<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE root>
<article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:ali="http://www.niso.org/schemas/ali/1.0/" article-type="review-article" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Annals of the Russian academy of medical sciences</journal-id><journal-title-group><journal-title xml:lang="en">Annals of the Russian academy of medical sciences</journal-title><trans-title-group xml:lang="ru"><trans-title>Вестник Российской академии медицинских наук</trans-title></trans-title-group></journal-title-group><issn publication-format="print">0869-6047</issn><issn publication-format="electronic">2414-3545</issn><publisher><publisher-name xml:lang="en">"Paediatrician" Publishers LLC</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">1396</article-id><article-id pub-id-type="doi">10.15690/vramn1396</article-id><article-categories><subj-group subj-group-type="toc-heading" xml:lang="en"><subject>ENDOCRINOLOGY: CURRENT ISSUES</subject></subj-group><subj-group subj-group-type="toc-heading" xml:lang="ru"><subject>АКТУАЛЬНЫЕ ВОПРОСЫ ЭНДОКРИНОЛОГИИ</subject></subj-group><subj-group subj-group-type="article-type"><subject>Review Article</subject></subj-group></article-categories><title-group><article-title xml:lang="en">Vitamin D-binding protein: multifunctional component of blood serum</article-title><trans-title-group xml:lang="ru"><trans-title>Витамин D-связывающий белок как многофункциональный компонент сыворотки крови</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-7634-5457</contrib-id><contrib-id contrib-id-type="spin">1970-2811</contrib-id><name-alternatives><name xml:lang="en"><surname>Povaliaeva</surname><given-names>Alexandra A.</given-names></name><name xml:lang="ru"><surname>Поваляева</surname><given-names>Александра Александровна</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><email>a.petrushkina@yandex.ru</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0001-6539-466X</contrib-id><contrib-id contrib-id-type="spin">6912-6331</contrib-id><name-alternatives><name xml:lang="en"><surname>Pigarova</surname><given-names>Ekaterina A.</given-names></name><name xml:lang="ru"><surname>Пигарова</surname><given-names>Екатерина Александровна</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p>MD, PhD</p></bio><bio xml:lang="ru"><p>д.м.н.</p></bio><email>kpigarova@gmail.com</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0001-7112-5896</contrib-id><contrib-id contrib-id-type="spin">3959-5866</contrib-id><name-alternatives><name xml:lang="en"><surname>Romanova</surname><given-names>Anastasia A.</given-names></name><name xml:lang="ru"><surname>Романова</surname><given-names>Анастасия Александровна</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p>MD</p></bio><email>svetasvetikova1535@gmail.com</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-0327-4619</contrib-id><contrib-id contrib-id-type="spin">2958-5555</contrib-id><name-alternatives><name xml:lang="en"><surname>Dzeranova</surname><given-names>Larisa K.</given-names></name><name xml:lang="ru"><surname>Дзеранова</surname><given-names>Лариса Константиновна</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p>MD, PhD</p></bio><bio xml:lang="ru"><p>д.м.н.</p></bio><email>dzeranovalk@yandex.ru</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-2729-9386</contrib-id><contrib-id contrib-id-type="spin">8513-7785</contrib-id><name-alternatives><name xml:lang="en"><surname>Zhukov</surname><given-names>Artem Y.</given-names></name><name xml:lang="ru"><surname>Жуков</surname><given-names>Артем Юрьевич</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p>MD</p></bio><email>zhukovartem@yahoo.com</email><xref ref-type="aff" rid="aff1"/></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0001-7041-0732</contrib-id><contrib-id contrib-id-type="spin">5691-7775</contrib-id><name-alternatives><name xml:lang="en"><surname>Rozhinskaya</surname><given-names>Liudmila Y.</given-names></name><name xml:lang="ru"><surname>Рожинская</surname><given-names>Людмила Яковлевна</given-names></name></name-alternatives><address><country country="RU">Russian Federation</country></address><bio xml:lang="en"><p>MD, PhD, Professor</p></bio><bio xml:lang="ru"><p>д.м.