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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.
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Human Polyclonal MMP28 Primary Antibody for ELISA, IHC - ABIN4335121
Singh, Kindelberger, Nagymanyoki, Ng, Quick, Elias, Yamamoto, Fichorova, Fulop, Berkowitz: Matrix metalloproteinases and their inhibitors and inducer in gestational trophoblastic diseases and normal placenta. in Gynecologic oncology 2011
Circulating MMP-28 was elevated in atrial fibrillation
Results suggest a crucial role of MMP9 (show MMP9 Antibodies) at the early stage of carcinogenesis in the large intestine. The increase in MMP9 (show MMP9 Antibodies) and TIMP1 (show TIMP1 Antibodies) mRNA concentration and the decrease in MMP28 in the large intestinal tissue may be a confirmation of cancer.
These results proved for the first time that epilysin expression was significantly elevated in glioblastoma
A decreased level of IL-33 (show IL33 Antibodies) and an elevated concentration of MMP-28 were found in coronary heart disease patients and correlated with disease severity.
MMP28 mRNA expression is highest in healthy tissues when compared to diseased periodontal tissues.
Data established a seven-gene (AR, ESR2 (show ESR2 Antibodies), GATA3 (show GATA3 Antibodies), GBX2 (show GBX2 Antibodies), KRT16 (show KRT16 Antibodies), MMP28 and WNT11 (show WNT11 Antibodies)) prognostic signature to define a subset of triple-negative breast cancer (TNBC).
Inhibition of BCMO1 (show BCMO1 Antibodies) expression is associated with increased invasiveness of colon cancer cells and increased expression of MMP7 (show MMP7 Antibodies) and MMP28. beta-Carotene can upregulate BCMO1 (show BCMO1 Antibodies) and reverse these effects.
Over-expression of MMP28 provides protection against apoptosis induced by either serum-deprivation or treatment with a protein kinase inhibitor.
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.
basal expression of MMP-2 (show MMP2 Antibodies), MMP-9 (show MMP9 Antibodies), MMP-28, and Filaggrin (show FLG Antibodies) 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
results demonstrate that Ranbp2 controls nucleocytoplasmic, chemokine and metalloproteinase 28 signaling, and proteostasis of substrates that are crucial to motoneuronal homeostasis and whose impairments by loss of Ranbp2 drive ALS-like syndromes
MMP28 promotes macrophage polarization toward M2 cells and augments pulmonary fibrosis.
MMP-28 deletion aggravated MI-induced LV dysfunction and rupture as a result of defective inflammatory response and scar formation by suppressing M2 macrophage activation.
Epilysin is alternatively spliced and processed by a furin (show FURIN Antibodies)-like proprotein convertase.
These results suggest that MMP-28 plays an evolutionarily conserved role in neural development and is likely to modulate the axonal-glial extracellular microenvironment.
Epilysin serves as a negative regulator of early macrophage recruitment, a novel function that may have evolved as a mechanism to restrain unnecessary and untimely inflammation.
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.
matrix metalloproteinase-28 b
, matrix metallopeptidase 28 b
, matrix metallopeptidase 28
, matrix metalloproteinase 28
, matrix metalloproteinase-28
, matrix metallopeptidase 28 (epilysin)
, matrix metalloproteinase 28 (epilysin)