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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Matrix metallopeptidase 28

MMP-28, Epilysin, MMP-25, Matrix metalloproteinase-28, MM-28
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix for both normal physiological processes, such as embryonic development, reproduction and tissue remodeling, and disease processes, such as asthma and metastasis. This gene encodes a secreted enzyme that degrades casein. Its expression pattern suggests that it plays a role in tissue homeostasis and in wound repair. Transcript variants encoding different isoforms have been described. [provided by RefSeq, Mar 2010] (from NCBI)
Top mentioned proteins: MMP-9, CAN, POLYMERASE, MMP-7, MMP-19
Papers on MMP-28
Transcriptomics and the mechanisms of antidepressant efficacy.
Dobson et al., Los Angeles, United States. In Eur Neuropsychopharmacol, Dec 2015
When analysing individual genes, we observed that changes in the expression of two genes (MMP28 and KXD1) were associated with better response to nortriptyline.
DNA hypermethylation of extracellular matrix-related genes in human periodontal fibroblasts induced by stimulation for a prolonged period with lipopolysaccharide derived from Porphyromonas gingivalis.
Abiko et al., Tōbetsu, Japan. In J Periodontal Res, Dec 2015
Among these genes, hypermethylation of nine ECM-related genes, FANK1, COL4A1-A2, 12A1 and 15A1, LAMA5 and B1, MMP25, POMT1 and EMILIN3, induced a significantly downregulated expression of their mRNA.
Matrix Metalloproteinases as Therapeutic Targets for Idiopathic Pulmonary Fibrosis.
Owen et al., Albuquerque, United States. In Am J Respir Cell Mol Biol, Nov 2015
These mechanisms include MMPs: (1) promoting epithelial-to-mesenchymal transition (MMP-3 and MMP-7); (2) increasing lung levels or activity of profibrotic mediators or reducing lung levels of antifibrotic mediators (MMP-3, MMP-7, and MMP-8); (3) promoting abnormal epithelial cell migration and other aberrant repair processes (MMP-3 and MMP-9); (4) inducing the switching of lung macrophage phenotypes from M1 to M2 types (MMP-10 and MMP-28); and (5) promoting fibrocyte migration (MMP-8).
Nicotine stimulation increases proliferation and matrix metalloproteinases-2 and -28 expression in human dental pulp cells.
Filippo et al., Novara, Italy. In Life Sci, Sep 2015
Moreover, as it is known that nicotine could upregulate the expression of matrix metalloproteinases (MMPs), enzymes involved in pulpal inflammation, the effects of nicotine stimulation on MMP-2 and MMP-28 gene expression have also been investigated.
miRNA-144 suppresses proliferation and migration of colorectal cancer cells through GSPT1.
Chai et al., Taiyuan, China. In Biomed Pharmacother, Aug 2015
In addition, further mechanic investigations revealed that miRNA-144 suppressed the expression of GSPT1 to regulate the expression of c-myc, survivin and Bcl2L15 which are involved in cell proliferation, and that metastasis related factor MMP28 was also down-regulated by miRNA144.
Expression and clinical significance of matrix metalloproteinase-17 and -25 in gastric cancer.
Luo et al., Wuhan, China. In Oncol Lett, Feb 2015
UNASSIGNED: The aim of the present study was to investigate the expression and clinicopathological features of matrix metalloproteinase 17 (MMP17; also known as MT4-MMP) and MMP25 (also known as MT6-MMP) in gastric cancer.
Immunohistochemical Similarities between Lichen Sclerosus et Atrophicus and Morphea: A Case Study.
Aiba et al., Sendai, Japan. In Case Rep Dermatol, 2015
In this report, we describe a case of LSA on the abdomen accompanied by morphea; we employed immunohistochemical staining for periostin as well as MMP-7 and MMP-28, both of which are reported to facilitate fibrosis in the development of various organs, including skin.
Epilysin is overexpressed in glioblastoma and related to clinical outcome of patients.
Sun et al., Changchun, China. In Med Oncol, 2015
As the newest identified member of the matrix metalloproteinase (MMP) family, the expression pattern and function of epilysin (MMP-28) are still not well understood.
Adult-onset acquired partial lipodystrophy accompanied by rheumatoid arthritis.
