Skip to main content
Top
Published in: Pathology & Oncology Research 3/2014

01-07-2014 | Review

Gastrointestinal Mucositis: The Role of MMP-Tight Junction Interactions in Tissue Injury

Authors: Noor Al-Dasooqi, Hannah R. Wardill, Rachel J Gibson

Published in: Pathology & Oncology Research | Issue 3/2014

Login to get access

Abstract

Chemotherapy for cancer causes significant gut toxicity known as mucositis. The pathogenesis of mucositis is ill defined. Recent clinical research guidelines have highlighted epithelial junctional complexes as emerging targets within mucositis research. Given the robust biological evidence linking tight junctions and matrix metalloproteinases, key mediators of mucositis, tight junction proteins have received significant attention. Despite this, the link between tight junctions, matrix metalloproteinases and mucositis development is yet to be established. This critical review therefore aims to describe the role of matrix metalloproteinases in mucositis, and how matrix metalloproteinase-dependent tight junction disruption may contribute to the pathobiology of mucositis.
Literature
1.
go back to reference Keefe D, Schubert M et al (2007) Updated clinical practice guidelines for the prevention and treatment of mucositis. Cancer 109:820–831PubMedCrossRef Keefe D, Schubert M et al (2007) Updated clinical practice guidelines for the prevention and treatment of mucositis. Cancer 109:820–831PubMedCrossRef
3.
go back to reference Sonis S, Shklar T et al (1990) An animal model for mucositis induced by cancer chemotherapy. Oral Surg Oral Med Oral Pathol 69:437–443PubMedCrossRef Sonis S, Shklar T et al (1990) An animal model for mucositis induced by cancer chemotherapy. Oral Surg Oral Med Oral Pathol 69:437–443PubMedCrossRef
4.
go back to reference Paris F, Fuks Z et al (2001) Endothelial apoptosis as the primary lesion initiating intestinal radiation damage in mice. Science 293:293–297PubMedCrossRef Paris F, Fuks Z et al (2001) Endothelial apoptosis as the primary lesion initiating intestinal radiation damage in mice. Science 293:293–297PubMedCrossRef
5.
go back to reference Logan R, Stringer A et al (2009) Is the pathobiology of chemotherapy-induced alimentary tract mucositis influenced by the type of mucotoxic drug administered? Cancer Chemother Pharmacol 63:239–251PubMedCrossRef Logan R, Stringer A et al (2009) Is the pathobiology of chemotherapy-induced alimentary tract mucositis influenced by the type of mucotoxic drug administered? Cancer Chemother Pharmacol 63:239–251PubMedCrossRef
6.
go back to reference Stringer A, Gibson R et al (2009) Irinotecan-induced mucositis manifesting as diarrhoea corresponds with an amended intestinal flora and mucin profile. Int J Exp Pathol 90:489–499PubMedCentralPubMedCrossRef Stringer A, Gibson R et al (2009) Irinotecan-induced mucositis manifesting as diarrhoea corresponds with an amended intestinal flora and mucin profile. Int J Exp Pathol 90:489–499PubMedCentralPubMedCrossRef
7.
go back to reference Stringer A, Gibson R et al (2009) Chemotherapy-induced changes to microflora: evidence and implications of change. Curr Drug Metab 10:79–83PubMedCrossRef Stringer A, Gibson R et al (2009) Chemotherapy-induced changes to microflora: evidence and implications of change. Curr Drug Metab 10:79–83PubMedCrossRef
8.
go back to reference Al-Dasooqi N, Bowen J et al (2011) Irinotecan-induced alterations in intestinal cell kinetics and extracellular matrix component expression in the dark agouti rat. Int J Exp Pathol 92:357–365PubMedCentralPubMedCrossRef Al-Dasooqi N, Bowen J et al (2011) Irinotecan-induced alterations in intestinal cell kinetics and extracellular matrix component expression in the dark agouti rat. Int J Exp Pathol 92:357–365PubMedCentralPubMedCrossRef
9.
