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Volumn 153, Issue 4, 1998, Pages 1267-1276

Bikunin present in human peritoneal fluid is in part derived from the interaction of serum with peritoneal mesothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TRYPSIN INHIBITOR; DECORIN; PROTEOCHONDROITIN SULFATE; ULINASTATIN; UNCLASSIFIED DRUG;

EID: 0031695122     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)65671-4     Document Type: Article
Times cited : (5)

References (57)
  • 1
    • 0025381189 scopus 로고
    • New concepts in molecular biology and ultrastructural pathology of the peritoneum: Their significance for peritoneal dialysis
    • Dobbie JW: New concepts in molecular biology and ultrastructural pathology of the peritoneum: their significance for peritoneal dialysis. Am J Kidney Dis 1990, 15:97-109
    • (1990) Am J Kidney Dis , vol.15 , pp. 97-109
    • Dobbie, J.W.1
  • 2
    • 0023735401 scopus 로고
    • Phosphatidylcholine synthesis by peritoneal mesothelium: Its implications for peritoneal dialysis
    • Dobbie JW, Pavlina T, Lloyd J, Johnson RC: Phosphatidylcholine synthesis by peritoneal mesothelium: its implications for peritoneal dialysis. Am J Kidney Dis 1988, 12:31-36
    • (1988) Am J Kidney Dis , vol.12 , pp. 31-36
    • Dobbie, J.W.1    Pavlina, T.2    Lloyd, J.3    Johnson, R.C.4
  • 3
    • 0027943151 scopus 로고
    • Synthesis of phospholipids by human peritoneal mesothelial cells
    • Beavis J, Harwood J, Coles G, Williams J: Synthesis of phospholipids by human peritoneal mesothelial cells. Perit Dial Int 1994, 14:348-355
    • (1994) Perit Dial Int , vol.14 , pp. 348-355
    • Beavis, J.1    Harwood, J.2    Coles, G.3    Williams, J.4
  • 7
    • 0027978894 scopus 로고
    • The source and possible significance of hyaluronan in the peritoneal cavity
    • Yung S, Coles GA, Williams JD, Davies M: The source and possible significance of hyaluronan in the peritoneal cavity. Kidney Int 1994, 46:527-533
    • (1994) Kidney Int , vol.46 , pp. 527-533
    • Yung, S.1    Coles, G.A.2    Williams, J.D.3    Davies, M.4
  • 8
    • 0028878579 scopus 로고
    • The source of peritoneal proteoglycans: Human peritoneal mesothelial cells synthesize and secrete mainly small dermatan sulfate proteoglycans
    • Yung S, Thomas GJ, Stylianou E, Coles GA, Williams JD, Davies M: The source of peritoneal proteoglycans: human peritoneal mesothelial cells synthesize and secrete mainly small dermatan sulfate proteoglycans. Am J Pathol 1995, 146:520-529
    • (1995) Am J Pathol , vol.146 , pp. 520-529
    • Yung, S.1    Thomas, G.J.2    Stylianou, E.3    Coles, G.A.4    Williams, J.D.5    Davies, M.6
  • 9
    • 0024402592 scopus 로고
    • Proteoglycans in cell regulation
    • Ruoslahti E: Proteoglycans in cell regulation. J Biol Chem 1989, 264:13369-13372
    • (1989) J Biol Chem , vol.264 , pp. 13369-13372
    • Ruoslahti, E.1
  • 10
    • 0030010512 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo RV, Murdoch AD: Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB 1996, 10:598-614
    • (1996) FASEB , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 11
    • 0027509462 scopus 로고
    • Glycosaminoglycans and the regulation of blood coagulation
