Inter-alpha-inhibitor, hyaluronan and inflammation

• Autorzy: Fries E. , Kaczmarczyk A.
• Języki publikacji: EN

Abstrakty

EN

Inter-a-inhibitor is an abundant plasma protein whose physiological function is only now beginning to be revealed. It consists of three polypeptides: two heavy chains and one light chain called bikunin. Bikunin, which has antiproteolytic activity, carries a chondroitin sulphate chain to which the heavy chains are covalently linked. The heavy chains can be transferred from inter-a-inhibitor to hyaluronan molecules and become covalently linked. This reaction seems to be mediated by TSG-6, a protein secreted by various cells upon stimulation by inflammatory cytokines. Inter-a-inhibitor has been shown to be required for the stabilization of the cumulus cell-oocyte complex during the expansion that occurs prior to ovulation. Hyaluronan-linked heavy chains in the extracellular matrix of this cellular complex have recently been shown to be tightly bound to TSG-6. Since TSG-6 binds to hyaluronan, its complex with heavy chains could stabilize the extracellular matrix by cross-linking hyaluronan molecules. Heavy chains linked to hyaluronan molecules have also been found in inflamed tissues. The physiological role of these complexes is not known but there are indications that they might protect hyaluronan against fragmentation by reactive oxygen species. TSG-6 also binds to bikunin thereby enhancing its antiplasmin activity. Taken together, these results suggest that inter-a-inhibitor is an anti-inflammatory agent which is acti­vated by TSG-6.

Słowa kluczowe

EN

hyaluronan; heavy chain; inter-alpha-inhibitor; inflammation; plasma protein; antiinflammatory agent; light chain; polypeptide

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 3
• Opis fizyczny: p.735-742,fig.

Twórcy

autor

Fries E.

• Uppsala University, Box 582, SE-751 23 Uppsala, Sweden

autor

Kaczmarczyk A.