go back to reference Al-Dasooqi N, Gibson R et al (2010) Matrix metalloproteinases are possible mediators for the development of alimentary tract mucositis in the DA rat. Exp Biol Med 235:1244–1256CrossRef Al-Dasooqi N, Gibson R et al (2010) Matrix metalloproteinases are possible mediators for the development of alimentary tract mucositis in the DA rat. Exp Biol Med 235:1244–1256CrossRef
10.
go back to reference Ma T, Iwamoto G et al (2004) TNF-alpha-induced increase in intestinal epithelial tight junction permeability requires NF-kappa B activation. Am J Physiol Gastrointest Liver Physiol 286:G367–G376PubMedCrossRef Ma T, Iwamoto G et al (2004) TNF-alpha-induced increase in intestinal epithelial tight junction permeability requires NF-kappa B activation. Am J Physiol Gastrointest Liver Physiol 286:G367–G376PubMedCrossRef
11.
go back to reference Blijlevens NM, Donnelly JP, de Pauw BE (2005) Prospective evaluation of gut mucosal barrier injury following various myeloablative regimens for haematopoietic stem cell transplant. Bone Marrow Transplant 35(7):707–711PubMedCrossRef Blijlevens NM, Donnelly JP, de Pauw BE (2005) Prospective evaluation of gut mucosal barrier injury following various myeloablative regimens for haematopoietic stem cell transplant. Bone Marrow Transplant 35(7):707–711PubMedCrossRef
12.
go back to reference Walsh-Reitz M, Huang E et al (2005) AMP-18 protects barrier function of colonic epithelial cells: role of tight junction proteins. Am J Physiol Gastrointest Liver Physiol 289:G163–G171PubMedCentralPubMedCrossRef Walsh-Reitz M, Huang E et al (2005) AMP-18 protects barrier function of colonic epithelial cells: role of tight junction proteins. Am J Physiol Gastrointest Liver Physiol 289:G163–G171PubMedCentralPubMedCrossRef
13.
go back to reference Wardill H, Bowen J, Gibson R (2013) Chemotherapy-induced gut toxicity: are alterations to intestinal tight junctions pivotal? Cancer Chemother Pharmacol 70:627–635CrossRef Wardill H, Bowen J, Gibson R (2013) Chemotherapy-induced gut toxicity: are alterations to intestinal tight junctions pivotal? Cancer Chemother Pharmacol 70:627–635CrossRef
14.
go back to reference Hollander D (1999) Intestinal permeability, leaky gut, and intestinal disorders. Curr Gastroenterol Rep 1:410–416PubMedCrossRef Hollander D (1999) Intestinal permeability, leaky gut, and intestinal disorders. Curr Gastroenterol Rep 1:410–416PubMedCrossRef
15.
go back to reference Gonzalez-Mariscal L, Tapia R, Chamorro D (2008) Crosstalk of tight junction components with signaling pathways. Biochim Biophys Acta 1778(3):729–756PubMedCrossRef Gonzalez-Mariscal L, Tapia R, Chamorro D (2008) Crosstalk of tight junction components with signaling pathways. Biochim Biophys Acta 1778(3):729–756PubMedCrossRef
16.
go back to reference Keefe D, Cummins AG et al (1997) Effect of high-dose chemotherapy on intestinal permeability in humans. Clin Sci 92:385–389PubMed Keefe D, Cummins AG et al (1997) Effect of high-dose chemotherapy on intestinal permeability in humans. Clin Sci 92:385–389PubMed
17.