    • Bourin M-C, Lindahl U: Glycosaminoglycans and the regulation of blood coagulation. Biochem J 1993, 289:313-330
    • (1993) Biochem J , vol.289 , pp. 313-330
    • Bourin, M.-C.1    Lindahl, U.2
  • 12
    • 0027992766 scopus 로고
    • Regulation of proteolytic activity in tissues
    • Twining SS: Regulation of proteolytic activity in tissues. Crit Rev Biochem Mol Biol 1994, 29:315-383
    • (1994) Crit Rev Biochem Mol Biol , vol.29 , pp. 315-383
    • Twining, S.S.1
  • 13
    • 0028143769 scopus 로고
    • Heparin and its derivatives modulate serine proteinases (SERPS) serine proteinase inhibitors (SERPINS) balance: Physiopathological relevance
    • Hornebeck W, Lafuma C, Robert L, Moczar M, Moczar E: Heparin and its derivatives modulate serine proteinases (SERPS) serine proteinase inhibitors (SERPINS) balance: physiopathological relevance. Pathol Res Pract 1994, 190:895-902
    • (1994) Pathol Res Pract , vol.190 , pp. 895-902
    • Hornebeck, W.1    Lafuma, C.2    Robert, L.3    Moczar, M.4    Moczar, E.5
  • 14
    • 0032521592 scopus 로고    scopus 로고
    • Inter-α-trypsin inhibitor proteoglycan family: A group of proteins binding and stabilizing the extracellular matrix
    • Bost F, Diarra-Mehrpour M, Martin J-P: Inter-α-trypsin inhibitor proteoglycan family: a group of proteins binding and stabilizing the extracellular matrix. Eur J Biochem 1998, 252:339-346
    • (1998) Eur J Biochem , vol.252 , pp. 339-346
    • Bost, F.1    Diarra-Mehrpour, M.2    Martin, J.-P.3
  • 15
    • 0032496145 scopus 로고    scopus 로고
    • Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids
    • Kainulainen V, Wang H, Schick C, Bernfield M: Syndecans, heparan sulfate proteoglycans, maintain the proteolytic balance of acute wound fluids. J Biol Chem 1998, 273:11563-11569
    • (1998) J Biol Chem , vol.273 , pp. 11563-11569
    • Kainulainen, V.1    Wang, H.2    Schick, C.3    Bernfield, M.4
  • 17
    • 0021192172 scopus 로고
    • Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissue
    • Couchman JR, Caterson B, Christner JE, Baker JR: Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissue. Nature 1984, 307:650-652
    • (1984) Nature , vol.307 , pp. 650-652
    • Couchman, J.R.1    Caterson, B.2    Christner, J.E.3    Baker, J.R.4
  • 19
    • 0027322558 scopus 로고
    • Anomalous structure of urinary chondroitin sulfate from cancer patients
    • Dietrich CP, Martins JRM, Sampaio LO, Nader HB: Anomalous structure of urinary chondroitin sulfate from cancer patients. Lab Invest 1993, 68:439-445
    • (1993) Lab Invest , vol.68 , pp. 439-445
    • Dietrich, C.P.1    Martins, J.R.M.2    Sampaio, L.O.3    Nader, H.B.4
  • 20
    • 0025315939 scopus 로고
    • Isolation, culture, and characterization of human peritoneal mesothelial cells
    • Stylianou E, Jenner LA, Davies M, Coles GA, Williams JD: Isolation, culture, and characterization of human peritoneal mesothelial cells. Kidney Int 1990, 37:1563-1570
    • (1990) Kidney Int , vol.37 , pp. 1563-1570
    • Stylianou, E.1    Jenner, L.A.2    Davies, M.3    Coles, G.A.4    Williams, J.D.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0023574521 scopus 로고
    • An improved method of sequential Alcian blue and ammonical silver staining of chondroitin sulfate proteoglycans in polyacrylamide gels
