Sentence examples for most extracellular matrix from inspiring English sources
Integrins, the key component of focal adhesion, are transmembrane receptors that recognize and bind to most extracellular matrix proteins, such as collagens, fibronectin, and laminins [18].
Metalloproteinases (MMP) are zinc-dependent endopeptidases that degrade most extracellular matrix proteins [ 64].
Pericytes are known to synthesize most extracellular matrix protein components [ 61].
A key role in periprosthetic ECM remodeling and destruction belongs to MMPs because of their ability to degrade in concert most extracellular matrix components, such as collagens, gelatin, elastin, laminin, fibronectin, or proteoglycan core proteins.
With the aim of simplifying hepatic fibrogenesis [ 64], hepatic stellate cells (HSCs) in response to damage (hepatocyte death…) and inflammation (TGF β) differentiate into myofibroblast-like cells, which produce most extracellular matrix components.
Most extracellular matrix genes such as members of collagen family, laminins (Lamb2, Lama2), fibulins and microfibrillar associated proteins (Mfap4, Mfap3l, Mfap5) among other proteins were down-regulated from 5 to 14 days.
Fibrillar collagen is the most abundant extracellular matrix (ECM) constituent which maintains the structure of most interstitial tissues and organs, including skin, gut, and breast.
This review summarises the most abundant extracellular matrix components that are used in tissue engineering applications for bone, intervertebral disc, cartilage and tendon.
Collagen is the most abundant extracellular matrix (ECM) protein in the human body, thus widely used in tissue engineering and subsequent clinical applications.
Type I collagen (COL-I) is the most abundant extracellular matrix protein in mammals.
Although most structural extracellular matrix genes were expressed at lower levels in the SRC tumors than in normal cartilage, closer analysis revealed changes in gene expression that were unique to the SRC tumor at each transplantation site.
