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<front>
<journal-meta>
<journal-id journal-id-type="publisher-id">IJMABHR</journal-id>
<journal-title-group><journal-title>International Journal of Medical and All Body Health Research</journal-title><abbrev-journal-title>IJMABHR</abbrev-journal-title></journal-title-group>
<issn pub-type="epub">2582-8940</issn>
<publisher><publisher-name>Anfo Publication House</publisher-name></publisher>
</journal-meta>
<article-meta>
<article-id pub-id-type="publisher-id">347</article-id>
<article-id pub-id-type="doi">10.54660/IJMBHR.2025.6.2.143-151</article-id>
<title-group><article-title>Association of Protein Glycosylation Disorders with Human Diabetes Diseases</article-title></title-group>
<contrib-group>
<contrib contrib-type="author" corresp="yes"><name><surname>Sheet</surname><given-names>Alaa Saeed</given-names></name><xref ref-type="aff" rid="aff1"/></contrib>
<contrib contrib-type="author"><name><surname>Hameed</surname><given-names>Amna Yarub</given-names></name><xref ref-type="aff" rid="aff1"/></contrib>
<aff id="aff1"><label>1</label>Department of Radiology Techniques, Mosul Medical Technical Institute, Northern Technical University, Iraq</aff>
</contrib-group>
<pub-date publication-format="electronic" date-type="pub"><year>2025</year></pub-date>
<volume>6</volume>
<issue>2</issue>
<fpage>143</fpage>
<lpage>151</lpage>
<history>
<date date-type="received"><day>22</day><month>04</month><year>2025</year></date>
<date date-type="accepted"><day>23</day><month>05</month><year>2025</year></date>
</history>
<permissions><license license-type="open-access" xlink:href="https://creativecommons.org/licenses/by-nc-sa/4.0/?utm"><license-p>CC BY-NC-SA 4.0</license-p></license></permissions>
<self-uri xlink:href="https://www.allmedicaljournal.com/article/347/association-of-protein-glycosylation-disorders-with-human-diabetes-diseases"/>
<self-uri content-type="pdf" xlink:href="https://www.allmedicaljournal.com/article/347/download"/>
<abstract><p>Glycosylation is a vital post-translational modification crucial for protein function, folding, and stability. Disorders of protein glycosylation have significant implications for human diseases, including diabetes mellitus. This review explores the biological mechanisms underpinning protein glycosylation, types of glycosylation disorders, and their clinical manifestations, focusing on their association with diabetes. Recent studies demonstrate shared molecular pathways between glycosylation disorders and diabetes pathophysiology, emphasizing oxidative stress, inflammation, and impaired insulin signaling. Understanding these links offers prospects for novel diagnostic strategies and therapeutic interventions. Continuous research into the molecular crosstalk between glycosylation and glucose metabolism is essential for developing precision medicine approaches to manage diabetes and related complications.</p></abstract>
<kwd-group kwd-group-type="author"><kwd>Diabetes</kwd><kwd>Disorders</kwd><kwd>Protein</kwd><kwd>and Pathophysiology</kwd></kwd-group>
</article-meta>
</front>
<back><ref-list><title>References</title>
<ref id="R1"><label>1</label><mixed-citation>Keser T, Gornik I, Vučković F, Selak N, Pavić T, Lukić E, et al. Increased plasma N-glycome complexity is associated with higher risk of type 2 diabetes. Biochim Biophys Acta Gen Subj. 2017;1861(9):2243–51. DOI: 10.1016/j.bbagen.2017.06.020.</mixed-citation></ref>
<ref id="R2"><label>2</label><mixed-citation>Naseri R, Navabi SJ, Samimi Z, Mishra AP, Nigam M, Chandra H, et al. Targeting glycoproteins as a therapeutic strategy for diabetes mellitus and its complications. Daru. 2020;28(2):707–24. DOI: 10.1007/s40199-020-00381-6.</mixed-citation></ref>