    • Kruger RC, Schwartz NB: An improved method of sequential Alcian blue and ammonical silver staining of chondroitin sulfate proteoglycans in polyacrylamide gels. Anal Biochem 1987, 167:295-300
    • (1987) Anal Biochem , vol.167 , pp. 295-300
    • Kruger, R.C.1    Schwartz, N.B.2
  • 23
    • 0024459170 scopus 로고
    • Analysis of inter-α-trypsin inhibitor and a novel trypsin inhibitor, pre-α-trypsin inhibitor, from human plasma
    • Enghild JJ, Thorgersen IB, Pizzo SV, Salvesen G: Analysis of inter-α-trypsin inhibitor and a novel trypsin inhibitor, pre-α-trypsin inhibitor, from human plasma. J Biol Chem 1989, 264:15975-15981
    • (1989) J Biol Chem , vol.264 , pp. 15975-15981
    • Enghild, J.J.1    Thorgersen, I.B.2    Pizzo, S.V.3    Salvesen, G.4
  • 24
    • 0019914963 scopus 로고
    • A direct spectrophotometric microassay for sulphated glycosaminoglycans in cartilage cultures
    • Farndale RW, Sayers CA, Barrett AJ: A direct spectrophotometric microassay for sulphated glycosaminoglycans in cartilage cultures. Connect Tissue Res 1982, 9:247-248
    • (1982) Connect Tissue Res , vol.9 , pp. 247-248
    • Farndale, R.W.1    Sayers, C.A.2    Barrett, A.J.3
  • 26
    • 0025784914 scopus 로고
    • The separation of chondroitin sulphate disaccharides and hyaluronan oligosaccharides by capillary zone electrophoresis
    • Carney SL, Osborne DJ: The separation of chondroitin sulphate disaccharides and hyaluronan oligosaccharides by capillary zone electrophoresis. Anal Biochem 1991, 195:132-140
    • (1991) Anal Biochem , vol.195 , pp. 132-140
    • Carney, S.L.1    Osborne, D.J.2
  • 27
  • 28
    • 0029741024 scopus 로고    scopus 로고
    • Covalent linkage between proteins of the inter-α-inhibitor family and hyaluronic acid is mediated by a factor produced by granulosa cells
    • Chen L, Zhang H, Powers RW, Russell PT, Larsen WJ: 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 1996, 271:19409-19414
    • (1996) J Biol Chem , vol.271 , pp. 19409-19414
    • Chen, L.1    Zhang, H.2    Powers, R.W.3    Russell, P.T.4    Larsen, W.J.5
  • 29
    • 0029669926 scopus 로고    scopus 로고
    • The inter-α-inhibitor family: From structure to regulation
    • Salier J-P, Rouet P, Raguenez G, Daveau M: The inter-α-inhibitor family: from structure to regulation. Biochem J 1996, 315:1-9
    • (1996) Biochem J , vol.315 , pp. 1-9
    • Salier, J.-P.1    Rouet, P.2    Raguenez, G.3    Daveau, M.4
  • 31
    • 0029120359 scopus 로고
    • Biosynthesis of bikunin proteins in the human carcinoma cell line HepG2 and in primary human hepatocytes: Polypeptide assembly by glycosaminoglycans
    • Thorgersen IB, Enghild JJ: Biosynthesis of bikunin proteins in the human carcinoma cell line HepG2 and in primary human hepatocytes: polypeptide assembly by glycosaminoglycans. J Biol Chem 1995, 270:18700-18709
    • (1995) J Biol Chem , vol.270 , pp. 18700-18709
    • Thorgersen, I.B.1    Enghild, J.J.2
  • 32
    • 0027520198 scopus 로고
    • A serum derived hyaluronan associated protein (SHAP) is the heavy chain of the inter-α-trypsin inhibitor
    • Huang L, Yoneda M, Kimata K: A serum derived hyaluronan associated protein (SHAP) is the heavy chain of the inter-α-trypsin inhibitor. J Biol Chem 1993, 268:26723-26730
    • (1993) J Biol Chem , vol.268 , pp. 26723-26730
