N., Meier M., Arnhold M., Zaneveld L.J.D., Schumacher G.F.B. Humanakrosin: zur Kinetik der Hemmung durch Human-seruminhibitoren. Hoppe-Zeyler's Z. Physiol. Chem. 353:1972;1953-1956.
87. Potempa J., Kwon K., Chawla R., Travis J. Inter-α-trypsin inhibitor. Inhibition spectrum of native and derived forms. J. Biol. Chem. 264:1989;15109-15114.
88. Pratt C.W., Pizzo S.V. Mechanism of action of inter-α-trypsin inhibitor. Biochemistry. 26:1987;2855-2863.
89. Morishita H., Yamakawa T., Matsusue T., Kusuyama T., Sameshima-Aruga R., Hirose J., Nii A., Miura T., Isaji M., Horisawa-Nakano R., Nagase Y., Kanamori T., Nobuhara M., Tanaka R., Koyama S., Naotsuka M. Novel factor Xa and plasma kallikrein inhibitory activities of the second Kunitz-type inhibitory domain of urinary trypsin inhibitor. Thromb. Res. 73:1994;193-204.
90. Kobayashi H., Shinohara H., Takeuchi K., Itoh M., Fujie M., Saitoh M., Tearo T. Inhibition of the soluble and the tumor cell receptor-bound plasmin by urinary trypsin inhibitor and subsequent effects on tumor cell invasion and metastasis. Cancer Res. 54:1994;844-849.
91. Kobayashi H., Fuije M., Shinohara H., Ohi H., Sugimura M., Terao T. Effects or urinary trypsin inhibitor on the invasion of reconstituted basement membranes by ovarian cancer cells. Int. J. Cancer. 57:1994;378-384.
92. Lee T.H., Wisniewski H.G., Vilcek J. A novel secretory tumor necrosis factor inducible protein (TSG-6) is a member of the family of hyaluronate binding proteins, closely related to the adhesion receptor CD44. J. Cell. Biol. 116:1992;545-557.
93. Wisniewski H.G., Maier R., Lotz M., Lee S., Klampfer L., Lee T.H., Vilcek J. TSG-6: a TNF, IL-1 and LPS inducible secreted glycoprotein associated with arthritis. J. Immunol. 151:1993;6593-6601.
94. Wisniewski H.G., Burgess W.H., Oppenheim J.D., Vilcek J. TSG-6, an arthritis-associated hyaluronan binding protein, forms a stable complex with the serum protein inter-α-inhibitor. Biochemistry. 33:1994;7423-7429.
95. Wisniewski H., Hua J.-C., Poppers D.M., Naime D., Vilcek J., Cronstein B.N. TNF/IL-1-inducible protein TSG-6 potentiates plasmin inhibition by inter-α-inhibitor and exerts a strong anti-inflammatory effect in vivo. J. Immunol. 156:1996;1609-1615.
96. Kido H., Yokogoshi Y., Katunuma N. Kunitz-type protease inhibitor found in rat mast cells. J. Biol. Chem. 263:1988;18104-18107.
97. Itoh H., Ide H., Ishikawa N., Nawa Y. Mast cell protease inhibitor, trypstatin, is a fragment of inter-α-trypsin inhibitor light chain. J. Biol. Chem. 269:1994;3818-3822.
98. Hochstrasser K., Gebhard W., Albrecht G., Rasp G., Kastenbauer E. Interaction of human mast cell tryptase and chymase with low-molecular-mass serine proteinase inhibitors from the human respiratory tract. Eur. Arch. Otorhinolaryng. 249:1993;455-458.
99. Hochstrasser K., Reichert R., Heimburger N. Antigenic relationship between the human bronchial mucus inhibitor and plasma inter-α-trypsin inhibitor. Hoppe-Seyler's Z. Physiol. Chem. 354:1973;587-588.