18.
go back to reference Hamada K, Shitara Y et al (2010) Zonula Occluden-1 alterations and enhances intestinal permeability in methotrexate-treated rats. Cancer Chemother Pharmacol 66:1031–1038PubMedCrossRef Hamada K, Shitara Y et al (2010) Zonula Occluden-1 alterations and enhances intestinal permeability in methotrexate-treated rats. Cancer Chemother Pharmacol 66:1031–1038PubMedCrossRef
19.
go back to reference Nakao T, Kurita N et al (2012) Irinotecan injures tight junction and causes bacterial translocation in rat. J Surg Res 173(2):341–347PubMedCrossRef Nakao T, Kurita N et al (2012) Irinotecan injures tight junction and causes bacterial translocation in rat. J Surg Res 173(2):341–347PubMedCrossRef
20.
go back to reference Youmba SB, Belmonte L et al (2011) Methotrexate Modulates Tight Junctions Through NF-kappaB, MEK and JNK Pathways. J Pediatr Gastroenterol Nutr Youmba SB, Belmonte L et al (2011) Methotrexate Modulates Tight Junctions Through NF-kappaB, MEK and JNK Pathways. J Pediatr Gastroenterol Nutr
21.
go back to reference Stringer A, Al-Dasooqi N et al (2013) Biomarkers of chemotherapy-induced diarrhoea: a clinical study of intestinal microbiome alterations, inflammation and circulating matrix metalloproteinases. Support Care Cancer. [Epub ahead of print] Stringer A, Al-Dasooqi N et al (2013) Biomarkers of chemotherapy-induced diarrhoea: a clinical study of intestinal microbiome alterations, inflammation and circulating matrix metalloproteinases. Support Care Cancer. [Epub ahead of print]
22.
go back to reference Sengupta N, MacDonald T (2007) The role of matrix metalloproteinases in stromal/epithelial interactions in the gut. Physiology 22:401–409PubMedCrossRef Sengupta N, MacDonald T (2007) The role of matrix metalloproteinases in stromal/epithelial interactions in the gut. Physiology 22:401–409PubMedCrossRef
23.
go back to reference Clark I, Swingler T et al (2008) The regulation of matrix metalloproteinases and their inhibitors. Int J Biochem Cell Biol 40:1362–1378PubMedCrossRef Clark I, Swingler T et al (2008) The regulation of matrix metalloproteinases and their inhibitors. Int J Biochem Cell Biol 40:1362–1378PubMedCrossRef
25.
go back to reference Wolf M, Albrecht S, Marki C (2008) Proteolytic processing of Chemokines: implications in physiological and pathological conditions. Int J Biochem Cell Biol 40:1185–1198PubMedCrossRef Wolf M, Albrecht S, Marki C (2008) Proteolytic processing of Chemokines: implications in physiological and pathological conditions. Int J Biochem Cell Biol 40:1185–1198PubMedCrossRef
27.
go back to reference Chakraborti S, Mandal M et al (2003) Regulation of matrix metalloproteinases: an overview. Mol Cell Biochem 253:269–285PubMedCrossRef Chakraborti S, Mandal M et al (2003) Regulation of matrix metalloproteinases: an overview. Mol Cell Biochem 253:269–285PubMedCrossRef
28.
go back to reference Pender S, MacDonald T (2004) Matrix metalloproteinases and the gut- new roles for old enzymes. Curr Opin Pharmacol 4:546–550PubMedCrossRef Pender S, MacDonald T (2004) Matrix metalloproteinases and the gut- new roles for old enzymes. Curr Opin Pharmacol 4:546–550PubMedCrossRef
29.
go back to reference Van Wart H, Birkedal-Hansen H (1990) The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci U S A 87:5578–5582PubMedCentralPubMedCrossRef Van Wart H, Birkedal-Hansen H (1990) The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci U S A 87:5578–5582PubMedCentralPubMedCrossRef
30.
go back to reference Dhaouadi T, Sfar I et al (2007) Role of immune system, apoptosis and angiogenesis in pathogenesis of rheumatoid arthritis and joint destruction, a systematic review. Tunis Med 85:991–998PubMed Dhaouadi T, Sfar I et al (2007) Role of immune system, apoptosis and angiogenesis in pathogenesis of rheumatoid arthritis and joint destruction, a systematic review. Tunis Med 85:991–998PubMed
31.
