Increase in the ratio of matrix metalloproteinase-9 to tissue inhibitor of metalloproteinase-1 in saliva from patients with primary Sjögren's syndrome

Asatsuma, Masumi; Ito, Satoshi; Watanabe, Mamoru; Takeishi, Hideyuki; Nomura, Sadahiro; Wada, Yoko; Nakano, Masaaki; Gejyo, Fumitake; Igarashi, Atsuko

doi:10.1016/j.cccn.2004.03.006

Cited by 37 publications

(35 citation statements)

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“…Those activities had been previously described in whole saliva of healthy subjects (15). Studies on metalloproteinases involving glandular saliva are rather scarce and have been restricted to low numbers of subjects (32,33).…”

Section: Discussionmentioning

confidence: 99%

“…If those physical changes of parotid saliva from ICRP patients could be associated with changes in its molecular composition, it might be expected to use parotid saliva as an indicator of the functional status of the gland. In that direction, the use of saliva for the diagnosis of disorders that affect salivary glands has been documented in regard to Sjögren syndrome, in therapeutic irradiation of the maxillofacial territory in cancer patients, and in cystic fibrosis (15)(16)(17)(18). However, in the specialized literature, just a few sialochemical studies are referred to ICRP.…”

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confidence: 99%

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Molecular Alterations of Parotid Saliva in Infantile Chronic Recurrent Parotitis

et al. 2007

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Infantile chronic recurrent parotitis (ICRP) is an insidious disease whose etiopathogenesis remains an enigma. Alterations in the physical appearance of parotid saliva from ICRP patients have been frequently reported. However, sialochemical studies in regard to ICRP are very rare. The aim of this study was to determine whether saliva of ICRP patients presents major physicochemical and biochemical alterations compared with saliva from paired healthy controls. Parotid, whole, and submandibular/sublingual saliva was collected at an asymptomatic stage from 33 ICRP patients (5-16 y old, both sexes) and from 33 sex-and age-matched healthy controls. Saliva was analyzed for protein concentration, mode of protein diffusion on cellulose membranes, unidimensional sodium dodecylsulfate (SDS)-polyacrylamide gel electrophoresis protein profiles and zymographic profiles of metalloproteinase 2 (MMP-2) and metalloproteinase 9 (MMP-9). Parotid saliva of ICRP patients showed an increased protein concentration, altered mode of protein diffusion, a higher frequency of polypeptide bands of 43, 37,33,29,26,16, and 10 kD, higher asymmetry in the polypeptide profiles of both contralateral parotid saliva, and an increase in the frequency of MMP-2 and MMP-9. Parotid saliva of patients with ICRP is molecularly altered with respect to normal saliva. Some of the molecular differences could be related to the etiopathogenesis of the disease. ICRP is an inflammatory disease associated with nonobstructive glandular sialectasia. It is characterized by recurrent episodes of swelling of one or both parotid glands that alternate with remission intervals lasting for weeks or months in which glands are clinically asymptomatic (1,2). The onset of the disease usually occurs around age 3 y. Symptoms may diminish and disappear spontaneously after puberty. Sometimes the disease may persist until adulthood (1-3).Among the postulated etiological factors of ICRP are congenital ductal malformations, genetic factors, allergies, bacterial infections, local manifestations of autoimmune disease, and immunodeficiencies (1,2,4 -9). However, none of them has been demonstrated to play a causative role in the disease, and to date its etiopathogenesis remains an enigma.Likewise, consensus on the therapeutic management of ICRP has yet to be achieved. Different specialists have opted for different therapies. Among the therapeutic indications described in the specialized literature is a diversity of physical maneuvers to stimulate the salivary flux (1) and pharmacotherapy with nonsteroid anti-inflammatory agents (7) in combination with sialogogues and/or antibiotics (3,6,10). Recently, Nahlieli et al. (11) proposed an interventional approach using a sialendoscope. In cases in which irreversible damage has occurred, ligation of the excretory duct is indicated to produce glandular atrophy (1,2). In severe cases, partial or total parotidectomy is prescribed as a last resource (1,2,12).Studies on glandular tissue obtained from patients with ICRP have shown lymphocyt...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Molecular Alterations of Parotid Saliva in Infantile Chronic Recurrent Parotitis

et al. 2007

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“…For example, the expression of MMP10 in healthy human plasma is commonly ~0.03 nM, 13 and the levels of MMPs in urine and saliva are much lower than that in plasma. 48,49 We can replace the MMP2 cleavage substrate in the Pep-FITC with MMP10 cleavage substrate for the sensitive MMP10 detection. In reality, ∆ Figure 9 Fluorescence responses of the nrgO/Pep-FITc (100 nM) to various substances: Kcl (150 mM), Mgcl 2 (2.5 mM), Zncl 2 (2.5 mM), glucose (10 mM), glycine (1 mM), glutamine (1 mM), Bsa (100 nM), hsa (100 nM), MMP9 (2 nM), and MMP2 (2 nM).…”

