Inter-alpha-trypsin inhibitor is concentrated in the pericellular environment of mouse granulosa cells through hyaluronan-binding

European Journal of Obstetrics and Gynecology and Reproductive Biology

Volumn 73, Issue 1, 1997, Pages 79-84

  Hirashima, Yasuyuki ^a   Kobayashi, Hiroshi ^a   Gotoh, Junko ^a   Terao, Toshihiko ^a  

^a HAMAMATSU UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

Cumulus oocyte complex; Heavy chains of ITI; Hyaluronan; Inter alpha trypsin inhibitor; Urinary trypsin inhibitor

Indexed keywords

HYALURONIC ACID; INTER ALPHA TRYPSIN INHIBITOR;

ANIMAL CELL; ARTICLE; CUMULUS OOPHORUS; FEMALE; FERTILIZATION IN VITRO; GRANULOSA CELL; MOUSE; NONHUMAN; OVARY FOLLICLE CELL; OVULATION; PRIORITY JOURNAL;

EID: 0030971716     PISSN: 03012115     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-2115(96)02689-9     Document Type: Article

References (20)

1. Moor RM, Smith WM, Dawson RMC. Measurement of intercellular coupling between oocytes and cumulus cells using intracellular marker. Exp Cell Res 1980; 126: 15-29.
2. Shioya Y, Kuwayama M, Fukushima M, Iwasaki S. In vitro fertilization and cleavage capability of bovine follicular oocytes classified by cumulus cells and matured in vitro. Theriogenology 1988; 30: 489-494.
3. Chen L, Mao SJ, Larsen WJ. Identification of a factor in fetal bovine serum that stabilizes the cumulus extracellular matrix. J Biol Chem 1992; 267: 12380-12386.
4. Huang L, Yoneda M, Kimata K. A serum-derived hyaluronan-associated protein (SHAP) is the heavy chain of the inter-alpha-trypsin inhibitor. J Biol Chem 1993; 268: 26725-26730.
5. Castillo GM, Templeton DM. Subunit structure of bovine ESF (extracellular-matrix stabilizing factor(s)): A chondroitin sulfate proteoglycan with homology to human Inter-alpha-inhibitor (interalpha-trypsin inhibitor). FEBS Lett 1993; 318: 292-296.
6. Jessen TE, Odum L, Johnsen AH. In vivo binding of human inter-alpha-trypsin inhibitor free heavy chains to hyaluronic acid. Biol Chem Hoppe-Seyler 1994; 375: 521-526.
7. Chen L, Mao SJT, McLean LR, Powers RW, Larsen WJ. Proteins of the Inter-alpha-trypsin inhibitor family stabilize the cumulus extracellular matrix through their direct binding with hyaluronic acid. J Biol Chem 1994; 269: 28282-28287.
8. Emghild JJ, Thogersen IB, Pizzo SV, Salvesen G. Analysis of inter-alpha-trypsin inhibitor and a novel trypsin inhibitor, pre-alpha-trypsin inhibitor, from human plasma. J Biol Chem 1989; 264: 15975-15981.
9. Gebhard W, Hochstrasser K, Fritz H, Enghild JJ, Pizzo SV, Salvesen G. Structure of inter-alpha-inhibitor (inter-alpha-trypsin inhibitor) and pre-alpha-inhibitor: current state and proposition of a new terminology. Biol Chem Hoppe-Seyler 1990; 371: Suppl 13-22.
10. Pratt CW, Roche PA, Pizzo SV. The role of inter-a-trypsin inhibitors and other proteinase inhibitors in the plasma clearance of neutrophil elastase and plasmin. Arch Biochem Biophys 1987; 258: 591-599.
11. Hardingham TE, Fosang AJ. Proteoglycans: many forms and many functions. FASEB J 1992; 6: 861-870.
12. Goetic PF, Stirpe NS, Tsonis PA, Carlone D. Tandemly repeat sequences of cartilage link protein contain the sites for interaction with HA. J Cell Biol 1987; 105: 2403-2408.
13. Bonnet F, Dunham DG, Hardingham TE. Structure and interactions of cartilage proteoglycan binding region and link protein. Biochem J 1985; 228: 77-85.
14. Salier JP. Inter-alpha-trypsin inhibitor: emergence of a family within the Kunitz-type protease inhibitor superfamily. TIBS 1990; 15: 435-439.
15. Wachter E, Hochstrasser K. Kunitz-type proteinase inhibitors derived by limited proteolysis of inter-alpha-trypsin inhibitor, IV. Hoppe-Seylers Z Physiol Chem 1981; 362: 1351-1355.
16. Tengblad A. Affinity chromatography on immobilized hyaluronate and its application to the isolation of hyaluronate binding proteins from cartilage. Biochem Biophys Acta 1979; 578: 281-289.
17. Bertheim U, Hellstrom S. The distribution of hyaluronan in human skin and mature, hypertrophic and keloid scars. Br J Plastic Surg 1994; 47: 483-489.
18. Aruffo A, Samenkovic I, Melnick M, Underhill CB, Seed B. CD44 is the principal cell surface receptor for hyaluronate. Cell 1990; 61: 1303-1313.
19. Kobayashi H, Gotoh J, Hirashima Y, Terao T. Inter-alpha-trypsin inhibitor bound to tumor cells is cleaved into the heavy chains and the light chain on the cell surface. J Biol Chem 1996; 271: 11362-11367.
20. Lin Y, Mahan K, Lathrop WF, Myles DG, Primakoff PA. Hyaluronidase activity of the sperm plasma membrane protein PH-20 enables sperm to penetrate the cumulus cell layer surrounding the egg. J Cell Biol 1994; 125: 1157-1163.