Last update 01 Nov 2024

Chondroitin sulfate proteoglycans x GAG

Last update 01 Nov 2024

Basic Info

Related Targets

Chondroitin sulfate proteoglycansGAG

Drugs associated with Chondroitin sulfate proteoglycans x GAG

Condoliase(Seikagaku Corp.)

Target

Chondroitin sulfate proteoglycans x GAG

Mechanism

Chondroitin sulfate proteoglycans modulators [+1]

Active Org.

Seikagaku Corp.

Originator Org.

Seikagaku Corp.

Active Indication

Intervertebral Disc Displacement [+2]

Inactive Indication-

Drug Highest PhaseApproved

First Approval Ctry. / Loc.

First Approval Date23 Mar 2018

Clinical Trials associated with Chondroitin sulfate proteoglycans x GAG

JPRN-jRCT1040220134 / Not yet recruitingNot ApplicableIIT

10 years follow-up study of chemonucleolysis with condoliase after phase III clinical trials (6603/1031) of condoliase for lumbar disc herniation

Start Date01 Mar 2023

Sponsor / Collaborator-

NCT03607838 / CompletedPhase 3

A Multicenter, Randomized, Double-blind, Sham-controlled, Comparative Study of SI-6603 in Subjects With Lumbar Disc Herniation (Phase 3)

This study is to evaluate the effectiveness of a single-dose intervertebral disc injection of SI-6603 in subjects with lumbar disc herniation (LDH)

Start Date30 May 2018

Sponsor / Collaborator

Seikagaku Corp.

EUCTR2014-001449-26-DE / Not yet recruitingPhase 3

A Multicenter, Open-label Study of SI-6603 in Patients with Lumbar Disc Herniation (Phase III)

Start Date01 Sep 2015

Sponsor / Collaborator

Seikagaku Corp.

100 Clinical Results associated with Chondroitin sulfate proteoglycans x GAG

100 Translational Medicine associated with Chondroitin sulfate proteoglycans x GAG

0 Patents (Medical) associated with Chondroitin sulfate proteoglycans x GAG

Literatures (Medical) associated with Chondroitin sulfate proteoglycans x GAG

01 Mar 2022·Enzyme and Microbial Technology

Cloning, expression, and characterization of a glycosaminoglycan lyase from Vibrio sp. H240

Article

Author: Wang, Zheng ; Song, Guanrui ; Gong, Qianhong ; Su, Hai ; Yu, Wengong ; Li, Yunlu ; Sun, Junhao

Glycosaminoglycan lyase is an effective tool for the functional studies of glycosaminoglycans and for the preparation of oligosaccharides. In this study, a new glycosaminoglycan lyase HCLaseV with a molecular weight of 90 kDa was cloned, expressed, and characterized from Vibrio sp. H240. The lyase belonged to the polysaccharide lyase (PL)- 8 family. HCLaseV showed enzyme activities toward chondroitin sulfate A, chondroitin sulfate B, chondroitin sulfate C, and hyaluronic acid. HCLaseV exhibited the highest activity against HA at pH 7.0 and 40 °C. HCLaseV was an endo-type enzyme whose degradation end-product was unsaturated disaccharides. Ca²⁺ inhibited the activity of HCLaseV to a certain extent, which was different from most of the enzymes in the PL-8 family. Mutagenesis studies showed that the Ca²⁺ inhibition might be related to the Asn²⁴⁴ residue. The sequence homology was evaluated by mutagenesis studies, and the catalytic residues in HCLaseV were presumed to be His²⁷⁸, Trp⁴⁸⁵, and Tyr²⁸⁷. These characteristics are helpful for further basic research and application.

01 Nov 2016·Cell ReportsQ1 · BIOLOGY

Retinal Proteoglycans Act as Cellular Receptors for Basement Membrane Assembly to Control Astrocyte Migration and Angiogenesis

Q1 · BIOLOGY

ArticleOA

Author: Zhang, Xin ; Tao, Chenqi

The basement membrane is crucial for cell polarity, adhesion, and motility, but how it is assembled on the cell surface remains unclear. Here, we find that ablation of glycosaminoglycan (GAG) side chains of proteoglycans in the neuroretina disrupts the retinal basement membrane, leading to arrested astrocyte migration and reduced angiogenesis. Using genetic deletion and time-lapse imaging, we show that retinal astrocytes require neuronal-derived PDGF as a chemoattractive cue and the retinal basement membrane as a migratory substrate. Genetic ablation of heparan sulfates does not produce the same defects as GAG null mutants. In contrast, enzymatic removal of heparan sulfates and chondroitin sulfates together inhibits de novo laminin network assembly. These results indicate that both heparan and chondroitin sulfate proteoglycans participate in retinal basement membrane assembly, thus promoting astrocyte migration and angiogenesis.

01 Apr 2006·Journal of VirologyQ2 · MEDICINE

Porcine Circovirus 2 Uses Heparan Sulfate and Chondroitin Sulfate B Glycosaminoglycans as Receptors for Its Attachment to Host Cells

Q2 · MEDICINE

Article

Author: Nauwynck, Hans J. ; Lefebvre, David J. ; Meerts, Peter ; Delputte, Peter L. ; Misinzo, Gerald

ABSTRACTMonocyte/macrophage lineage cells are target cells in vivo for porcine circovirus 2 (PCV2) replication. The porcine monocytic cell line 3D4/31 supports PCV2 replication in vitro, and attachment and internalization kinetics of PCV2 have been established in these cells. However, PCV2 receptors remain unknown. Glycosaminoglycans (GAG) are used by several viruses as receptors. The present study examined the role of GAG in attachment and infection of PCV2. Heparin, heparan sulfate (HS), chondroitin sulfate B (CS-B), but not CS-A, and keratan sulfate reduced PCV2 infection when these GAG were incubated with PCV2 prior to and during inoculation of 3D4/31 cells. Enzymatic removal of HS and CS-B prior to PCV2 inoculation of 3D4/31 cells significantly reduced PCV2 infection. Similarly, when PCV2 virus-like particles (VLP) were allowed to bind onto 3D4/31 cells in the presence of heparin and CS-B, attachment was strongly reduced. Titration of field isolates and low- and high-passage laboratory strains of PCV2 in the presence of heparin significantly reduced PCV2 titers, showing that the capacity of PCV2 to bind GAG was not acquired during in vitro cultivation but is an intrinsic feature of wild-type virus. When Chinese hamster ovary (CHO) cells were inoculated with PCV2, relative percentages of PCV2-infected cells were 27% ± 8% for HS-deficient and 12% ± 10% for GAG-deficient cells compared to wild-type cells (100%). Furthermore, it was shown using heparin-Sepharose chromatography that both PCV2 and PCV2 VLP directly interacted with heparin. Together, these results show that HS and CS-B are attachment receptors for PCV2.

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