An Inhibitor of Cell Proliferation Associated with Adhesion Formation Is Suppressed by N,O-Carboxymethyl Chitosan

References

• Buckman R. F., Woods M., Sargent L., Gervin A. S. A unifying pathogenetic mechanism in the etiology of intraperitoneal adhesions. J Surg Res. 1976; 20: 1–5
   PubMed Web of Science ®Google Scholar
• Buckman RFJ, Buckman P. D., Hufnagel H. V., Gervin A. S. A physiologic basis for the adhesion-free healing of deperitonealized surfaces. J Surg Res. 1976; 21: 67–76
   PubMed Web of Science ®Google Scholar
• Raftery A. T. Regeneration of parietal and visceral peritoneum: An electron microscopical study. J Anat. 1973; 115: 1375–392
   Google Scholar
• Raftery A. T. An enzyme histochemical study of mesothelial cells in rodents. J Anat. 1973; 115: 365–373
   PubMed Web of Science ®Google Scholar
• Raftery A. T. Regeneration of peritoneum: A fibrinolytic. study. J Anat. 1979; 129: 659–664
   PubMed Web of Science ®Google Scholar
• Strange C., Tomlinson J. R., Wilson C., Harley R., Miller K. S., Sahn SA. The histology of experimental pleural injury with tetracycline, empyema, and carrageenan. Exp Mol Pathol. 1989; 51: 205–219
   PubMed Web of Science ®Google Scholar
• Leak L. V., Ferrans V. J., Cohen S. R., Eidbo E. E., Jones M. Animal model of acute pericarditis and its progression to pericardial fibrosis and adhesions: Ultrastructural studies. Am J Anat. 1987; 180: 1373–390
   Google Scholar
• Holmdahl L., Risberg B., Beck D. E., Burns J. W., Chegini N., diZerega G. S., Ellis H. Adhesions: Pathogenesis and prevention—Panel discussion and summary. Eur J Surg Suppl. 1997; 56–62
   PubMedGoogle Scholar
• Gabbay S., Guindy A. M., Andrews J. F., Amato J. J., Seaver P., Khan MY. New outlook on pericardial substitution after open heart operations. Ann Thorac Surg. 1989; 48: 803–812
   PubMed Web of Science ®Google Scholar
• Bunton R. W., Xabregas A. A., Miller AP. Pericardial closure after cardiac operations. An animal study to assess currently available materials with particular reference to their suitability for use after coronary artery bypass grafting. J Thorac Cardiovasc Surg. 1990; 100: 99–107
   PubMed Web of Science ®Google Scholar
• Eng J., Ravichandran P. S., Abbott C. R., Kay P. H., Murday A. J., Shreiti I. Reoperation after pericardial closure with bovine pericardium. Ann Thorac Surg. 1989; 48: 813–815
   PubMedGoogle Scholar
• Young R. L., Cota J., Zund G., Mason B. A., Wheeler JM. The use of an amniotic membrane graft to prevent postoperative adhesions. Fertil Steril. 1991; 55: 624–628
   PubMedGoogle Scholar
• Heydorn W. H., Daniel J. S., Wade CE. A new look at pericardial substitutes. J Thorac Cardiovasc Surg. 1987; 94: 291–296
   PubMedGoogle Scholar
• Vander TJ Salm, Okike O. N., Marsicano T. H., Compton C., Espinoza E. Prevention of postoperative pericardial adhesions. An animal study. Arch Surg. 1986; 121: 462–467
   PubMedGoogle Scholar
• Revuelta J. M., Garcia-Rinaldi R., Val F., Crego R., Duran CM. Expanded polytetrafluoroethylene surgical membrane for pericardial closure. An experimental study. J Thorac Cardiovasc Surg. 1985; 89: 451–455
   PubMed Web of Science ®Google Scholar
• Risberg B. Adhesions: Preventive strategies. fur J Surg Suppl. 1997; 32–39
   Google Scholar
• Pennisi E. Chitin craze. Science News. 1993; 144: 72–74
   Google Scholar
• Krause T. J., Zazanis G. A., McKinnon RD. Prevention of post-operative adhesions with the chitin derivative N,O-carboxymethyl chitosan. Wound Repair and Regeneration 1996; 4: 53–57