    • Huang, L.1    Yoneda, M.2    Kimata, K.3
  • 33
    • 0025126313 scopus 로고
    • Inter-α-trypsin inhibitor: A plasma proteinase inhibitor with a unique chemical structure
    • Odum L: Inter-α-trypsin inhibitor: a plasma proteinase inhibitor with a unique chemical structure. Int J Biochem 1990, 22:925-930
    • (1990) Int J Biochem , vol.22 , pp. 925-930
    • Odum, L.1
  • 34
    • 0026939015 scopus 로고
    • Electrophoretic pattern of the inter-α-inhibitor family of proteins in human serum, characterized by chain specific antibodies
    • Rouet P, Daveau M, Salier JP: Electrophoretic pattern of the inter-α-inhibitor family of proteins in human serum, characterized by chain specific antibodies. Biol Chem Hoppe-Seyler 1992, 373:1019-1024
    • (1992) Biol Chem Hoppe-Seyler , vol.373 , pp. 1019-1024
    • Rouet, P.1    Daveau, M.2    Salier, J.P.3
  • 35
    • 0027468918 scopus 로고
    • Subunit structure of bovine ESF (extra-cellular-matrix stabilizing factor(s)): A chondroitin sulfate proteoglycan with homology to human α-1 trypsin inhibitors
    • Castillo GM, Templeton DM: Subunit structure of bovine ESF (extra-cellular-matrix stabilizing factor(s)): a chondroitin sulfate proteoglycan with homology to human α-1 trypsin inhibitors. FEBS Lett 1993, 318:292-296
    • (1993) FEBS Lett , vol.318 , pp. 292-296
    • Castillo, G.M.1    Templeton, D.M.2
  • 36
    • 0027208218 scopus 로고
    • Human inter-α-inhibitor family in inflammation: Simultaneous synthesis of positive and negative acute-phase proteins
    • Daveau M, Rouet P, Scotte M, Faye L, Hiron M, Lebreton J-P, Salier J-P: Human inter-α-inhibitor family in inflammation: simultaneous synthesis of positive and negative acute-phase proteins. Biochem J 1993, 292:485-492
    • (1993) Biochem J , vol.292 , pp. 485-492
    • Daveau, M.1    Rouet, P.2    Scotte, M.3    Faye, L.4    Hiron, M.5    Lebreton, J.-P.6    Salier, J.-P.7
  • 37
    • 0030671446 scopus 로고    scopus 로고
    • Intracellular coupling of bikunin and the heavy chain of rat pre-α inhibitor in cos-1 cells
    • Blom A, Thuveson M, Fries E: Intracellular coupling of bikunin and the heavy chain of rat pre-α inhibitor in cos-1 cells. Biochem J 1997, 328:185-189
    • (1997) Biochem J , vol.328 , pp. 185-189
    • Blom, A.1    Thuveson, M.2    Fries, E.3
  • 38
    • 0024320839 scopus 로고
    • Clearance and distribution of acid-stable trypsin inhibitor (ASTI)
    • Sugiki H, Sumi H, Maruyama M, Yosihda E, Mihara H: Clearance and distribution of acid-stable trypsin inhibitor (ASTI). Enzyme 1989, 42: 31-38
    • (1989) Enzyme , vol.42 , pp. 31-38
    • Sugiki, H.1    Sumi, H.2    Maruyama, M.3    Yosihda, E.4    Mihara, H.5
  • 40
    • 0030984283 scopus 로고    scopus 로고
    • High glomerular permeability of bikunin despite similarity in charge to albumin and hydrodynamic size to serum albumin
    • Lindstrom KE, Blom A, Johnsson E, Haraldsson B, Fries E: High glomerular permeability of bikunin despite similarity in charge to albumin and hydrodynamic size to serum albumin. Kidney Int 1997, 51:1053-1058
    • (1997) Kidney Int , vol.51 , pp. 1053-1058
    • Lindstrom, K.E.1    Blom, A.2    Johnsson, E.3    Haraldsson, B.4    Fries, E.5
  • 41
    • 0002770758 scopus 로고
    • Inter-α-trypsin inhibitor, and its close relatives