go back to reference Sorsa T, Tjaderhane L et al (2006) Matrix metalloproteinases: contribution to pathogenesis, diagnosis and treatment of periodontal inflammation. Ann Med 38:306–321PubMedCrossRef Sorsa T, Tjaderhane L et al (2006) Matrix metalloproteinases: contribution to pathogenesis, diagnosis and treatment of periodontal inflammation. Ann Med 38:306–321PubMedCrossRef
32.
go back to reference Vandenbroucke R, Dejonckheere E, and Libert C (2011) A therapeutic role for MMP inhibitors in lung diseases? Eur Respir J [Epub ahead of print] Vandenbroucke R, Dejonckheere E, and Libert C (2011) A therapeutic role for MMP inhibitors in lung diseases? Eur Respir J [Epub ahead of print]
33.
go back to reference Parks W, Wilson C, Lopez-Boado Y (2004) Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat Rev Immunol 4:617–629PubMedCrossRef Parks W, Wilson C, Lopez-Boado Y (2004) Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat Rev Immunol 4:617–629PubMedCrossRef
34.
go back to reference Shipley J, Wesselschmidt R et al (1996) Metalloelastase is required for macrophage-mediated proteolysis and matrix invasion in mice. Proc Natl Acad Sci 93:3942–3946PubMedCentralPubMedCrossRef Shipley J, Wesselschmidt R et al (1996) Metalloelastase is required for macrophage-mediated proteolysis and matrix invasion in mice. Proc Natl Acad Sci 93:3942–3946PubMedCentralPubMedCrossRef
36.
go back to reference Lanone S, Zheng T et al (2002) Overlapping and enzyme-specific contributions of matrix metalloproteinases-9 and -12 in IL-13-induced inflammation and remodeling. J Clin Invest 110:463–474PubMedCentralPubMedCrossRef Lanone S, Zheng T et al (2002) Overlapping and enzyme-specific contributions of matrix metalloproteinases-9 and -12 in IL-13-induced inflammation and remodeling. J Clin Invest 110:463–474PubMedCentralPubMedCrossRef
37.
go back to reference Itoh T, Matsuda H et al (2002) The role of matrix metalloproteinase-2 and matrix metalloproteinase-9 in antibody-induced arthritis. J Immunol 169:2643–2647PubMedCrossRef Itoh T, Matsuda H et al (2002) The role of matrix metalloproteinase-2 and matrix metalloproteinase-9 in antibody-induced arthritis. J Immunol 169:2643–2647PubMedCrossRef
38.
go back to reference Mudgett J, Hutchinson N et al (1998) Susceptability of stromelysin-1 deficient mice to collagen-induced arthritis and cartilage destruction. Arthritis Rheum 41:110–121PubMedCrossRef Mudgett J, Hutchinson N et al (1998) Susceptability of stromelysin-1 deficient mice to collagen-induced arthritis and cartilage destruction. Arthritis Rheum 41:110–121PubMedCrossRef
39.
go back to reference Corry D, Rishi K et al (2002) Decreased allergic lung inflammatory cell egression and increased susceptability to asphyxiation in MMP2-deficiency. Nat Immunol 3:347–353PubMedCentralPubMedCrossRef Corry D, Rishi K et al (2002) Decreased allergic lung inflammatory cell egression and increased susceptability to asphyxiation in MMP2-deficiency. Nat Immunol 3:347–353PubMedCentralPubMedCrossRef
40.
go back to reference Hartzell W, Shapiro S (1999) Marcophage elastase prevents Gemella morbillorum infection and improves outcome following murine bone marrow transplantation. Chest 116:31S–32SPubMedCrossRef Hartzell W, Shapiro S (1999) Marcophage elastase prevents Gemella morbillorum infection and improves outcome following murine bone marrow transplantation. Chest 116:31S–32SPubMedCrossRef
41.