Section: Detection Of Mmp2 Using Nrgo/pep-fitc Sensormentioning

confidence: 99%

A reduced graphene oxide-based fluorescence resonance energy transfer sensor for highly sensitive detection of matrix metalloproteinase 2

Xi¹,

Wang²,

Chen³

2016

IJN

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A novel fluorescence nanoprobe (reduced nano-graphene oxide [nrGO]/fluorescein isothiocyanate-labeled peptide [Pep-FITC]) for ultrasensitive detection of matrix metalloproteinase 2 (MMP2) has been developed by engineering the Pep-FITC comprising the specific MMP2 substrate domain (PLGVR) onto the surface of nrGO particles through non-covalent linkage. The nrGO was obtained by water bathing nano-graphene oxide under 90°C for 4 hours. After mixing the nrGO and Pep-FITC for 30 seconds, the fluorescence from Pep-FITC was almost completely quenched due to the fluorescence resonance energy transfer between fluorescein isothiocyanate (FITC) and nrGO. Upon cleavage of the amide bond between Leu and Gly in the Pep-FITC by protease-MMP2, the FITC bound to nrGO was separated from nrGO surface, disrupting the fluorescence resonance energy transfer process and resulting in fluorescence recovery of FITC. Under optimal conditions, the fluorescence recovery of nrGO/Pep-FITC was found to be directly proportional to the concentration of MMP2 within 0.02–0.1 nM. The detection limit of the nrGO/Pep-FITC was determined to be 3 pM, which is approximately tenfold lower than that of the unreduced carboxylated nano-graphene oxide/Pep-FITC probe.

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“…Cancer metastasis occurs as a result of imbalance between MMPs and TIMPs (Giannelli et al 2004). TIMPs and MMPs can be produced by many different cell types and are also found in all body fluids, such as saliva, gingival crevicular fluid, serum and urine (Asatsuma et al 2004). Unlike the other TIMPs, which are soluble, TIMP-3 is unique in being a component of ECM.…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and characterisation of the tissue inhibitor of metalloproteinase-3 gene from canine mammary tumour

Kumar

Yadav

Kumar

et al. 2013

Journal of Applied Animal Research

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Inhibition of matrix metalloproteinases (MMPs) by tissue inhibitors of metalloproteinases (TIMPs) has been reported to decrease metastasis and tumour-associated angiogenesis. The present study is aimed at characterising the gene encoding TIMP-3 from canine mammary tumour. We identified and cloned the full-length cDNA encoding TIMP-3 from canine mammary tumour. The entire open reading frame consisted of 636 nucleotides and 213 residues (accession number JF508171). Nucleotide and translated protein sequence were close to Sus scrofa but clustered away from the rodent group. Synonymous substitution (dS) was higher than non-synonymous substitution (dN), suggesting that the TIMP-3 gene was not under positive selection and that no advantageous mutations had any significant role in its evolutionary adaptation. The predicted SWISS-MODEL of canine TIMP-3 protein is composed of 7 a-helices and 12 b-turns. The G-factor score for the TIMP-3 protein model based on Ramachandran plot was found to be (0.47 for dihedral bonds, (0.08 for covalent bonds and (0.31 overall, which suggests that the model obtained for TIMP-3 is a reliable one.

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Increase in the ratio of matrix metalloproteinase-9 to tissue inhibitor of metalloproteinase-1 in saliva from patients with primary Sjögren's syndrome

Cited by 37 publications

References 14 publications

Molecular Alterations of Parotid Saliva in Infantile Chronic Recurrent Parotitis

Molecular Alterations of Parotid Saliva in Infantile Chronic Recurrent Parotitis

A reduced graphene oxide-based fluorescence resonance energy transfer sensor for highly sensitive detection of matrix metalloproteinase 2

Molecular cloning and characterisation of the tissue inhibitor of metalloproteinase-3 gene from canine mammary tumour

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