    • Edited by AJ Barrett, G Salvesen. Amsterdam, Elsevier
    • Gebhard W, Hochstrasser K: Inter-α-trypsin inhibitor, and its close relatives. Proteinase Inhibitors. Edited by AJ Barrett, G Salvesen. Amsterdam, Elsevier, 1986, pp 375-388
    • (1986) Proteinase Inhibitors , pp. 375-388
    • Gebhard, W.1    Hochstrasser, K.2
  • 42
    • 0018512380 scopus 로고
    • Kunitz type proteinase inhibitors derived from limited proteolysis of the a trypsin inhibitor. II. Characterization of a second inhibitory inactive domain by amino acid sequence determination
    • Wachter E, Hochstrasser K, Bretzel G, Heindl S: Kunitz type proteinase inhibitors derived from limited proteolysis of the a trypsin inhibitor. II. Characterization of a second inhibitory inactive domain by amino acid sequence determination. Biol Chem Hoppe-Seyler 1979, 360:1297-1303
    • (1979) Biol Chem Hoppe-Seyler , vol.360 , pp. 1297-1303
    • Wachter, E.1    Hochstrasser, K.2    Bretzel, G.3    Heindl, S.4
  • 44
    • 0025255603 scopus 로고
    • Hyaluronic acid associated with the surfaces of cultured fibroblasts is linked to a serum-derived 85-kd protein
    • Yoneda M, Susuki S, Kimata K: Hyaluronic acid associated with the surfaces of cultured fibroblasts is linked to a serum-derived 85-kd protein. J Biol Chem 1990, 265:5247-5257
    • (1990) J Biol Chem , vol.265 , pp. 5247-5257
    • Yoneda, M.1    Susuki, S.2    Kimata, K.3
  • 45
    • 0028815634 scopus 로고
    • Evidence for the covalent binding of SHAP, heavy chains of inter-α-trypsin inhibitor, to hyaluronan
    • Zhao M, Yoneda M, Ohashi Y, Curono 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 1995, 270:26657-26663
    • (1995) J Biol Chem , vol.270 , pp. 26657-26663
    • Zhao, M.1    Yoneda, M.2    Ohashi, Y.3    Curono, S.4    Iwata, H.5    Ohnuki, Y.6    Kimata, K.7
  • 46
    • 0028485259 scopus 로고
    • In vivo binding of human inter a trypsin inhibitor free heavy chains to hyaluronic acid
    • Jessen TE, Odum L, Johnson AH: In vivo binding of human inter a trypsin inhibitor free heavy chains to hyaluronic acid. Biol Chem Hoppe-Seyler 1994, 375:521-526
    • (1994) Biol Chem Hoppe-Seyler , vol.375 , pp. 521-526
    • Jessen, T.E.1    Odum, L.2    Johnson, A.H.3
  • 47
    • 0026637956 scopus 로고
    • Identification of a factor in fetal bovine serum that stabilizes the cumulus extracellular matrix
    • Chen L, Moa JT, Larsen WJ: Identification of a factor in fetal bovine serum that stabilizes the cumulus extracellular matrix. J Biol Chem 1992, 267:12380-12386
    • (1992) J Biol Chem , vol.267 , pp. 12380-12386
    • Chen, L.1    Moa, J.T.2    Larsen, W.J.3
  • 48
    • 0021985069 scopus 로고
    • α-1 anti-trypsin, and the serpins: Variations and counter variations
    • Carrell R, Travis J: α-1 anti-trypsin, and the serpins: variations and counter variations. Trends Biochem Sci 1985, 10:20-24
    • (1985) Trends Biochem Sci , vol.10 , pp. 20-24
    • Carrell, R.1    Travis, J.2
  • 49
    • 0028206262 scopus 로고
    • The serpin superfamily of proteinase inhibitors: Structure, function, and regulation
    • Potempa J, Korzus E, Travis J: The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J Biol Chem 1994, 269:15957-15960
    • (1994) J Biol Chem , vol.269 , pp. 15957-15960
