Biological Activities of Heparan Sulfate

Muthuvel, A.; Sadhasivam, Giji

doi:10.1016/b978-0-12-800269-8.00008-7

Cited by 3 publications

(2 citation statements)

References 22 publications

(18 reference statements)

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“…In addition, that could inhibit in vitro FXa (IC50 0.835 g/mL) and thrombin (IC50 9.3 g mL/L) in the presence of antithrombin and in vivo formation of thrombus in photochemically injured arteries [ 51 ]. In the case of heparin sulfate isolated from different mollusks species Tridacna maxima and Perna viridis , it has demonstrated low anticoagulant activity, 7.4 USP units/mg and 4.3 USP units/mg, respectively, but with higher yields of 20,128 USP units/kg and 9460 USP units/kg respectively [ 52 ]. However, the clam Tapes philippinarum had not only a higher heparin yield and anticoagulant activity, but had identical antithrombin III (ATIII) binding sites, similar to that of human, porcine, and bovine intestinal mucosal heparins [ 53 ].…”

Section: Sulfated Polysaccharidesmentioning

confidence: 99%

Marine Biological Macromolecules and Chemically Modified Macromolecules; Potential Anticoagulants

et al. 2022

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Coagulation is a potential defense mechanism that involves activating a series of zymogens to convert soluble fibrinogen to insoluble fibrin clots to prevent bleeding and hemorrhagic complications. To prevent the extra formation and diffusion of clots, the counterbalance inhibitory mechanism is activated at levels of the coagulation pathway. Contrariwise, this system can evade normal control due to either inherited or acquired defects or aging which leads to unusual clots formation. The abnormal formations and deposition of excess fibrin trigger serious arterial and cardiovascular diseases. Although heparin and heparin-based anticoagulants are a widely prescribed class of anticoagulants, the clinical use of heparin has limitations due to the unpredictable anticoagulation, risk of bleeding, and other complications. Hence, significant interest has been established over the years to investigate alternative therapeutic anticoagulants from natural sources, especially from marine sources with good safety and potency due to their unique chemical structure and biological activity. This review summarizes the coagulation cascade and potential macromolecular anticoagulants derived from marine flora and fauna.

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Section: Sulfated Polysaccharidesmentioning

confidence: 99%

Marine Biological Macromolecules and Chemically Modified Macromolecules; Potential Anticoagulants

et al. 2022

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“…Marine bioactive compounds have great potential in the treatment of thrombosis, which attracts much attention. Many studies have reported that marine heparin exhibit pretty good coagulation such as derive from Tridacna maxima and Perna viridis ( Arumugam and Giji, 2014 ), crabs ( Andrade et al, 2013 ), shrimp head ( Chen, 2021 ). Beyond that, ascidian heparin showed stronger antithrombotic activity than mammalian heparin in arterial animal models, its bleeding effect is lower ( Santos et al, 2007 ).…”

Section: Introductionmentioning

confidence: 99%

A natural heparinoid from mollusc Meretrix lusoria: Purification, structural characterization, and antithrombotic evaluation

Chen

Du²,

Song³

et al. 2022

Current Research in Food Science

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Role of duck plague virus glycoprotein C in viral adsorption: Absence of specific interactions with cell surface heparan sulfate

Jing

Sun

et al. 2017

Journal of Integrative Agriculture

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Many mammalian herpes viruses utilize heparan sulfate (HS) moieties present on cell surface proteoglycans as receptors for cell entry, and this process also requires viral glycoprotein C (gC) homologues. However, our understanding of the role of gC in facilitating attachment of other alpha-herpes viruses such as the duck plague virus (DPV) remains preliminary. To study the role of gC during DPV infection, we used a gC-deleted mutant virus (DPV-ΔgC-EGFP). Examination of the viral copy number by real-time PCR, as well as time course studies of viral adsorption and proliferation revealed that gC was involved in the viral binding to the cell surface. The affinity of viral glycoproteins (gB-DPV, gC-DPV, and gE-DPV) to HS was assessed using a prokaryotic expression system and HiTrap TM Heparin HP column chromatography. In addition, to confirm that gC played a role in the interaction between DPV and HS, viruses were treated with the HS analogue heparin and host cells were treated with its inhibitors heparinase prior to exposure to DPV-ΔgC-EGFP or wild-type strain Chinese virulent duck plague virus (DPV-CHv). The effects of heparin and heparinase on virus infectivity demonstrated that function of gC on viral adsorption is independent of interactions between gC and heparin sulfate on cell surface. All in all, this study demonstrated that the gC of DPV can mediate viral adsorption in an HS-independent manner, which distinguish it from the gC of some other alpha-herpes viruses. Future studies will be required to identify the receptors involved in gC protein binding to cells. This work provides us a foundation for further studies of examining the roles of gC in the adsorption during duck plague virus infection.

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Biological Activities of Heparan Sulfate

Cited by 3 publications

References 22 publications

Marine Biological Macromolecules and Chemically Modified Macromolecules; Potential Anticoagulants

Marine Biological Macromolecules and Chemically Modified Macromolecules; Potential Anticoagulants

A natural heparinoid from mollusc Meretrix lusoria: Purification, structural characterization, and antithrombotic evaluation

Role of duck plague virus glycoprotein C in viral adsorption: Absence of specific interactions with cell surface heparan sulfate

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