   PubMedGoogle Scholar
• Kennedy R., Costain D. J., McAlister V. C., Lee T. D. Prevention of experimental postoperative peritoneal adhesions by N,O-carboxymethyl chitosan. Surgery 1996; 120: 866–870
   PubMedGoogle Scholar
• Costain D. J., Kennedy R., Ciona C., McAlister V. C., Lee TD. Prevention of postsurgical adhesions with N,O-carboxymethyl chitosan: Examination of the most efficacious preparation and the effect of N,O-carboxymethyl chitosan on postsurgical healing. Surgery 1997; 121: 314–319
   PubMed Web of Science ®Google Scholar
• Docherty R., Forrester J. V., Lackie J. M., Gregory D. W. Glycosaminoglycans facilitate the movement of fibroblasts through three-dimensional collagen matrices. J Cell Sci. 1989; 92: 263–270
   PubMed Web of Science ®Google Scholar
• Gessin J. C., Brown L. J., Gordon J. S., Berg R. A. Regulation of collagen synthesis in human dermal fibroblasts in contracted collagen gels by ascorbic acid, growth factors, and inhibitors of lipid peroxidation. Exp Cell Res. 1993; 206: 283–290
   PubMedGoogle Scholar
• Klein N. J., Shennan G. I., Heyderman R. S., Levin M. Alteration in glycosaminoglycan metabolism and surface charge on human umbilical vein endothelial cells induced by cytokines, endotoxin and neutrophils. J Cell Sci. 1992; 102: 821–832
   PubMedGoogle Scholar
• Huang-Lee L. L., Nimni ME. Fibroblast contraction of collagen matrices with and without covalently bound hyaluronan. J Biomater Sci Polym Ed. 1993; 5: 99–109
   PubMed Web of Science ®Google Scholar
• Brecht M., Mayer U., Schlosser E., Prehm P. Increased hyaluronate synthesis is required for fibroblast detachment and mitosis. Biochem J. 1986; 239: 445–450
   PubMed Web of Science ®Google Scholar
• Heldin P., Laurent T. C., Heldin CH. Effect of growth factors on hyaluronan synthesis in cultured human fibroblasts. Biochem J. 1989; 258: 919–922
   PubMed Web of Science ®Google Scholar
• Miller D. A., Pelton R. W., Derynck R., Moses H. L. Transforming growth factor-β. A family of growth regulatory peptides. Ann NY Acad Sci. 1990; 593: 208–217
   PubMed Web of Science ®Google Scholar
• Border W. A., Noble NA. Transforming growth factor β in tissue fibrosis. N Engl J Med. 1994; 331: 1286–1292
   PubMed Web of Science ®Google Scholar
• Chegini N., Gold L. I., Williams R. S., Masterson B. J. Localization of transforming growth factor β isoforms TGF-β1, TGF-β2, and TGF-β3 in surgically induced pelvic adhesions in the rat. Obstet Gynecol. 1994; 83: 449–454
   PubMed Web of Science ®Google Scholar
• Chang J., Most D., Stelnicki E., Siebert J. W., Longaker M. T., Hui K., Lineaweaver WC. Gene expression of transforming growth factor β-1 in rabbit zone II flexor tendon wound healing: Evidence for dual mechanisms of repair. Plast Reconstr Surg. 1997; 100: 937–944
   PubMed Web of Science ®Google Scholar
• Danielpour D., Dart L. L., Flanders K. C., Roberts A. B., Sporn MB. Immunodetection and quantitation of the two forms of transforming growth factor-β(TGF-β1 and TGF-β2) secreted by cells in culture. J Cell Physiol. 1989; 138: 79–86
   PubMed Web of Science ®Google Scholar
• McKinnon R. D., Piras G., Ida JA, Jr, Dubois-Dalcq M. A role for TGF-p in oligodendrocyte differentiation. J Cell Biol. 1993; 121: 1397–1407
   PubMed Web of Science ®Google Scholar
• Laiho M., Weis M. B., Massague J. Concomitant loss of transforming growth factor(TGF)-β receptor types I and II in TGF-p-resistant cell mutants implicates both receptor types in signal transduction. J Biol Chem. 1990; 265: 18518–18524
