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Only MMP-1 and MMP-8 cleaved CXCL5, with MMPs 1, 8, 9, 13 and 14 cleaving CXCL8.
MMPs 1, 8, and 13 are true collagenases, where their ancillary hemopexin domains are essential for the ability of these enzymes to degrade triple helical collagen.
The aim was to evaluate immunoexpression of matrix metalloproteinases (MMPs) 1, 2, 7, 9, and 26 in calcifying cystic odontogenic tumor (CCOT).
The objective of this study was to analyze the expression of matrix metalloproteinases (MMPs) 1, 7, and 26 in odontogenic keratocysts (OKCs) associated with Gorlin syndrome (SOKCs) and nonsyndrome OKCs (NSOKCs).
Both salmon calcitonin (sCT) and hyaluronic acid (HA) attenuated activated mRNA expression of NR4A1, NR4A2, NR4A3, and matrix metalloproteinases (MMPs) 1, 3 and 13 in three human cell lines: SW1353 chondrocytes, U937 and THP-1 monocytes.
In addition to MMP-9, other important stromal, endothelial and leukocytic MMPs 1, -2, and -13 could also process LIX at Ser4∼Val5 (Figure 3), but like MMP-8, did not cleave KC, MIP-2, or DCIP-1 (not shown).
Similar(31)
During OA, much of the cartilaginous ECM is degraded by catabolic enzymes namely ADAMTS's and other MMPs [ 1, 2, 6].
This interpretation is supported by evidence that E-cadherin cleavage is mediated by MMPs [ 1, 32, 33].
Collectively, however, the implicated MMPs (−1, -2, -3, -7, -8, -9, -12 and −13) are capable of degrading most dermal ECM components [9, 52].
Invasion of cells through the extracellular matrix (ECM) is a complicated process involving migration by two alternating modes of action with either cellular deformation allowing movement through the ECM or by degradation of the ECM using factors such as MMPs [1], [2].
The mRNA expression of MMPs -1, -3 and -13 was studied by real time PCR.
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