TY - JOUR
T1 - Chondroitin sulfate proteoglycans of bovine cornea
T2 - Structural characterization and assessment for the adherence of Plasmodium falciparum-infected erythrocytes
AU - Achur, Rajeshwara N.
AU - Muthusamy, Arivalagan
AU - Madhunapantula, Subbarao V.
AU - Bhavanandan, Veer P.
AU - Seudieu, Clement
AU - Channe Gowda, D.
N1 - Funding Information:
We thank Dr. Larry Fisher, Craniofacial and Skeletal Disease Branch, NIDR, NIH, Bethesda, for providing antidecorin and antibiglycan antisera; Dr. Bruce Stanley, Research Resource Facility, Pennsylvania State University, Hershey; and Professor Keiichi Takagaki, Department of Biochemistry, Hirosaki University School of Medicine, Hirosaki, Japan, for the mass spectral analysis. This work was supported by Public Health Service grant AI-45086 from the National Institute of Allergy and Infectious Diseases, NIH.
PY - 2004/9/1
Y1 - 2004/9/1
N2 - The structures of the bovine corneal chondroitin sulfate (CS) chains and the nature of core proteins to which these chains are attached have not been studied in detail. In this study, we show that structurally diverse CS chains are present in bovine cornea and that they are mainly linked to decorin core protein. DEAE-Sephacel chromatography fractionated the corneal chondroitin sulfate proteoglycans (CSPGs) into three distinct fractions, CSPG-I, CSPG-II, and CSPG-III. These CSPGs markedly differ in their CS and dermatan sulfate (DS) contents, and in particular the CS structure - the overall sulfate content and 4- to 6-sulfate ratio. In general, the CS chains of the corneal CSPGs have low to moderate levels (15-64%) of sulfated disaccharides and 0-30% DS content. Structural analysis indicated that the DS disaccharide units in the CS chains are segregated as large blocks. We have also assessed the suitability of the corneal CSPGs as an alternative to placental CSPG or the widely used bovine tracheal chondroitin sulfate A (CSA) for studying the structural interactions involved in the adherence of Plasmodium falciparum-infected red blood cells (IRBCs) to chondroitin 4-sulfate. The data demonstrate that the corneal CSPGs efficiently bind IRBCs, and that the binding strength is either comparable or significantly higher than the placental CSPG. In contrast, the IRBC binding strength of bovine tracheal CSA is markedly lower than the human placental and bovine corneal CSPGs. Thus, our data demonstrate that the bovine corneal CSPG but not tracheal CSA is suitable for studying structural interactions involved in IRBC-C4S binding.
AB - The structures of the bovine corneal chondroitin sulfate (CS) chains and the nature of core proteins to which these chains are attached have not been studied in detail. In this study, we show that structurally diverse CS chains are present in bovine cornea and that they are mainly linked to decorin core protein. DEAE-Sephacel chromatography fractionated the corneal chondroitin sulfate proteoglycans (CSPGs) into three distinct fractions, CSPG-I, CSPG-II, and CSPG-III. These CSPGs markedly differ in their CS and dermatan sulfate (DS) contents, and in particular the CS structure - the overall sulfate content and 4- to 6-sulfate ratio. In general, the CS chains of the corneal CSPGs have low to moderate levels (15-64%) of sulfated disaccharides and 0-30% DS content. Structural analysis indicated that the DS disaccharide units in the CS chains are segregated as large blocks. We have also assessed the suitability of the corneal CSPGs as an alternative to placental CSPG or the widely used bovine tracheal chondroitin sulfate A (CSA) for studying the structural interactions involved in the adherence of Plasmodium falciparum-infected red blood cells (IRBCs) to chondroitin 4-sulfate. The data demonstrate that the corneal CSPGs efficiently bind IRBCs, and that the binding strength is either comparable or significantly higher than the placental CSPG. In contrast, the IRBC binding strength of bovine tracheal CSA is markedly lower than the human placental and bovine corneal CSPGs. Thus, our data demonstrate that the bovine corneal CSPG but not tracheal CSA is suitable for studying structural interactions involved in IRBC-C4S binding.
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U2 - 10.1016/j.bbapap.2004.06.007
DO - 10.1016/j.bbapap.2004.06.007
M3 - Article
C2 - 15450180
AN - SCOPUS:4344634360
SN - 1570-9639
VL - 1701
SP - 109
EP - 119
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
IS - 1-2
ER -