1997 Fiscal Year Final Research Report Summary
Degradation system of extracellular matrix components in nasal polyp formation
| Project/Area Number |
07671851
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Otorhinolaryngology
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| Research Institution | Mie University |
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Principal Investigator |
HARADA Teruhiko Mie University, Hospital Lecturer, 医学部・附属病院, 講師 (20183569)
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| Co-Investigator(Kenkyū-buntansha) |
MAJIMA Yuichi Mie University, Hospital Lecturer, 医学部・附属病院, 講師 (60024791)
SAKAKURA Yasuo Mie University, Faculty of Medicine, Professor, 医学部, 教授 (40024723)
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| Project Period (FY) |
1995 – 1997
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| Keywords | Nasal polyp / Paranasal sinusitis / Nasal allergy / Extracellular matrix / Matrix metalloproteinase |
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| Research Abstract |
The etiology and pathogenesis of nasal polyps and polypoid formations of nasal of paranasal mucosa have been the subjects of debate. We have reported that the extracellular matrix is a complex aggregate of distinct collagenous and non-collagenous protein components in nasal polyps, which in physiologic situations are in a dynamic equlibrium.
Remodeling of the extracellular matrix is a prominent feature in various biological processes ranging from wound healing and tissue development to tumor invasion and chronic inflammatory disorders. During nasal polyp formation, degradative enzymes are probably involved in the removal of devitalized tissues, epidermal : mesenchymal interactions, angiogenesis, and remodeling of newly synthesized connective tissue. We have, therefore, studied the distribution of matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) in nasal and paranasal mucosa, in an attempt to elucidate the mechanism of nasal polyp formation.
The distribution of 4 major MMPs was studied in nasal polyps : collagenase (MMP-1) which degrades fibrillar interstitial collagens, a 72-kDa gelatinase (MMP-2) which mainly degrades type IV collagen and denatured collagens, stromelysin (MMP-3) which has a wider range of action, and a 92-kDa gelatinase (MMP-9) which has a wide range of substrate specificity against collagens. These MMPs and the MMP tissual inhibitors (TIMP-1 and TIMP-2) were detected by immunohistochemistry. MMP-1 and MMP-2 were detected in the fibroblasts at the periphery fo nasal polyp stalks. MMP-9 was detected in the inflammatory cells in the subepithelial area of polypoid mucosa and nasal polyps. TIMP-1 and TIMP-2 were also detected in a few fibroblasts in the edematous mucosa. These results suggest the role of MMPs in the breakdown of collagenous and non-collagenous connective tissue and basement membranes. The disequilibrium of MMPs and TIMPs in nasal and paranasal mucosa may promote nasal polyp growth.
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