Bibliografia

• Blom A, Pertoft H, Fries E. (1995) Inter-alpha-inhibitor is required for the formation of the hyaluronan-containing coat on fibroblasts and mesothelial cells. J Biol Chem.; 270: 9698-701.
• Blom AM, Thuveson M, Fries E. (1997) Intracellular coupling of bikunin and the heavy chain of rat pre-alpha-inhibitor in COS-1 cells. Biochem J.; 328: 185-91.
• Bork P, Rohde K. (1991) More von Willebrand factor type A domains? Sequence similarities with malaria thrombospondin-related anonymous protein, dihydropyridine-sensitive calcium channel and inter-alpha-trypsin inhibitor. Biochem J. ; 279: 908-10.
• Bratt T, Olsson H, Sjoberg EM, Jergil B, Akerstrom B. (1993) Cleavage of the alpha1-microglobulin-bikunin precursor is localized to the Golgi apparatus of rat liver cells. Biochim Biophys Acta.; 1157: 147-54.
• Camenisch TD, Spicer AP, Brehm-Gibson T, Biesterfeldt J, Augustine ML, Calabro A Jr, Kubalak S, Klewer SE, McDonald JA. (2000) Disruption of hyaluronan synthase-2 abrogates normal cardiac morphogenesis and hyaluronan- mediated transformation of epithelium to mesenchyme. J Clin Invest.; 106: 349-60.
• Chen L, Wert SE, Hendrix EM, Russell PT, Cannon M, Larsen WJ. (1990) Hyaluronic acid synthesis and gap junction endocytosis are necessary for normal expansion of the cumulus mass. Mol ReprodDev.; 26: 236-47.
• Chen L, Mao SJ, Larsen WJ. (1992) Identification of a factor in fetal bovine serum that stabilizes the cumulus extracellular matrix. A role for a member of the inter-alpha-trypsin inhibitor family. J Biol Chem.; 267: 12380-6.
• Chen L, Russell PT, Larsen WJ. (1993) Functional significance of cumulus expansion in the mouse: roles for the preovulatory synthesis of hyaluronic acid within the cumulus mass. Mol Reprod Dev.; 34: 87-93.
• Chen L, Mao JT, McLean LR, Powers RW, Larsen WJ. (1994) Proteins of the inter-alpha-trypsin inhibitor family stabilize the cumulus extracellular matrix through their direct binding with hyaluronic acid. J Biol Chem.; 269: 28282-7.
• Clarris BJ, Fraser JRE. (1968) On the pericellular zone of some mammalian cells in vitro. Exp Cell Res.; 49: 181-93.
• Enghild JJ, Salvesen G, Hefta SA, Thogersen IB, Rutherfurd S, Pizzo SV. (1991) Chondroitin 4-sulfate covalently cross­links the chains of the human blood protein pre-alpha-inhibitor. J Biol Chem.; 266: 747-51.
• Eppig JJ. (1980) Role of serum in FSH stimulated cumulus expansion by mouse oocyte-cumulus cell complexes in vitro. Biol Reprod. ; 22: 629-33.
• Espey LL. (1994) Current status of the hypothesis that mammalian ovulation is comparable to an inflammatory reaction. Biol Reprod.; 50: 233-8.
• Fries E, Blom AM. (2000) Bikunin — not just a plasma proteinase inhibitor. Int J Biochem Cell Biol.; 32: 125-37.
• Getting SJ, Mahoney DJ, Cao T, Rugg MS, Fries E, Milner CM, Perretti M, Day AJ. (2002) The link module from human TSG-6 inhibits neutrophil migration in a hyaluronan- and inter-alpha-inhibitor-independent manner. J Biol Chem.; 277: 51068-76.
• Heide K, Heimburger N, Haupt H. (1965) An inter-alpha-trypsin inhibitor of human serum. Clin Chim Acta.; II: 82-5.
• Hutadilok N, Ghosh P, Brooks PM. (1988) Binding of haptoglobin, inter-alpha-trypsin inhibitor and alpha^proteinase inhibitor to synovial fluid hyaluronate and the influence of these proteins on its degradation by oxygen derived free radicals. Ann Rheum Dis.; 47: 377-85.
• Iyer VR, Eisen MB, Ross DT, Schuler G, Moore T, Lee JC, Trent JM, Staudt LM, Hudson JJr, Boguski MS, Lashkari D, Shalon D, Botstein D, Brown PO. (1999) The transcriptional program in the response of human fibroblasts to serum. Science.; 283: 83-7.
• Jessen TE, Odum L. (2003) Role of tumour necrosis factor stimulated gene 6 (TSG-6) in the coupling of inter-alpha- trypsin inhibitor to hyaluronan in human follicular fluid. Reproduction.; 125: 27-31.
• Kaczmarczyk A, Thuveson M, Fries E. (2002) Intracellular coupling of the heavy chain of pre-alpha-inhibitor to chondroitin sulfate. J Biol Chem.; 277: 13578-82.
• Lee TH, Wisniewski HG, Vilcek J. (1992) 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: 545-57.
• Morelle W, Capon C, Balduyck M, Sautiere P, Kouach M, Michalski C, Fournet B, Mizon J. (1994) Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-alpha-trypsin inhibitor. Eur JBiochem.; 221: 881-8.
• 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. (1994) Novel factor Xa and plasma kallikrein inhibitory activities of the second Kunitz-type inhibitory domain of urinary trypsin inhibitor. Thromb Res.; 73: 193-204.
• Mukhopadhyay D, Hascall VC, Day AJ, Salustri A, Fulop C. (2001) Two distinct populations of tumor necrosis factor- stimulated gene-6 protein in the extracellular matrix of expanded mouse cumulus cell-oocyte complexes. Arch Biochem Biophys.; 394: 173-81.
• Potempa J, Kwon K, Chawla R, Travis J. (1989) Inter-alpha-trypsin inhibitor. Inhibition spectrum of native and derived forms. J Biol Chem.; 264: 15109-14.
• Powers RW, Chen L, Russell PT, Larsen WJ. (1995) Gonadotropin-stimulated regulation of blood-follicle barrier is mediated by nitric oxide. Am J Physiol. ; 269: E290-8.
• Salier J-P, Rouet P, Raguenez G, Daveau M. (1996) The inter-alpha-inhibitor family: from structure to regulation. Biochem J. ; 315: 1-9.
• Sjoberg EM, Fries E. (1992) Biosynthesis of bikunin (urinary trypsin inhibitor) in rat hepatocytes. Arch Biochem Biophys.; 295: 217-22.
• Steinbuch M, Loeb J. (1961) Isolation of an alpha2-globulin from human plasma. Nature.; 192: 1196.
• Thogersen IB, Enghild JJ. (1995) Biosynthesis of bikunin proteins in the human carcinoma cell line HepG2 and in primary human hepatocytes. J Biol Chem.; 270: 18700-9.
• Thuveson M, Fries E. (1999) Intracellular proteolytic processing of the heavy chain of rat pre-alpha-inhibitor. The COOH- terminal propeptide is required for coupling to bikunin. J Biol Chem.; 274: 6741-6.
• Wächter E, Hochstrasser K. (1981) Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha- trypsin inhibitor, IV: the amino acid sequence of the human urinary trypsin inhibitor isolated by affinity chromatography. Hoppe-Seyler's Z Physiol Chem.; 362: 1351-5.
• Wisniewski HG, Vilcek J. (1997) TSG-6: an IL-1/TNF-inducible protein with anti-inflammatory activity. Cytokine Growth Factor Rev.; 8: 143-56.
• Wisniewski HG, Burgess WH, Oppenheim JD, Vilcek J. (1994) TSG-6, an arthritis-associated hyaluronan binding protein, forms a stable complex with the serum protein inter-alpha-inhibitor. Biochemistry.; 33: 7423-9.
• Wisniewski HG, Hua J-C, Poppers DM, Naime D, Vilcek J, Cronstein BN. (1996) TNF/IL-1-inducible protein TSG-6 potentiates plasmin inhibition by inter-alpha-inhibitor and exerts a strong anti-inflammatory effect in vivo. J Immunol. ; 156: 1609-15.
• Xu Y, Carr PD, Guss JM , Ollis DL. (1998) The crystal structure of bikunin from the inter-alpha-inhibitor complex: a serine proteinase inhibitor with two Kunitz domains. J Mol Biol.; 276: 955-66.
• Zhao M, Yoneda M, Okashi Y, Kurono S, Iwata H, Ohnuki Y, Kimata K. (1995) Evidence for the covalent binding of SHAP, heavy chains of inter-alpha-trypsin inhibitor, to hyaluronan. J Biol Chem.; 270: 26657-63.
• Zhuo L, Yoneda M, Zhao M, Yingsung W, Yoshida N, Kitagawa Y, Kawamura K, Suzuki T, Kimata K. (2001) Defect in SHAP-hyaluronan complex causes severe female infertility. J Biol Chem.; 276: 7693-6.