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 50
    • 0024428832 scopus 로고
    • Inter-α-trypsin inhibitor: Inhibition spectrum of native and derived forms
    • Potempa J, Kwon K, Chawla R, Travis J: Inter-α-trypsin inhibitor: inhibition spectrum of native and derived forms. J Biol Chem 1989, 264:15109-15114
    • (1989) J Biol Chem , vol.264 , pp. 15109-15114
    • Potempa, J.1    Kwon, K.2    Chawla, R.3    Travis, J.4
  • 51
    • 0027494155 scopus 로고
    • Synthesis and assembly of the hyaluronan-coats around normal human mesothelial cells
    • Heldin P, Pertoft H: Synthesis and assembly of the hyaluronan-coats around normal human mesothelial cells. Exp Cell Res 1993, 208:422-429
    • (1993) Exp Cell Res , vol.208 , pp. 422-429
    • Heldin, P.1    Pertoft, H.2
  • 52
    • 0028986781 scopus 로고
    • Inter-α-inhibitor is required for the formation of the hyaluronan-containing coat on fibroblasts, and mesothelial cells
    • 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 1995, 270:9698-9701
    • (1995) J Biol Chem , vol.270 , pp. 9698-9701
    • Blom, A.1    Pertoft, H.2    Fries, E.3
  • 53
    • 0028171422 scopus 로고
    • Proteins of the inter-α-trypsin inhibitor family stabilize the cumulus extracellular matrix through their direct binding with hyaluronic acid
    • Chen L, Moa SJT, McLean LR, Powers RW, Larsen WJ: Proteins of the inter-α-trypsin inhibitor family stabilize the cumulus extracellular matrix through their direct binding with hyaluronic acid. J Biol Chem 1994, 269:28282-28287
    • (1994) J Biol Chem , vol.269 , pp. 28282-28287
    • Chen, L.1    Moa, S.J.T.2    McLean, L.R.3    Powers, R.W.4    Larsen, W.J.5
  • 54
    • 0027165825 scopus 로고
    • Effects of exogenous hyaluronic acid and serum on matrix organization and stability in the mouse cumulus cell-oocyte complex
    • Camaioni A, Hascall VC, Yanagishita M, Salustri A: Effects of exogenous hyaluronic acid and serum on matrix organization and stability in the mouse cumulus cell-oocyte complex. J Biol Chem 1993, 268: 20473-20481
    • (1993) J Biol Chem , vol.268 , pp. 20473-20481
    • Camaioni, A.1    Hascall, V.C.2    Yanagishita, M.3    Salustri, A.4
  • 56
    • 0031885413 scopus 로고    scopus 로고
    • Hyaluronan prevents the decreased net ultrafiltration caused by increased peritoneal dialysate fill volume
    • Wang T, Cheng H-H, Heimburger O, Waniewski J, Bergstrom J, Lindholm B: Hyaluronan prevents the decreased net ultrafiltration caused by increased peritoneal dialysate fill volume. Kidney Int 1998, 53:496-502
    • (1998) Kidney Int , vol.53 , pp. 496-502
    • Wang, T.1    Cheng, H.-H.2    Heimburger, O.3    Waniewski, J.4    Bergstrom, J.5    Lindholm, B.6
  • 57
    • 0023056270 scopus 로고
    • The messenger RNA for a proteinase inhibitor related to the HI-30 domain of inter-α-trypsin inhibitor also encodes α-1-microglobulin
    • Kaumeyer JF, Polazzi JO, Kotick MP: The messenger RNA for a proteinase inhibitor related to the HI-30 domain of inter-α-trypsin inhibitor also encodes α-1-microglobulin. Nucleic Acids Res 1986, 14:7839-7850
    • (1986) Nucleic Acids Res , vol.14 , pp. 7839-7850
    • Kaumeyer, J.F.1    Polazzi, J.O.2    Kotick, M.P.3


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