100. Ohlsson K., Tegner H., Fritz H., Schiessler H. Immunological similarity between low molecular weight trypsin-chymotrypsin inhibitors from human bronchial secretion and seminal plasma. Hoppe-Seyler's Z. Physiol. Chem. 357:1976;1241-1244.
101. Hoshi H., McKeehan W.L. Brain- and liver cell-derived factors are required for growth of human endothelial cells in serum-free culture. Proc. Natl. Acad. Sci. USA. 81:1984;6413-6417.
102. McKeehan W.L., Sakagami Y., Hoshi H., McKeehan K.A. Two apparent human endothelial cell growth factors from human hepatoma cells are tumor-associated proteinase inhibitors. J. Biol. Chem. 261:1986;5378-5383.
103. Perry J.K., Scott G.K., Tse C.A. Modulation of proliferation of cultured human cells by urinary trypsin inhibitor. Biochim. Biophys. Acta. 1221:1994;145-152.
104. Manilal S.B., Scott G.K. Further evidence for the mitogenic action of urinary trypsin inhibitor. Biochem. Molec. Biol. Intern. 39:1996;711-720.
105. Kobayashi H., Hirashima Y., Sun G.W., Fujie M., Shibata S., Tamotsu S., Miura K., Sugino D., Terao T. Internalization of urinary trypsin inhibitor in human uterine fibroblasts. Biochim. Biophys. Acta. 1383:1998;253-268.
106. +2 in human neutrophils and HUVEC cells. Biochem. Biophys. Res. Comm. 207:1995;324-330.
107. ++ influx. Am. J. Obstet. Gynecol. 173:1995;192-199.
108. Kaga N., Katsuki Y., Futamura Y., Obata M., Shibutani Y. Role of urinary trypsin inhibitor in the maintenance of pregnancy in mice. Obstet. Gynecol. 88:1996;872-882.
109. Maradny E.E., Kanayama N., Halim A., Maehara K., Terao T. Urinary trypsin inhibitor has a protective effect on the amnion. Gynecol. Obstet. Invest. 38:1994;169-172.
110. 2+ influx. Biochim. Biophys. Acta. 1381:1998;139-146.
111. Tani T., Aoki H., Yoshioka T., Lin K.J., Kodama M. Treatment of septic shock with a protease inhibitor in a canine model: a prospective, randomized, controlled trial. Crit. Care Med. 21:1993;925-930.
112. Chen L., Mao J.T., McLean L.R., Powers R.W., Larsen W.J. Proteins of the inter-α-trypsin inhibitor family stabilize the cumulus extracellular matrix through their direct binding with hyaluronic acid. J. Biol. Chem. 269:1994;28282-28287.
113. Chen L., Zhang H., Powers R.W., Russel P.T., Larsen W.J. Covalent linkage between proteins of the inter-α-inhibitor family and hyaluronic acid is mediated by a factor produced by granulosa cells. J. Biol. Chem. 271:1996;19409-19414.
114. Zhao M., Yoneda M., Okashi Y., Kurona S., Iwata H., Ohnuki Y., Kimata K. Evidence for the covalent binding of SHAP, heavy chains of inter-α-trypsin inhibitor to hyaluronan. J. Biol. Chem. 270:1995;26657-26663.
115. Hutadilok N., Ghosh P., Brooks P.M. Binding of haptoglobin, inter-α-trypsin inhibitor and α1-proteinase inhibitor to synovial fluid hyaluronate and the influence of these proteins on its degradation by oxygen derived free radicals. Ann. Rheum. Dis. 47:1988;377-385.
116. Atmani F., Mizon J., Khan S.R. Identification of uronic-acid-rich protein as urinary bikunin, the light chain of inter-α-inhibitor. Eur. J. Biochem. 236:1996;984-990.
117. Medetognon-Benissan J., Tardivel S., Hennequin C., Daudon M., Drueke T., Lacour B. Inhibitory effect of bikunin on calcium oxalate crystallization in vitro and urinary bikunin decrease in renal stone formers. Urol. Res. 27:1999;69-75.