go back to reference Burke B (2004) The role of matrix metalloproteinase 7 in innate immunity. Immunobiology 209:51–56PubMedCrossRef Burke B (2004) The role of matrix metalloproteinase 7 in innate immunity. Immunobiology 209:51–56PubMedCrossRef
43.
go back to reference Will C, Fromm M, Muller D (2008) Claudin tight junction proteins: novel aspects in paracellular transport. Perit Dial Int J Int Soc Perit Dial 28(6):577–584 Will C, Fromm M, Muller D (2008) Claudin tight junction proteins: novel aspects in paracellular transport. Perit Dial Int J Int Soc Perit Dial 28(6):577–584
44.
go back to reference Anderson JM, Balda MS, Fanning AS (1993) The structure and regulation of tight junctions. Curr Opin Cell Biol 5(5):772–778PubMedCrossRef Anderson JM, Balda MS, Fanning AS (1993) The structure and regulation of tight junctions. Curr Opin Cell Biol 5(5):772–778PubMedCrossRef
45.
go back to reference Fanning AS, Anderson JM (2009) Zonula occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions. Ann N Y Acad Sci 1165:113–120PubMedCentralPubMedCrossRef Fanning AS, Anderson JM (2009) Zonula occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions. Ann N Y Acad Sci 1165:113–120PubMedCentralPubMedCrossRef
46.
go back to reference Katsuno T, Umeda K et al (2008) Deficiency of zonula occludens-1 causes embryonic lethal phenotype associated with defected yolk sac angiogenesis and apoptosis of embryonic cells. Mol Biol Cell 19(6):2465–2475PubMedCentralPubMedCrossRef Katsuno T, Umeda K et al (2008) Deficiency of zonula occludens-1 causes embryonic lethal phenotype associated with defected yolk sac angiogenesis and apoptosis of embryonic cells. Mol Biol Cell 19(6):2465–2475PubMedCentralPubMedCrossRef
48.
go back to reference Umeda K, Ikenouchi J et al (2006) ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation. Cell 126(4):741–754PubMedCrossRef Umeda K, Ikenouchi J et al (2006) ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation. Cell 126(4):741–754PubMedCrossRef
49.
go back to reference Bertiaux-Vandaele N, Youmba SB et al (2011) The expression and the cellular distribution of the tight junction proteins are altered in irritable bowel syndrome patients with differences according to the disease subtype. Am J Gastroenterol 106(12):2165–2173PubMedCrossRef Bertiaux-Vandaele N, Youmba SB et al (2011) The expression and the cellular distribution of the tight junction proteins are altered in irritable bowel syndrome patients with differences according to the disease subtype. Am J Gastroenterol 106(12):2165–2173PubMedCrossRef
50.
go back to reference Schulzke JD, Ploeger S et al (2009) Epithelial tight junctions in intestinal inflammation. Ann N Y Acad Sci 1165:294–300PubMedCrossRef Schulzke JD, Ploeger S et al (2009) Epithelial tight junctions in intestinal inflammation. Ann N Y Acad Sci 1165:294–300PubMedCrossRef
51.
go back to reference Turner J (2009) Intestinal mucosal barrier function in health and disease. Nat Rev Immunol 9:799–809PubMedCrossRef Turner J (2009) Intestinal mucosal barrier function in health and disease. Nat Rev Immunol 9:799–809PubMedCrossRef
53.
go back to reference Schulzke JD, Gitter AH et al (2005) Epithelial transport and barrier function in occludin-deficient mice. Biochim Biophys Acta 1669(1):34–42PubMedCrossRef Schulzke JD, Gitter AH et al (2005) Epithelial transport and barrier function in occludin-deficient mice. Biochim Biophys Acta 1669(1):34–42PubMedCrossRef
54.
go back to reference Ulluwishewa D, Anderson RC et al (2011) Regulation of tight junction permeability by intestinal bacteria and dietary components. J Nutr 141(5):769–776PubMedCrossRef Ulluwishewa D, Anderson RC et al (2011) Regulation of tight junction permeability by intestinal bacteria and dietary components. J Nutr 141(5):769–776PubMedCrossRef
55.
