软骨组织中提取RNA 通过软骨组织中的金属蛋白酶以及其抑

Excess proteolysis of the extracellular matrix (ECM) of articular
cartilage is a key characteristic of arthritis. The main enzymes
involved belong to the metalloproteinase family, specifically the
matrix metalloproteinases (MMPs) and a group of proteinases
with a disintegrin and metalloproteinase domain with
thrombospondin motifs (ADAMTS). Chondrocytes are the only
cell type embedded in the cartilage ECM, and cell-matrix
interactions can influence gene expression and cell behaviour.
Thus, although the use of monolayer cultures can be informative,
it is essential to study chondrocytes encapsulated within their
native environment, cartilage, to fully assess cellular responses.
The aim of this study was to profile the temporal gene
expression of metalloproteinases and their endogenous
inhibitors, the tissue inhibitors of metalloproteinases (TIMPs),
reversion-inducing cysteine-rich protein with Kazal motifs
(RECK), and 2-macroglobulin (2M), in actively resorbing
cartilage. The addition of the pro-inflammatory cytokine
combination of interleukin-1 (IL-1) + oncostatin M (OSM) to
bovine nasal cartilage induces the synthesis and subsequent
activation of pro-metalloproteinases, leading to cartilage
resorption. SPEX6770 全自动冷冻研磨机 SPEX6870 全自动冷冻研磨机 SPEX6970EFM 冷冻研磨机