<ref id="R3"><label>3</label><mixed-citation>Pasala C, Sharma S, Roychowdhury T, Moroni E, Colombo G, Chiosis G. N-glycosylation as a modulator of protein conformation and assembly in disease. Biomolecules. 2024;14(1):102. DOI: 10.3390/biom14010102.</mixed-citation></ref>
<ref id="R4"><label>4</label><mixed-citation>Sparks SE. Congenital disorders of glycosylation. Adv Pediatr. 2012;59(1):285 –302. DOI: 10.1016/j.yapd.2012.04.003.</mixed-citation></ref>
<ref id="R5"><label>5</label><mixed-citation>Goreta SS, Dabelic S, Dumic J. Insights into complexity of congenital disorders of glycosylation. Biochem Med (Zagreb). 2012;22(2):156–70. DOI: 10.11613/BM.2012.019.</mixed-citation></ref>
<ref id="R6"><label>6</label><mixed-citation>Gümüş E, Özen H. Glycogen storage diseases: An update. World J Clin Pediatr. 2023;12(5):293–308. DOI: 10.5409/wjcp.v12.i5.293.</mixed-citation></ref>
<ref id="R7"><label>7</label><mixed-citation>Andjelkovic M, Skakic A, Ugrin M, Spasovski V, Klaassen K, Pavlovic S, et al. Crosstalk between glycogen-selective autophagy, autophagy and apoptosis as a road towards modifier gene discovery and new therapeutic strategies for glycogen storage diseases. Front Genet. 2022;13:1021028. DOI: 10.3389/fgene.2022.1021028.</mixed-citation></ref>
<ref id="R8"><label>8</label><mixed-citation>Mahjabeen W. Diabetes mellitus and its laboratory diagnosis. J Pak Med Assoc. 2018;68(7):1089–94.</mixed-citation></ref>
<ref id="R9"><label>9</label><mixed-citation>Crist C. Insulin resistance due to obesity. Nat Educ. 2015;8(1):1.</mixed-citation></ref>
<ref id="R10"><label>10</label><mixed-citation>Du C, Whiddett RO, Buckle I, Chen C, Forbes JM, Fotheringham AK. Advanced glycation end products and inflammation in type 1 diabetes development. Cells. 2022;11(21):3503. DOI: 10.3390/cells11213503.</mixed-citation></ref>
<ref id="R11"><label>11</label><mixed-citation>Bolanle IO, Palmer TM. Targeting protein O-GlcNAcylation, a link between type 2 diabetes mellitus and inflammatory disease. Cells. 2022;11(4):704. DOI: 10.3390/cells11040704.</mixed-citation></ref>
<ref id="R12"><label>12</label><mixed-citation>Wada Y. Matrix-assisted laser desorption/ionization mass spectrometry to detect diagnostic glycopeptide markers of congenital disorders of glycosylation. Mass Spectrom (Tokyo) . 2020;9(1):A0084. DOI: 10.5702/massspectrometry.A0084.</mixed-citation></ref>
<ref id="R13"><label>13</label><mixed-citation>Ding Y, Li N, Lou D, Zhang Q, Chang G, Li J, et al. Clinical and genetic analysis in a Chinese cohort of children and adolescents with diabetes/persistent hyperglycemia. Front Endocrinol (Lausanne). 2021;12:653283. DOI: 10.3389/fendo.2021.653283.</mixed-citation></ref>
<ref id="R14"><label>14</label><mixed-citation>Carmichael AG, Hulswit BB, Moe EJ, Jayaratne TE, International Journal of Medical and All Body Health Research www.allmedicaljournal.com Yashar BM. A qualitative study of anticipated decision making around type 2 diabetes genetic testing: the role of scientifically concordant and discordant expectations. J Genet Couns. 2017;26(6):1308–18. DOI: 10.1007/s10897-017-0113-8.</mixed-citation></ref>
<ref id="R15"><label>15</label><mixed-citation>Brasil S, Pascoal C, Francisco R, Marques-da-Silva D, Andreotti G, Videira PA, et al. CDG therapies: From bench to bedside. Int J Mol Sci. 2018;19(5):1304. DOI: 10.3390/ijms19051304.</mixed-citation></ref>
<ref id="R16"><label>16</label><mixed-citation>Sena CM, Bento CF, Pereira P, Marques F, Seiça R. Diabetes mellitus: New challenges and innovative therapies. EPMA J. 2013;4(1):11. DOI: 10.1186/1878-5085-4-11.</mixed-citation></ref>
<ref id="R17"><label>17</label><mixed-citation>Sharma C, Hamza A, Boyle E, Donu D, Cen Y. Post-translational modifications and diabetes. Biomolecules. 2024;14(2):219. DOI: 10.3390/biom14020219.</mixed-citation></ref>
</ref-list></back>
</article>