Isolation and characterization of chondroitin sulfate proteoglycans from porcine thoracic aorta

1986 ◽  
Vol 883 (1) ◽  
pp. 83-90 ◽  
Author(s):  
Junichiro Aikawa ◽  
Mamoru Isemura ◽  
Hiroshi Munakata ◽  
Noboru Ototani ◽  
Chie Kodama ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Thoracic Aorta ◽  
Chondroitin Sulfate Proteoglycans ◽  
Isolation And Characterization

scholarly journals An affinity chromatography and glycoproteomics workflow to profile the chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in the placenta and in cancer

Glycobiology ◽  
2020 ◽  
Vol 30 (12) ◽  
pp. 989-1002 ◽  
Author(s):  
Alejandro Gómez Toledo ◽  
Jessica Pihl ◽  
Charlotte B Spliid ◽  
Andrea Persson ◽  
Jonas Nilsson ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Affinity Purification ◽  
Chondroitin Sulfate Proteoglycans ◽  
Intervillous Space ◽  
Core Proteins ◽  
Heterogenous Group ◽  
Tumor Tissues ◽  
Infected Cells ◽  
Cancer Tissues

Abstract Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection. Infected cells adhere to syncytiotrophoblasts or get trapped within the intervillous space by binding to a determinant in a 4-O-sulfated CS chains. However, the exact structure of these glycan sequences remains unclear. VAR2CSA-reactive CS is also expressed by tumor cells, making it an attractive target for cancer diagnosis and therapeutics. The identities of the proteoglycans carrying these modifications in placental and cancer tissues remain poorly characterized. This information is clinically relevant since presentation of the glycan chains may be mediated by novel core proteins or by a limited subset of established proteoglycans. To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow. We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins. Additionally, this work demonstrates how affinity purification in combination with glycoproteomics analysis can facilitate the characterization of CSPGs with distinct CS epitopes. A similar workflow can be applied to investigate the interaction of CSPGs with other CS binding lectins as well.

scholarly journals Isolation and characterization of a novel chondroitin sulfate from squid liver integument rich in N-acetylgalactosamine(4,6-disulfate) and glucuronate(3-sulfate) residues

2009 ◽  
Vol 344 (12) ◽  
pp. 1526-1532 ◽  
Author(s):  
Ajaya Kumar Shetty ◽  
Takanari Kobayashi ◽  
Shuji Mizumoto ◽  
Masaki Narumi ◽  
Yoshiaki Kudo ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Isolation And Characterization

scholarly journals Isolation and characterization of monoclonal antibodies specific for chondroitin sulfate E

Glycobiology ◽  
2015 ◽  
Vol 25 (9) ◽  
pp. 953-962 ◽  
Author(s):  
Ippei Watanabe ◽  
Tomoya Hikita ◽  
Haruka Mizuno ◽  
Risa Sekita ◽  
Akira Minami ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Chondroitin Sulfate ◽  
Isolation And Characterization ◽  
Chondroitin Sulfate E

scholarly journals The isolation and characterization of a glycoprotein from human thoracic aorta

1968 ◽  
Vol 109 (5) ◽  
pp. 883-896 ◽  
Author(s):  
M. J. Barnes ◽  
S. M. Partridge
Keyword(s):  
Molecular Weight ◽  
Sialic Acid ◽  
Proteolytic Activity ◽  
Thoracic Aorta ◽  
Deae Cellulose ◽  
Human Aorta ◽  
Isolation And Characterization ◽  
Intimate Association ◽  
Carbohydrate Digestion

1. A glycoprotein extracted by cold alkali from the walls of human aorta was purified by chromatography on DEAE-cellulose. 2. The compound was electrophoretically homogeneous and essentially so by chromatography on DEAE-cellulose. Ultracentrifugal examination revealed two components, and it is suggested that the faster-sedimenting component represents an aggregated form of the glycoprotein. 3. Glycoprotein preparations contained approx. 8% of carbohydrate. Digestion with Pronase yielded a glycopeptide fraction containing all the carbohydrate of the glycoprotein. The glycopeptide, of molecular weight about 7800, contained sialic acid, galactose, mannose, fucose and hexosamine in the approximate molar proportions 5:10:5:2:11. Sialic acid was terminal with respect to the polysaccharide chains. 4. Both elastase and elastomucoproteinases exhibited proteolytic activity towards the glycoprotein. Studies by other investigators have led to the conclusion that elastomucoproteinases attack protein–carbohydrate complexes occurring in intimate association with elastin in aorta and other tissues, and it is suggested that the glycoprotein may be identified with one of these compounds.

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