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    <ns1:identifier>o:33847</ns1:identifier>
    <ns1:title language="en">Glycosylation and Characterization of Human Transferrin in an End-Stage Kidney Disease</ns1:title>
    <ns2:alt_title language="sr">Glikozilacija i karakterizacija humanog transferina u terminalnoj bubrežnoj insuficijenciji</ns2:alt_title>
    <ns1:language>en</ns1:language>
    <ns1:description language="en">ABSTRACT
Chronic kidney disease (CKD) is a global health concern affecting approximately one billion individuals worldwide. End-stage kidney disease (ESKD), the most severe form of CKD, is often accompanied by anemia. Peritoneal dialysis (PD), a common treatment for ESKD, utilizes the
peritoneum for solute transfer but is associated with complications including protein loss, including
transferrin (Tf) a key protein involved in iron transport. This study investigated Tf characteristics in ESKD patients compared to healthy individuals using lectin microarray, spectroscopic techniques and
immunocytochemical analysis to assess Tf interaction with transferrin receptors (TfRs). ESKD patients exhibited altered Tf glycosylation patterns, evidenced by significant changes in lectin reactivity compared to healthy controls. However, structural analyses revealed no significant differences in the Tf secondary or tertiary structures between the two groups. A functional analysis demonstrated comparable Tf-TfR interaction in both PD and healthy samples. Despite significant alterations in Tf glycosylation, structural integrity and Tf-TfR interaction remained preserved in PD patients. These findings suggest that while glycosylation changes may influence iron metabolism, they do not impair
Tf function. The study highlights the importance of a glucose-free dialysis solutions in managing
anemia exacerbation in PD patients with poorly controlled anemia, potentially offering a targeted therapeutic approach to improve patient outcomes.</ns1:description>
    <ns1:keyword language="en">transferrin; glycosylation; end-stage kidney disease; peritoneal dialysis; structure; lectin microarray; FTIR</ns1:keyword>
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      <ns2:resource>1552099</ns2:resource>
      <ns2:identifier>10.3390/ijms25094625</ns2:identifier>
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    <ns1:upload_date>2024-05-28T09:22:59.140Z</ns1:upload_date>
    <ns1:status>44</ns1:status>
    <ns2:peer_reviewed>yes</ns2:peer_reviewed>
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    <ns12:name_magazine language="en">International Journal of Molecular Sciences</ns12:name_magazine>
    <ns12:volume>25</ns12:volume>
    <ns12:publisher>MDPI</ns12:publisher>
    <ns12:releaseyear>2024</ns12:releaseyear>
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