heparan sulphate

There is also a potential heparan sulphate binding site in the von Willebrand factor A domain.

Most significantly, an interesting similarity to the human basement membrane heparan sulphate proteoglycan core protein was detected.

Alpha-N-acetylglucosaminidase is a lysosomal enzyme required for the stepwise degradation of heparan sulphate.

It is involved in the catabolism of heparin, heparan sulphate, and keratan sulphate.

Other than water, the mesoglea is composed of several substances including fibrous proteins like collagen and heparan sulphate proteoglycans.

Heparan sulphate proteoglycan linked to the cytoskeleton can be copurified with attached nuclei, providing a possible link between matrix-integrin interaction nd nuclear events.

It is found in a number of different proteins that include, heparan sulphate proteoglycan from basement membrane, a laminin-like protein from Caenorhabditis elegans and laminin.

Unless otherwise stated, whenever FGFs were added to culture medium, heparan sulphate (10-100ngml -1 ; Sigma) was also added for protein stabilization.

Heparan sulphate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices.

Fibronectin is an extracellular glycoprotein that can bind to integrins and other ECM components like collagen, fibrin and heparan sulphate proteoglycans(HSPGs).

The presence of heparin and heparan sulphate during the phase of MIP-1 β immobilization substantially inhibited subsequent adhesion induction (Fig. 3 c),suggesting an involvement for GAG-binding.

Hepatocytes may produce heparan sulphate proteoglycans but 'in situ' hybridisation studies suggest the major source of type IV collagen is lipocytes, while laminin is derived predominantly from lpocytes and endothelial cells.

Some anti-dsDNA antibodies are cross reactive with other antigens found on the glomerular basement membrane (GBM) of the kidney, such as heparan sulphate, collagen IV, fibronectin and laminin.

Hence, cleavage of heparan sulphate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena involving cell migration and response to changes in the extracellular microenvironment.

Heparan sulphate proteoglycan, laminin, and collagen have all been shown to be linked across cell membranes to cytoskeletal elements, and cytoskeletal proteins have been demonstrated to be condensed at cell-cell and cell-matrix interfaces.

Control experiments showed that addition of heparan sulphate, alone or in conjunction with other growth factors, BSA alone, or supernatant prepared appropriately from bacterial cells containing only pGEX2T expression vector, had no apparent effect on limb growth.

These include basic fibroblast growth factor (bFGF) which binds to heparan sulphate proteoglycan and can be released by the activity of plasmin which in turn may be activated by matrix bound tissue plasminogen activator (tPA).

Atherosclerotic lesions also show a loss of heparan sulphate proteoglycans - inhibitors of smooth muscle cell proliferation - and an increase in chondroitin sulphate proteoglycan, which retains LDL, thereby inhibiting HDL-mediated cholesterol loss from the vessel wall.