The role of matrix metalloproteinases in recurrent tonsillitis

Acıoğlu, Engin; Yiğit, Özgür; Alkan, Zeynep; Server, Ela Araz; Uzun, Hafize; Gelişgen, Ramisa

doi:10.1016/j.ijporl.2010.02.016

Cited by 10 publications

(5 citation statements)

References 28 publications

(28 reference statements)

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“…In particular, it has been reported that the joint action of PEP and metalloprotease-8 and -9 produce a chemokine, proline-glycineproline (PGP), a peptide that has chemoattractant properties in these processes [24]. Bearing in mind that changes in metalloprotease levels have been reported in tonsil disease [7] and that the activity of PEP is also altered, it is possible that the combined action of these proteolytic enzymes has a role in CT, TH and/or AH.…”

Section: Discussionmentioning

confidence: 99%

Altered dipeptidyl peptidase IV and prolyl endopeptidase activities in chronic tonsillitis, tonsillar hyperplasia and adenoid hyperplasia

Larrinaga¹,

Perez²,

Sanz³

et al. 2011

International Journal of Pediatric Otorhinolaryngology

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Section: Discussionmentioning

confidence: 99%

Altered dipeptidyl peptidase IV and prolyl endopeptidase activities in chronic tonsillitis, tonsillar hyperplasia and adenoid hyperplasia

Larrinaga¹,

Perez²,

Sanz³

et al. 2011

International Journal of Pediatric Otorhinolaryngology

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“…The specific increases in MMP-7 and -9 activities suggest that they are the main promoters of ECM degradation that responded to inflammatory changes in the tonsillar tissue. 128 MMP-7 has also been described as a useful biomarker for idiopathic pulmonary fibrosis. 116 …”

Section: Special Attributes Of Specific Mmpsmentioning

confidence: 99%

Biochemical and Biological Attributes of Matrix Metalloproteinases

Cui

Khalil

2017

Progress in Molecular Biology and Translational Science

961

891

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Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that are involved in the degradation of various proteins in the extracellular matrix (ECM). Typically, MMPs have a propeptide sequence, a catalytic metalloproteinase domain with catalytic zinc, a hinge region or linker peptide, and a hemopexin domain. MMPs are commonly classified on the basis of their substrates and the organization of their structural domains into collagenases, gelatinases, stromelysins, matrilysins, membrane-type (MT)-MMPs, and other MMPs. MMPs are secreted by many cells including fibroblasts, vascular smooth muscle (VSM) and leukocytes. MMPs are regulated at the level of mRNA expression and by activation of their latent zymogen form. MMPs are often secreted as inactive proMMP form which is cleaved to the active form by various proteinases including other MMPs. MMPs cause degradation of ECM proteins such as collagen and elastin, but could influence endothelial cell function as well as VSM cell migration, proliferation, Ca2+ signaling and contraction. MMPs play a role in tissue remodeling during various physiological processes such as angiogenesis, embryogenesis, morphogenesis and wound repair, as well as in pathological conditions such as myocardial infarction, fibrotic disorders, osteoarthritis, and cancer. Increases in specific MMPs could play a role in arterial remodeling, aneurysm formation, venous dilation and lower extremity venous disorders. MMPs also play a major role in leukocyte infiltration and tissue inflammation. MMPs have been detected in cancer, and elevated MMP levels have been associated with tumor progression and invasiveness. MMPs can be regulated by endogenous tissue inhibitors of metalloproteinases (TIMPs), and the MMP/TIMP ratio often determines the extent of ECM protein degradation and tissue remodeling. MMPs have been proposed as biomarkers for numerous pathological conditions and are being examined as potential therapeutic targets in various cardiovascular and musculoskeletal disorders as well as cancer.

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“…MMP‐7 expression was found to be increased in the bronchial epithelial cells of asthmatic patients, but the association of MMP‐7 with wound repair and the low level of expression in asthmatic patients indicates this may be more of a result of the condition rather than a cause (Parker et al, ). MMP‐7 was also found to be a major promoter of inflammation in tonsillitis and was identified as a potential treatment target for recurrent tonsillitis (Acioglu et al, ). Recently, MMP‐7 was identified as a key player in the pathogenesis of noise‐induced hearing loss.…”

Section: Matrix Metalloproteinase‐7mentioning

confidence: 99%

Intricate Functions of Matrix Metalloproteinases in Physiological and Pathological Conditions

Mittal

Patel

Debs

et al. 2016

Journal Cellular Physiology

143

115

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Matrix metalloproteinases (MMPs) are a diverse group of proteolytic enzymes and play an important role in the degradation and remodeling of the extracellular matrix (ECM). In normal physiological conditions, MMPs are usually minimally expressed. Despite their low expression, MMPs have been implicated in many cellular processes ranging from embryological development to apoptosis. The activity of MMPs is controlled at three different stages: (1) transcription; (2) zymogen activation; and (3) inhibition of active forms by tissue inhibitor metalloproteinases (TIMPs). They can collectively degrade any component of ECM and basement membrane, and their excessive activity has been linked to numerous pathologies mainly including, but not limited to, tumor invasion and metastasis. The lack of information about several MMPs and the steady stream of new discoveries suggest that there is much more to be studied in this field. In particular, there is a need for controlling their expression in disease states. Various studies over the past 30 years have found that each MMP has a specific mode of activation, action, and inhibition. Drugs specifically targeting individual MMPs could revolutionize the treatment of a great number of health conditions and tremendously reduce their burden. In this review article, we have summarized the recent advances in understanding the role of MMPs in physiological and pathological conditions. J. Cell. Physiol. 231: 2599-2621, 2016. © 2016 Wiley Periodicals, Inc.

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The role of matrix metalloproteinases in recurrent tonsillitis

Cited by 10 publications

References 28 publications

Altered dipeptidyl peptidase IV and prolyl endopeptidase activities in chronic tonsillitis, tonsillar hyperplasia and adenoid hyperplasia

Altered dipeptidyl peptidase IV and prolyl endopeptidase activities in chronic tonsillitis, tonsillar hyperplasia and adenoid hyperplasia

Biochemical and Biological Attributes of Matrix Metalloproteinases

Intricate Functions of Matrix Metalloproteinases in Physiological and Pathological Conditions

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