н., профессор</p></bio><email>lrozhinskaya@gmail.com</email><xref ref-type="aff" rid="aff1"/></contrib></contrib-group><aff-alternatives id="aff1"><aff><institution xml:lang="en">Endocrinology Research Centre</institution></aff><aff><institution xml:lang="ru">Национальный медицинский исследовательский центр эндокринологии</institution></aff></aff-alternatives><pub-date date-type="pub" iso-8601-date="2021-04-12" publication-format="electronic"><day>12</day><month>04</month><year>2021</year></pub-date><volume>76</volume><issue>1</issue><issue-title xml:lang="en"/><issue-title xml:lang="ru"/><fpage>103</fpage><lpage>110</lpage><history><date date-type="received" iso-8601-date="2020-07-13"><day>13</day><month>07</month><year>2020</year></date><date date-type="accepted" iso-8601-date="2021-02-16"><day>16</day><month>02</month><year>2021</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2021, "Paediatrician" Publishers LLC</copyright-statement><copyright-statement xml:lang="ru">Copyright ©; 2021, Издательство "Педиатръ"</copyright-statement><copyright-year>2021</copyright-year><copyright-holder xml:lang="en">"Paediatrician" Publishers LLC</copyright-holder><copyright-holder xml:lang="ru">Издательство "Педиатръ"</copyright-holder><ali:free_to_read xmlns:ali="http://www.niso.org/schemas/ali/1.0/" start_date="2022-04-12"/></permissions><self-uri xlink:href="https://vestnikramn.spr-journal.ru/jour/article/view/1396">https://vestnikramn.spr-journal.ru/jour/article/view/1396</self-uri><abstract xml:lang="en"><p>Vitamin D-binding protein (DBP) was discovered more than half a century ago as a polymorphic serum protein and is currently characterized by a variety of physiological properties. First of all, DBP carries the bulk of vitamin D metabolites circulating in the bloodstream, while albumin is the second most important transport protein, especially in patients with a low concentration of DBP in serum. Since it was discovered that only 1–2% of the total circulating DBP have occupied steroid binding sites, a vigorous study of other potential biological roles of DBP was initiated: actin utilization, regulation of inflammation and innate immunity mechanisms, fatty acid binding, effects on bone metabolism and participation in the tumor pathogenesis. This review focuses on the main known biological functions of DBP.</p></abstract><trans-abstract xml:lang="ru"><p>Витамин D-связывающий белок (DBP) был открыт более полувека назад в качестве полиморфного белка сыворотки крови и к настоящему моменту характеризуется многообразием физиологических свойств. Прежде всего, DBP переносит основную часть циркулирующих в кровотоке метаболитов витамина D, тогда как альбумин является вторым по значимости транспортным белком, особенно у пациентов с низкой концентрацией DBP в сыворотке. Поскольку было открыто, что сайты связывания стероидов заняты лишь у 1–2% от общего количества циркулирующего DBP, инициировано активное изучение других потенциальных биологических ролей этого белка: утилизация актина, регуляция процессов воспаления и механизмов врожденного иммунитета, связывание жирных кислот, влияние на метаболизм костной ткани и связь с патогенезом опухолевых заболеваний. Данный обзор посвящен рассмотрению основных известных биологических функций DBP.</p></trans-abstract><kwd-group xml:lang="en"><kwd>vitamin D-binding protein</kwd><kwd>vitamin D</kwd><kwd>carrier proteins</kwd><kwd>inflammation</kwd><kwd>chemotaxis</kwd></kwd-group><kwd-group xml:lang="ru"><kwd>витамин D-связывающий белок</kwd><kwd>витамин D</kwd><kwd>транспортные белки</kwd><kwd>воспаление</kwd><kwd>хемотаксис</kwd></kwd-group><funding-group><award-group><funding-source><institution-wrap><institution xml:lang="ru">Российский научный фонд</institution></institution-wrap><institution-wrap><institution xml:lang="en">Russian Science Foundation</institution></institution-wrap></funding-source><award-id>19-15-00243</award-id></award-group></funding-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Bouillon R, van Haelen V, Rombauts W, de Moor P. The purification and characterisation of the human‐serum binding protein for the 25‐hydroxycholecalciferol (transcalciferin) identity with group‐specific component. Eur J Biochem. 1976;66(2):285–291. doi: https://doi.org/10.1111/j.1432-1033.1976.tb10518.x</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>Imawari M, Kida K, Goodman DS. The transport of vitamin D and its 25 hydroxy metabolite in human plasma. Isolation and partial characterization of vitamin D and 25 hydroxyvitamin D binding protein. J Clin Invest. 1976;58(2):514–523. doi: https://doi.org/10.1172/JCI108495</mixed-citation></ref><ref id="B3"><label>3.</label><mixed-citation>Haddad JG, Hillman L, Rojanasathit S. Human serum binding capacity and affinity for 25-hydroxyergocalciferol and 25-hydroxycholecalciferol. J Clin Endocrinol Metab. 