aggrecan

Aggrecanase-1 (initial name reflecting its ability to cleave aggrecan)

As part of aggrecan, chondroitin sulfate is a major component of cartilage.

Aggrecan plays an important role in mediating chondrocyte-chondrocyte and chondrocyte-matrix interactions through its ability to bind hyaluronan.

The synthesis and degradation of aggrecan are being investigated for their roles in cartilage deterioration during joint injury, disease, and aging.

Versican has been shown to interact with HAPLN1 and Aggrecan.

Although both proteins can cleave the substrate aggrecan at the same position, they differ in kinetics and in secondary cleavage sites.

Fibulin-1 exhibits calcium-dependent binding to the carboxyl-terminal domain of aggrecan and versican [ 41 ] .

Neurocan, brevican, versican, and aggrecan all share similar N-terminal and C-terminal domains.

Cartilage contains up to 10% proteoglycan consisting of mainly the large aggregating chondroitin sulfate proteoglycan aggrecan.

This function is typical of the large aggregating proteoglycans: aggrecan, versican, brevican, and neurocan, collectively termed the lecticans.

It is responsible for the degradation of aggrecan, a major proteoglycan of cartilage, and brevican, a brain-specific extracellular matrix protein.

TSG-6 also interacts with a plethora of matrix associated molecules, such an aggrecan, versican, thrombospondin (1&2), pentraxin-3 and fibronectin.

Versican belongs to the lectican protein family, with aggrecan (abundant in cartilage), brevican and neurocan (nervous system proteoglycans) as other members.

The CSPGs aggrecan, versican, neurocan, breican, and phosphacan are bound to hyaluronan.

Avocado/soybean unsaponifiables increase aggrecan synthesis and reduce catabolic and proinflammatory mediator production by human osteoarthritic chondrocytes.

PTP-sigma binds with very high affinity to CSPGs, specifically neurocan and aggrecan.

PNNs are composed of brevican, neurocan, versican, aggrecan, phosphacan, hyaluronan, tenascin-R and various link proteins.

Specifically, there is a reduction in the CSPGs aggrecan, versican, and phosphacan and an accumulation of full-length neurocan.

Attached to each aggrecan molecule are the glycosaminoglycan (GAG) chains of chondroitin sulfate and keratan sulfate.

The enzyme encoded by this gene contains two C-terminal TS motifs and functions as aggrecanase to cleave aggrecan, a major proteoglycan of cartilage.

Inhibiting EGFR has been shown to block the activities of certain CSPGs, including neurocan, phosphacan, versican, and aggrecan.

The cleavage of aggrecan and brevican suggests key roles of this enzyme in arthritic disease and in the central nervous system, potentially, in the progression of glioma.

The localized high concentrations of aggrecan provide the osmotic properties necessary for normal tissue function with the GAGs producing the swelling pressure that counters compressive loads on the tissue.

However, CS-E and aggrecan were shown to be the most inhibitory by a large margin, which contained mostly 4,6-sulfated GAG and 4-sulfated GAG, respectively.