go back to reference Fazeny-Dorner B, Veitl M et al (2002) Alterations in intestinal permeability following the intensified polydrug-chemotherapy IFADIC (ifosfamide, Adriamycin, dacarbazine). Cancer Chemother Pharmacol 49(4):294–298PubMedCrossRef Fazeny-Dorner B, Veitl M et al (2002) Alterations in intestinal permeability following the intensified polydrug-chemotherapy IFADIC (ifosfamide, Adriamycin, dacarbazine). Cancer Chemother Pharmacol 49(4):294–298PubMedCrossRef
56.
go back to reference Wardill H, Bowen J and Gibson R (2013) Irinotecan disrupts tight junction protein occludin in the rat small intestine, in Multinational Association for Supprotive Care in Cancer. J Support Care Cancer. Berlin, Germany Wardill H, Bowen J and Gibson R (2013) Irinotecan disrupts tight junction protein occludin in the rat small intestine, in Multinational Association for Supprotive Care in Cancer. J Support Care Cancer. Berlin, Germany
57.
go back to reference Bauer A, Burgers H et al (2010) Matrix metalloproteinase-9 mediates hypoxia-induced vascular leakage in the brain via tight junction rearrangement. J Cereb Blood Flow Metab 30:837–848PubMedCentralPubMedCrossRef Bauer A, Burgers H et al (2010) Matrix metalloproteinase-9 mediates hypoxia-induced vascular leakage in the brain via tight junction rearrangement. J Cereb Blood Flow Metab 30:837–848PubMedCentralPubMedCrossRef
58.
go back to reference Lischper M, Beuck S et al (2010) Metalloproteinase mediated occludin cleavage in the cerebral microcapillary endothelium under pathological conditions. Brain Res 1326:114–127PubMedCrossRef Lischper M, Beuck S et al (2010) Metalloproteinase mediated occludin cleavage in the cerebral microcapillary endothelium under pathological conditions. Brain Res 1326:114–127PubMedCrossRef
59.
go back to reference Vermeer P, Denker J et al (2009) MMP9 modulates tight junction integrity and cell viability in human airway epithelia. Am J Physiol Lung Cell Mol Physiol 296:L751–L762PubMedCentralPubMedCrossRef Vermeer P, Denker J et al (2009) MMP9 modulates tight junction integrity and cell viability in human airway epithelia. Am J Physiol Lung Cell Mol Physiol 296:L751–L762PubMedCentralPubMedCrossRef
60.
go back to reference Blecharz K, Haghikia A et al (2010) Glucocorticoid effects on endothelial barrier function in the murine brain endothelial cell line cEND incubated with sera from patients with multiple sclerosis. Mult Scler 16:293–302PubMedCrossRef Blecharz K, Haghikia A et al (2010) Glucocorticoid effects on endothelial barrier function in the murine brain endothelial cell line cEND incubated with sera from patients with multiple sclerosis. Mult Scler 16:293–302PubMedCrossRef
61.
go back to reference Liu W, Hendren J et al (2009) Normobaric hyperoxia attenuates early blood–brain barrier disruption by inhibiting MMP-9-mediated occludin degradation in focal cerebral ischemia. J Neurochem 108:811–820PubMedCentralPubMedCrossRef Liu W, Hendren J et al (2009) Normobaric hyperoxia attenuates early blood–brain barrier disruption by inhibiting MMP-9-mediated occludin degradation in focal cerebral ischemia. J Neurochem 108:811–820PubMedCentralPubMedCrossRef
62.
