gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Matrix metallopeptidase 8

MMP-8, Matrix Metalloproteinase 8
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MMP-9, MMP-2, matrix metalloproteinase, HAD, CAN
Papers using MMP-8 antibodies
Inhibition of type 1 procollagen production in photodamage: correlation between presence of high molecular weight collagen fragments and reduced procollagen synthesis
Kang Young-Hee et al., In Nutrition Research and Practice, 2001
... Antibodies against human MMP-1, human MMP-8, human MMP-13, human type1 collagen, and human type1 procollagen were purchased from Santa Cruz Biotechnology (Santa Cruz, CA) ...
Papers on MMP-8
Vaginal Inflammation: Association between Leukocyte Concentration and Levels of Immune Mediators.
Gonçalves et al., Campinas, Brazil. In Am J Reprod Immunol, Feb 2016
We correlated extracellular matrix metalloproteinase inducer (EMMPRIN), matrix metalloproteinase-8 (MMP-8), hyaluronan (HA), hyaluronidase-1 (Hyal-1), human β-defensin-2 (hBD2), and neutrophil gelatinase-associated lipocalin (NGAL) concentrations with the extent of leukocyte infiltration into the vagina and suggest their participation in vaginal inflammation.
Analysis of matrix metalloproteinases, especially MMP-8, in gingival creviclular fluid, mouthrinse and saliva for monitoring periodontal diseases.
Mäntylä et al., In Periodontol 2000, Feb 2016
Matrix metalloproteinase-8 is a promising candidate biomarker for oral fluid (gingival crevicular fluid, peri-implant sulcular fluid and saliva) and mouthrinse chair-side/point-of-care diagnostics to predict, diagnose and determine the progressive phases of episodic periodontitis and peri-implantitis, as well as to monitor the treatments and medications.
Development and validation of a small single domain antibody that effectively inhibits matrix metalloproteinase 8.
Vandenbroucke et al., Gent, Belgium. In Mol Ther, Feb 2016
UNASSIGNED: A detrimental role for matrix metalloproteinase 8 (MMP8) has been identified in several pathological conditions, e.g.
Differential Effects of Dexamethasone and Doxycycline on Inflammation and MMP Production in Alkali-Burned Corneas Associated with Dry Eye.
de Paiva et al., Houston, United States. In Ocul Surf, Feb 2016
Dex treatment significantly decreased expression of IL-1β, IL-6, MMPs -1, -9, -13, and TIMP-1 after 2 days but increased levels of MMP-8, while Doxy treatment significantly decreased IL-1β, IL-6, MMP-8, and -9, compared to vehicle.
Use of crosslinkers to inactivate dentin MMPs.
Tezvergil-Mutluay et al., Turku, Finland. In Dent Mater, Feb 2016
Multiplex analysis of extracts of crosslinker-treated dentin showed a reduction in the MMP-8, MMP-2 and MMP-9 release.
Neutrophil proteolytic activation cascades: a possible mechanistic link between chronic periodontitis and coronary heart disease.
Sorsa et al., Helsinki, Finland. In Innate Immun, Jan 2016
MMP-8, MMP-9 and neutrophil elastase).
Decreased salivary matrix metalloproteinase-8 reflecting a defensive potential in juvenile parotitis.
Lauhio et al., Helsinki, Finland. In Int J Pediatr Otorhinolaryngol, Jan 2016
However, the role of MMP-8 has not been addressed previously.
FGR in the setting of preterm sterile intra-uterine milieu is associated with a decrease in RDS.
Yoon et al., Seoul, South Korea. In Pediatr Pulmonol, Jan 2016
AF inflammation was defined in the presence of AF MMP-8 ≥23 ng/ml.
Activation of dickkopf-1 and focal adhesion kinase pathway by tumour necrosis factor α induces enhanced migration of fibroblast-like synoviocytes in rheumatoid arthritis.
Kim et al., Taegu, South Korea. In Rheumatology (oxford), Jan 2016
Quantitative real-time PCR was used to measure the expression levels of DKK-1, integrin αv, laminin, fibronectin, E-cadherin, MMP-8 and MMP-13.
Low levels of tissue inhibitor of metalloproteinase-2 at birth may be associated with subsequent development of bronchopulmonary dysplasia in preterm infants.
