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MMP7 shedding of syndecan-1 (zeige SDC1 Proteine)/CXCL1 (zeige CXCL1 Proteine) complexes functions as a checkpoint that restricts neutrophil activation at sites of epithelial injury.
MMP7 exerts a restrictive role on H. pylori-induced gastric injury and the development of premalignant lesions by suppressing M1 macrophage polarization.
absence of MMP7 protects mice from LPS (zeige TLR4 Proteine)-induced intestinal permeability and lethality.
regulator of beta-catenin (zeige CTNNB1 Proteine) function in injured lung epithelium
Angiotensin II suppresses RECK (zeige RECK Proteine), but induces matrix metalloproteinases both in vivo and in vitro.
MMP7 regulated ciliated cell formation.
SPARC (zeige SPARC Proteine) suppresses angiogenesis of gastric cancer by down-regulating the expression of VEGF (zeige VEGFA Proteine) and MMP-7
Protein expression levels of MMP-7, MMP-14 and ERK1/2 phosphorylation level were all elevated with the increasing pathological grades in brain glioma tissues.
levels of renal MMP-7 correlate with Wnt (zeige WNT2 Proteine)/beta-catenin (zeige CTNNB1 Proteine) activity.
STAT3 (zeige STAT3 Proteine) plays an important role in regulation of tumor growth, invasion, and angiogenesis, which could be act by reducing MMP-7 expression in pancreatic cancer cells.
Studies have identified an unexpected tumor-suppressive role for host-derived MMP-7 in myeloma bone disease in vivo, and highlight the importance of elucidating the effect of individual MMPs in a disease-specific context.
the crosstalk between ARF and MMP7 in nucleus contributes to ECM (zeige MMRN1 Proteine) network in tumor microenvironments in vivo, implicating a novel therapeutic target for advanced PCa (zeige FLVCR1 Proteine) treatment.
Data suggest that HAI1 (zeige SPINT1 Proteine), a protease on the surface of colon carcinoma cells, is an MMP7 substrate; proteolysis by MMP7 releases extracellular region as soluble HAI1 (zeige SPINT1 Proteine) (sHAI1); sHAI1 induces cancer cell aggregation; cholesterol sulfate is required for MMP-7--catalyzed generation of sHAI1. (HAI1 (zeige SPINT1 Proteine) = hepatocyte growth factor activator inhibitor type 1 (zeige SPINT1 Proteine); MMP7 = matrix metalloproteinase-7)
Results indicate that the matrix metallopeptidase 7 (MMP7)A-181G genotype interacts with age and gender and may serve as an early and predictive biomarker for childhood acute lymphoblastic leukemia (ALL).
The A/A genotype (OR=0.120) and A allele (OR=0.442) reduce the risk of recurrent depressive disorder occurrence in the examined polymorphisms for MMP-2 (zeige MMP2 Proteine), MMP-7 and MMP-9 (zeige MMP9 Proteine).
SLC12A5 (zeige SLC12A5 Proteine) promoted the migration and invasion of BUC by enhancing MMP-7 expression.
Overexpression of LAMC2 (zeige LAMC2 Proteine) and knockdown of CD82 (zeige CD82 Proteine) markedly promoted GC cell invasion and activated EGFR (zeige EGFR Proteine)/ERK1/2-MMP7 signaling via upregulation of the expression of phosphorylated (p)-EGFR (zeige EGFR Proteine), p-ERK1/2 and MMP7.
Matrix Metalloproteinase-7 Promoter polymorphism is associated with breast Cancer.
Data suggest that the cytoplasmic domain of Sdc2 (zeige SDC2 Proteine) is involved in regulation of expression of MMP7 in colon carcinoma/adenocarcinoma cells; induction of MMP7 involves protein kinase C gamma (zeige PRKCG Proteine)-mediated FAK (zeige PTK2 Proteine)/ERK (zeige EPHB2 Proteine) signaling. (Sdc2 (zeige SDC2 Proteine) = syndecan-2 (zeige SDC2 Proteine); MMP7 = matrix metalloproteinase-7; FAK (zeige PTK2 Proteine) = focal adhesion kinase 1 (zeige PTK2 Proteine))
We conclude that in the resected esophageal cancer an increased mRNA expression of MMP-7, MMP-10 (zeige MMP10 Proteine) and TIMP-1 (zeige TIMP1 Proteine) correlated with clinicopathologic features. We suggest that these genes may play a role during progression of the disease MMP-10 (zeige MMP10 Proteine), MMP-7, TIMP-1 (zeige TIMP1 Proteine), TIMP-2 (zeige TIMP2 Proteine) were overexpressed in 73%, 85%, 55% and 42% of esophageal cancer samples, respectively.
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. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
, matrilysin, uterine
, matrix metalloproteinase 7
, matrix metalloproteinase-7
, pump-1 protease
, uterine metalloproteinase
, Matrix metalloproteinase 7 (matrilysin)
, matrix metalloproteinase 7 (matrilysin, uterine)
, uterine matrilysin
, matrilysin-related protein