go back to reference Chen W, Hartman R, Ayer R, Marcantonio S, Kamper J, Tang J, Zhang JH (2009) Matrix metalloproteinases inhibition provides neuroprotection against hypoxia-ischemia in the developing brain. J Neurochem 111:726–736PubMedCrossRef Chen W, Hartman R, Ayer R, Marcantonio S, Kamper J, Tang J, Zhang JH (2009) Matrix metalloproteinases inhibition provides neuroprotection against hypoxia-ischemia in the developing brain. J Neurochem 111:726–736PubMedCrossRef
63.
go back to reference Higashida T, Kreipke CW, Rafols JA, Peng C, Schafer S, Schafer P, Ding JY, Dornbos D 3rd, Li X, Guthikonda M, Rossi NF, Ding Y (2011) The role of hypoxia-inducible factor-1alpha, aquaporin-4 and matrix metalloproteinase-9 in blood–brain barrier disruption and brain edema after traumatic brain injury. J Neurosurg 114:92–101PubMedCrossRef Higashida T, Kreipke CW, Rafols JA, Peng C, Schafer S, Schafer P, Ding JY, Dornbos D 3rd, Li X, Guthikonda M, Rossi NF, Ding Y (2011) The role of hypoxia-inducible factor-1alpha, aquaporin-4 and matrix metalloproteinase-9 in blood–brain barrier disruption and brain edema after traumatic brain injury. J Neurosurg 114:92–101PubMedCrossRef
64.
go back to reference Siu M, Lee W, Cheng C (2003) The interplay of collagen IV, tumor necrosis factor-alpha, gelatinase B (matrix metalloprotease-9), and tissue inhibitor of metalloproteases-1 in the basal lamina regulates Sertoli cell-tight junction dynamics in the rat testis. Endocrinology 144:371–387PubMedCrossRef Siu M, Lee W, Cheng C (2003) The interplay of collagen IV, tumor necrosis factor-alpha, gelatinase B (matrix metalloprotease-9), and tissue inhibitor of metalloproteases-1 in the basal lamina regulates Sertoli cell-tight junction dynamics in the rat testis. Endocrinology 144:371–387PubMedCrossRef
65.
go back to reference Gorodeski G (2007) Estrogen decrease in tight junction resistance involves matrix metalloproteinase-7-mediated remodeling of occludin. Endocrinology 148:218–231PubMedCentralPubMedCrossRef Gorodeski G (2007) Estrogen decrease in tight junction resistance involves matrix metalloproteinase-7-mediated remodeling of occludin. Endocrinology 148:218–231PubMedCentralPubMedCrossRef
66.
go back to reference Jeong S, Ledee D et al (2012) Interaction of clusterin and matrix metalloproteinase-9 and its implication for epithelial homeostasis and inflammation. Am J Pathol 180:2028–2039PubMedCentralPubMedCrossRef Jeong S, Ledee D et al (2012) Interaction of clusterin and matrix metalloproteinase-9 and its implication for epithelial homeostasis and inflammation. Am J Pathol 180:2028–2039PubMedCentralPubMedCrossRef
Metadata
Title
Gastrointestinal Mucositis: The Role of MMP-Tight Junction Interactions in Tissue Injury
Authors
Noor Al-Dasooqi
Hannah R. Wardill
Rachel J Gibson
Publication date
01-07-2014
Publisher
Springer Netherlands
Published in
Pathology & Oncology Research / Issue 3/2014
Print ISSN: 1219-4956
Electronic ISSN: 1532-2807
DOI
https://doi.org/10.1007/s12253-013-9733-y

Other articles of this Issue 3/2014

Pathology & Oncology Research 3/2014 Go to the issue
Webinar | 19-02-2024 | 17:30 (CET)

Keynote webinar | Spotlight on antibody–drug conjugates in cancer

Antibody–drug conjugates (ADCs) are novel agents that have shown promise across multiple tumor types. Explore the current landscape of ADCs in breast and lung cancer with our experts, and gain insights into the mechanism of action, key clinical trials data, existing challenges, and future directions.

Dr. Véronique Diéras
Prof. Fabrice Barlesi
Developed by: Springer Medicine