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At the molecular level, this switch could be linked to two main changes: the decrease in the expression of matrix protease genes and the reduced expression of the Rho GTP-binding protein Rnd3.
The lack of major abnormalities is attributed to a marked elevation in the expression of matrix metalloproteinases, for example, MMP2 and MMP14 in the Hpse-KO liver and kidney.
Despite complete lack of heparanase gene expression and enzymatic activity, the mice developed normally, were fertile and did not exhibit apparent anatomical and functional abnormalities, presumably because heparanase deficiency was compensated in most organs (i.e., liver, kidney) by a marked elevation in the expression of matrix metalloproteinase i.e., MMP-9 and MMP-14 family members.
The osteocyte activity, resulting from excess mechanical loading, increases the respective activities of osteoblasts and osteoclasts, as evident from increase in the expression of matrix proteins (COL1A, SPARC, and IBSP) and osteoclast-specific enzymes (CTSK and ACP5) (Table 3 & 4; Figure 5).
Real-time quantitative polymerase chain reaction was used to quantify changes in the expression of matrix proteinase in the treated cells.
There was strong suppression in the expression of matrix proteins including collagen types 1, 2, 6 and 9, proteoglycans, aggrecan and fibromodulin.
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In addition, the expression of matrix metaloproteinase-9, a gelatinase involved in leukocyte migration within the damaged liver was inhibited by the treatment [ 30].
In addition, the expression of matrix metalloproteinases (MMPs), responsible for the degradation of extracellular matrix components, is increased during HP infection, thereby enhancing chronic atrophic gastritis (Bergin et al, 2004).
A progressive increase in the expression of matrix-metalloproteasis MMP-2 ( i.e. the ability of invasion) was observed.
We next investigated the possible role of NAMPT in the expression of matrix-degrading enzymes and ECM proteins in chondrocytes.
Kong et al. [ 48] observed that HP stimulates the synthesis of CACUL1 in a gastric tumor cell line, which in turn promotes the expression of matrix metalloproteinase 9 and increases invasion and metastasis.
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