Aiba et al., Sendai, Japan. In Case Rep Dermatol, 2015
Interestingly, immunohistochemical staining revealed dense infiltration of IL-27-producing cells as well as MMP-7-and MMP-28-expressing cells, both of which have been reported to facilitate the development of autoimmune disease.
Parp-1 genetic ablation in Ela-myc mice unveils novel roles for Parp-1 in pancreatic cancer.
Navarro et al., Barcelona, Spain. In J Pathol, 2014
Finally, molecular analysis revealed that Parp-1 modulates ADM downstream of the Stat3-MMP7 axis and is also involved in transcriptional up-regulation of the MDM2, VEGFR1 and MMP28 cancer-related genes.
Proteinases and plaque rupture: unblocking the road to translation.
Newby, Bristol, United Kingdom. In Curr Opin Lipidol, 2014
Novel targets, including MMP-8, MMP-10, MMP-14, MMP-19, MMP-25 and MMP-28, are also being considered.
Characterization of interleukin-33 and matrix metalloproteinase-28 in serum and their association with disease severity in patients with coronary heart disease.
Zhang et al., Zhengzhou, China. In Coron Artery Dis, 2014
OBJECTIVE: To investigate serum levels of interleukin (IL)-33 and matrix metalloproteinase-28 (MMP-28) in patients with coronary heart disease (CHD) and to evaluate their association with disease severity.
Ovarian membrane-type matrix metalloproteinases: induction of MMP14 and MMP16 during the periovulatory period in the rat, macaque, and human.
Curry et al., Göteborg, Sweden. In Biol Reprod, 2014
Among the six known MT-MMPs, mRNA expression of Mmp14, Mmp16, and Mmp25 was increased after human chorionic gonadotropin (hCG) administration in rats.
Chronic exposure to cigarette smoke increases matrix metalloproteinases and Filaggrin mRNA expression in oral keratinocytes: role of nicotine stimulation.
Cannas et al., Novara, Italy. In Oral Oncol, 2011
basal expression of MMP-2, MMP-9, MMP-28, and Filaggrin was evaluated in oral keratinocytes to collect information about ability of cigarette smoke to modify basal expression pattern of these key enzymes in the absence of clinical signs in oral epithelium
MMP28 (epilysin) as a novel promoter of invasion and metastasis in gastric cancer.
Jian et al., Suzhou, China. In Bmc Cancer, 2010
MMP28 is frequently overexpressed during progression of gastric carcinoma, and contributes to tumor cell invasion and metastasis.
Human MMP28 expression is unresponsive to inflammatory stimuli and does not correlate to the grade of intervertebral disc degeneration.
Wuertz et al., Zürich, Switzerland. In J Negat Results Biomed, 2010
Gene expression of MMP28 in the intervertebral disk is not regulated by inflammatory mechanisms, is donor-dependent and cannot be positively or negatively linked to the grade of degeneration and only weakly to the occurrence of trauma.
Epilysin (matrix metalloproteinase-28) contributes to airway epithelial cell survival.
Parks et al., Seattle, United States. In Respir Res, 2010
Over-expression of MMP28 provides protection against apoptosis induced by either serum-deprivation or treatment with a protein kinase inhibitor.
MMP28 gene expression is regulated by Sp1 transcription factor acetylation.
Clark et al., Norwich, United Kingdom. In Biochem J, 2010
MMP28 gene expression is regulated by Sp1 transcription factor acetylation.
Epilysin (MMP-28)--structure, expression and potential functions.
Keski-Oja et al., Helsinki, Finland. In Exp Dermatol, 2008
Epilysin (MMP-28) is the newest member of the matrix metalloproteinase (MMP) family of extracellular proteases.
MT4-(MMP17) and MT6-MMP (MMP25), A unique set of membrane-anchored matrix metalloproteinases: properties and expression in cancer.
Fridman et al., Detroit, United States. In Cancer Metastasis Rev, 2008
Two members of the MT-MMP subfamily, MMP-17 (MT4-MMP) and MMP-25 (MT6-MMP), are anchored to the plasma membrane via a glycosyl-phosphatidyl inositol (GPI) anchor, which confers these enzymes a unique set of regulatory and functional mechanisms that separates them from the rest of the MMP family.
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