heparan sulfate

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Related to heparan sulfate: keratan sulfate, dermatan sulfate

hep·a·ran sulfate

A glycosaminoglycan found on cell surfaces and basement membranes in mammals that regulates a wide variety of biological processes, including angiogenesis and blood coagulation. Also called heparitin sulfate.

[hepar(in) (to which it is close in structure) + -an.]
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The large reductions in heparan sulfate in both CSF and urine, significant organ changes and demonstration of neurocognitive benefits represent important findings that support our path to regulatory guidance later this year.
Heparan sulfate (HS) plays a primary role in cell-to-cell communications.
Sanfilippo B, a lysosomal storage disease, is caused by deficiency in the enzyme alpha-N-acetyglucosaminidase (NAGLU), one of the four enzymes required for heparan sulfate degradation.
HSA, she continued, "is an analog of endogenous heparan sulfate, a biologically active glycosaminoglycan (GAG) that has been described as the most information-dense biopolymer in nature due to the multiple functions that can perform such as rebalanced dermal matrix health, deep dermal hydration and modulating the activity of key secreted factors and enzymes.
The testing of urinary samples included an untargeted analysis of low-molecular-mass metabolites using selective reaction monitoring LC-MS/MS with conditions detailed in Tables 2 and 3 and a targeted analysis of selected proteins and heparan sulfate [15-19].
sup][3],[4] Human sulfatase 1 (Hsulf-1) is a recently characterized endosulfatase that selectively removes sulfate groups from heparan sulfate proteoglycans (HSPG), thereby altering the binding sites on HSPG for signaling molecules.
Heparan sulfate proteoglycans of the cardiovascular system.
Heparan sulfate plays a central role in a dynamic in vitro model of protein-losing enteropathy.
One of them is genetic engineering of BMPs to increase binding capacity to the extracellular matrix components such as heparin and heparan sulfate proteoglycans (HSPGs) (8).
Changes in heparan sulfate correlate with increased glomerular permeability.
We also observed a non-metachromatic fraction migrating between dermatan sulfate and the heparan sulfate standard.
The essential conditions found for the transglycosylation reaction are as follows: (38) (i) acceptors are peptides bearing a serine residue, and (ii) acceptable donors are any ChS (Ch, Ch4S and Ch6S), DS or heparan sulfate (HS) that possesses a linkage region, although the order of efficiency is ChS > DS > HS.