Sheen et al., South Korea. In Korean J Pediatr, Nov 2015
METHODS: Serum was collected from 62 preterm infants at birth and analyzed for MMP-8, MMP-9, TIMP-2, and TIMP-1 by using enzyme-linked immunosorbent assay.
Matrix Metalloproteinases as Therapeutic Targets for Idiopathic Pulmonary Fibrosis.
Owen et al., Albuquerque, United States. In Am J Respir Cell Mol Biol, Nov 2015
MMPs and their inhibitors, tissue inhibitors of MMPs (TIMPs), have been implicated in the pathogenesis of IPF based upon the results of clinical studies reporting elevated levels of MMPs (including MMP-1, MMP-7, MMP-8, and MMP-9) in IPF blood and/or lung samples.
Pathology and immune reactivity: understanding multidimensionality in pulmonary tuberculosis.
Kaufmann et al., Berlin, Germany. In Semin Immunopathol, Nov 2015
Gradients of cytokines and chemokines (CCR2, CXCR2, CXCR3/CXCR5 agonists; TNF/IL-10, IL-1/IFN-I), expression of activation/death markers on immune cells (TNF receptor 1, PD-1, IL-27 receptor) or abundance of enzymes [arginase-1, matrix metalloprotease (MMP)-1, MMP-8, MMP-9] drive genesis and progression of lesions.
Non-healing foot ulcers in diabetic patients: general and local interfering conditions and management options with advanced wound dressings.
Giurato et al., Roma, Italy. In J Wound Care, Apr 2015
EPA (mainly MMP 9, MMP-8 and elastase) and inflammatory factors present in the wound bed (such as IL-1, IL-6, and TNFa) account for the catabolic state of non-healing ulcers.
Metalloproteinases and Their Tissue Inhibitors in Comparison between Different Chronic Pneumopathies in the Horse.
Gehlen et al., Berlin, Germany. In Mediators Inflamm, 2014
Zymography and equine MMP and TIMP assays were used to detect MMP-2, MMP-8, MMP-9 as well as TIMP-1, and TIMP-2 in BALF supernatant.
Single nucleotide polymorphism -799C/T in matrix metalloproteinase-8 promoter region in arterial disease.
Sorsa et al., Helsinki, Finland. In Innate Immun, 2012
gene polymorphism is associated with atherosclerosis in Finland
[Association between matrix metalloproteinase-8 -799C/T polymorphism and instability of carotid plaque].
Jin et al., Linhai, China. In Zhonghua Yi Xue Yi Chuan Xue Za Zhi, 2012
Serum level of MMP-8 in the carotid vulnerable plaque group was higher than that in the carotid stable plaque group.
MMP-8 -799 C>T genetic polymorphism is associated with the susceptibility to chronic and aggressive periodontitis in Taiwanese.
Tsai et al., Kao-hsiung, Taiwan. In J Clin Periodontol, 2011
Multivariate logistic regression analysis with adjustment for age, gender and smoking indicated that increased risks of aggressive periodontitis and chronic periodontitis were associated with the -799 T allele of matrix metalloproteinase-8.
[Study on association between single nucleotide polymorphisms of MMP7, MMP8, MMP9 genes and development of gastric cancer and lymph node metastasis].
Kwack et al., South Korea. In Korean J Gastroenterol, 2011
The allele and genotype frequencies of MMP8 rs11225395 were not associated with the development of gastric cancer development and lymph node metastasis.
Association of MMP-8 polymorphisms with tendinopathy of the primary posterior tibial tendon: a pilot study.
Santos et al., São Paulo, Brazil. In Clinics (sao Paulo), 2010
The preliminary results indicate that this polymorphism may be a risk factor for tendinopathy and could be used as a genetic marker for the primary lesions of the posterior tibial tendon.
Analysis of the matrix metalloproteinase family reveals that MMP8 is often mutated in melanoma.
Samuels et al., Bethesda, United States. In Nat Genet, 2009
Expression of wild-type but not mutant MMP8 in human melanoma cells inhibited growth on soft agar in vitro and tumor formation in vivo, suggesting that wild-type MMP-8 has the ability to inhibit melanoma progression.
share on facebooktweetadd +1mail to friends