   PubMed Web of Science ®Google Scholar
• Sporn M. B., Roberts A. B., Wakefield L. M., de Crombrugghe B. Some recent advances in the chemistry and biology of transforming growth factor-β. J Cell Biol. 1987; 105: 1039–1045
   PubMed Web of Science ®Google Scholar
• Roberts A. B., Heine U. I., Flanders K. C., Sporn M. B. Transforming growth factor-β. Major role in regulation of extracellular matrix. Ann N YA cad Sci. 1990; 580: 225–232
   PubMed Web of Science ®Google Scholar
• Chegini N., Simms J., Williams R. S., Masterson B. J. Identification of epidermal growth factor, transforming growth factor-α, and epidermal growth factor receptor in surgically induced pelvic adhesions in the rat and intraperitoneal adhesions in the human. Am J Obstet Gynecol. 1994; 171: 321–327
   PubMed Web of Science ®Google Scholar
• Chegini N. The role of growth factors in peritoneal healing: transforming growth factor β(TGF-beta). Eur J Surg Suppl. 1997; 17–23
   PubMedGoogle Scholar
• Dou Q., Williams R. S., Chegini N. Inhibition of transforming growth factor-β1 alters the growth, anchor-dependent cell aggregation and integrin mRNA expression in human promonocytes: Implications for endometriosis and peritoneal adhesion formation. Mol Hum Reprod. 1997; 3: 383–391
   PubMedGoogle Scholar
• Williams R. S., Rossi A. M., Chegini N., Schultz G. Effect of transforming growth factor β on postoperative adhesion formation and intact peritoneum. J Surg Res. 1992; 52: 65–70
   PubMed Web of Science ®Google Scholar
• Shull M. M., Ormsby I., Kier A. B., Pawlowski S., Diebold R. J., Yin M., Allen R., Sidman C., Proetzel G., Calvin D. Targeted disruption of the mouse transforming growth factor-β1 gene results in multifocal inflammatory disease. Nature 1992; 359: 693–699
   PubMed Web of Science ®Google Scholar
• Kulkarni A. B., Huh C. G., Becker D., Geiser A., Lyght M., Flanders K. C., Roberts A. B., Sporn M. B., Ward J. M., Karlsson S. Transforming growth factor β1 null mutation in mice causes excessive inflammatory response and early death. Proc Natl Acad Sci USA. 1993; 90: 770–774
   PubMed Web of Science ®Google Scholar
• Orita H., Fukasawa M., Girgis W., diZerega G. S. Inhibition of postsurgical adhesions in a standardized rabbit model: intraperitoneal treatment with tissue plasminogen activator. Int J Fertil. 1991; 36: 172–177
   PubMedGoogle Scholar
• Holmdahl L. E., Al-Jabreen M., Risberg B. Role offibrinoly-sis in the formation of postoperative adhesions. Wound Repair Regenerat. 1994; 2: 171–176
   PubMedGoogle Scholar
• Nkere U. U., Whawell S. A., Sarraf C. E., Schofield J. B., Thompson J. N., Taylor KM. Perioperative histologic and ultrastructural changes in the pericardium and adhesions. Ann Thorac Surg. 1994; 58: 437–444
   PubMedGoogle Scholar
• Wiseman D. M., Kamp L., Linsky C. B., Jochen R. F., Pang R. H., Scholz PM. Fibrinolytic drugs prevent pericardial adhesions in the rabbit. J Surg Res. 1992; 53: 362–368
   PubMedGoogle Scholar
• Holmdahl L. The role of fibrinolysis in adhesion formation. Eur J Surg Suppl. 1997; 24–31
   PubMedGoogle Scholar
• O'Reilly M. S., Holmgren L., Shing Y., Chen C., Rosenthal R. A., Moses M., Lane W. S., Cao Y., Sage E. H., Folkman J. Angiostatin: A novel angiogenesis inhibitor that mediates the suppression of metastases by a Lewis lung carcinoma. Cell 1994; 79: 315–328
   PubMed Web of Science ®Google Scholar