1976;43(1):86–91. doi: https://doi.org/10.1210/jcem-43-1-86</mixed-citation></ref><ref id="B4"><label>4.</label><mixed-citation>Song YH, Naumova AK, Liebhaber SA, Cooke NE. Physical and meiotic mapping of the region of human chromosome 4q11-q13 encompassing the vitamin D binding protein DBP/Gc-globulin and albumin multigene cluster. Genome Res. 1999;9(6):581–587.</mixed-citation></ref><ref id="B5"><label>5.</label><mixed-citation>Bikle DD, Schwartz J. Vitamin D binding protein, total and free vitamin D levels in different physiological and pathophysiological conditions. Front Endocrinol (Lausanne). 2019;10:317. doi: https://doi.org/10.3389/fendo.2019.00317</mixed-citation></ref><ref id="B6"><label>6.</label><mixed-citation>Speeckaert M, Huang G, Delanghe JR, Taes YEC. Biological and clinical aspects of the vitamin D binding protein (Gc-globulin) and its polymorphism. Clin Chim Acta. 2006;372(1–2):33–42. doi: https://doi.org/10.1016/j.cca.2006.03.011</mixed-citation></ref><ref id="B7"><label>7.</label><mixed-citation>Delanghe JR, Speeckaert R, Speeckaert MM. Behind the scenes of vitamin D binding protein: More than vitamin D binding. Best Pract Res Clin Endocrinol Metab. 2015;29(5):773–786. doi: https://doi.org/10.1016/j.beem.2015.06.006</mixed-citation></ref><ref id="B8"><label>8.</label><mixed-citation>Song YH, Ray K, Liebhaber SA, Cooke NE. Vitamin D-binding protein gene transcription is regulated by the relative abundance of hepatocyte nuclear factors 1α and 1β. J Biol Chem. 1998;273(43):28408–28418. doi: https://doi.org/10.1074/jbc.273.43.28408</mixed-citation></ref><ref id="B9"><label>9.</label><mixed-citation>Zhang JY, Lucey AJ, Horgan R, et al. Impact of pregnancy on vitamin D status: A longitudinal study. Br J Nutr. 2014;112(7):1081–1087. doi: https://doi.org/10.1017/S0007114514001883</mixed-citation></ref><ref id="B10"><label>10.</label><mixed-citation>Møller UK, Streym S, Jensen LT, et al. Increased plasma concentrations of vitamin D metabolites and vitamin D binding protein in women using hormonal contraceptives: A cross-sectional study. Nutrients. 2013;5(9):3470–3480. doi: https://doi.org/10.3390/nu5093470</mixed-citation></ref><ref id="B11"><label>11.</label><mixed-citation>Nykjaer A, Dragun D, Walther D, et al. An endocytic pathway essential for renal uptake and activation of the steroid 25-(OH) vitamin D3. Cell. 1999;96(4):507–515. doi: https://doi.org/10.1016/s0092-8674(00)80655-8</mixed-citation></ref><ref id="B12"><label>12.</label><mixed-citation>Guha C, Osawa M, Werner PA, et al. Regulation of human Gc (vitamin D-binding) protein levels: Hormonal and cytokine control of gene expression in vitro. Hepatology. 1995;21(6):1675–1681.</mixed-citation></ref><ref id="B13"><label>13.</label><mixed-citation>Wang X, Shapses SA, Al-Hraishawi H. Free and bioavailable 25-hydroxyvitamin D levels in patients with primary hyperparathyroidism. Endocr Pract. 2017;23(1):66–71. doi: https://doi.org/10.4158/EP161434.OR</mixed-citation></ref><ref id="B14"><label>14.</label><mixed-citation>Thrailkill KM, Fowlkes JL. The role of vitamin D in the metabolic homeostasis of diabetic bone. Clin Rev Bone Min Metab. 2014;11(1):28–37. doi: https://doi.org/10.1007/s12018-012-9127-9</mixed-citation></ref><ref id="B15"><label>15.</label><mixed-citation>Anderson RL, Ternes SB, Strand KA, Rowling MJ. Vitamin D homeostasis is compromised due to increased urinary excretion of the 25-hydroxycholecalciferol-vitamin D-binding protein complex in the Zucker diabetic fatty rat. Am J Physiol Endocrinol Metab. 2010;299(6):959–967. doi: https://doi.org/10.1152/ajpendo.00218.2010</mixed-citation></ref><ref id="B16"><label>16.</label><mixed-citation>Altinova AE, Ozkan C, Akturk M, et al. Vitamin D-binding protein and free vitamin D concentrations in acromegaly. Endocrine. 2016;52(2):374–379. doi: https://doi.org/10.1007/s12020-015-0789-1</mixed-citation></ref><ref id="B17"><label>17.</label><mixed-citation>Björkhem-Bergman L, Torefalk E, Ekström L, Bergman Pl. Vitamin D binding protein is not affected by high-dose vitamin D supplementation: A post hoc analysis of a randomised, placebo-controlled study. BMC Res Notes. 2018;11(1):619. doi: https://doi.org/10.1186/s13104-018-3725-7</mixed-citation></ref><ref id="B18"><label>18.</label><mixed-citation>Bouillon R, Schuit F, Antonio L, Rastinejad F. Vitamin D binding protein: a historic overview. Front Endocrinol (Lausanne). 2020;10:910. doi: https://doi.org/10.3389/fendo.2019.00910</mixed-citation></ref><ref id="B19"><label>19.</label><mixed-citation>Bouillon R. