To investigate collagen metabolism in keratinocytes and fibroblasts co-culture under pressure, and study the role of IL-1[alpha] and MMP-3
in terms of regulating fibroblasts-keratinocytes collagen metabolism with pressure.
Matrix metalloproteinases (MMPs) are special class of proteases that are categorized in five groups as per their substrate specificity: collagenases (MMP-1, -8 and -13), gelatinases (MMP-2 and -9), stromelysins (MMP-3
, -10, and -11), matrilysins (MMP-7) and membrane-type (MMP-14 to -17, -24 and -25).
Glycitein inhibits glioma cell invasion through down-regulation of MMP-3
and MMP-9 gene expression.
Twenty-four MMPs have been identified, including collagenases (MMP-1, 8, 13, and 18), gelatinases (MMP-2 and 9), stromelysins (MMP-3
and 10), matrilisins (MMP-7 and 26), and membrane-type MMPs (MMP-14, 15, 16, 17, 24, and 25), among other types.
Depending on the substrate specificity and structure, MMPs are divided into several subgroups: collagenases (e.g., MMP-1), gelatinases (e.g., MMP-2 and MMP-9), stromelysins (e.g., MMP-3
and MMP-10), matrilysins (e.g., MMP-7 and MMP-26), and membrane-type matrix metalloproteinase-1 (MT1-MMP).
The fourth group comprises stromelysins: MMP-3
(stromelysin 1), MMP-10 (stromelysin 2) and MMP-11 (stromelysin 3).
Celastrol is also an inhibitor of Hsp90[beta] to significantly downregulate the expression of MMP-1, MMP-3
, MMP-13, iNOS-2, and COX-2 induced by IL-1[beta] .
They found that MMP-1, MMP-2, MMP-3
, and TIMP2 were expressed in the filtering areas.
In order to determine whether a mixture of undefined DAMPs released from mechanically injured cartilage was able to evoke MMP-3
secretion from chondrocytes, culture media containing substance diffused from mechanically impacted cartilage at 24 hr postinjury were collected and then applied to chondrocyte monolayer cultures and the expression of MMP-3
was examined after 24 hrs of incubation.
Levels of dermal expression of MMP-3
, MMP-9, and MMP-12 are increased in cutis laxa lesional fibroblasts or lymphocytes and are correlated with the degree of disruption of elastic fibers .
Among these, MMP-1 has been shown to degrade fibrillar collagens while MMP-3
has a wide range of ECM substrates such as nonfibrillar collagens and laminin .
Collagenases (MMP-1, MMP-8, and MMP-13) and stromelysins (MMP-3
, MMP-10, and MMP11) are composed of a catalytic domain and a hemopexin-like domain.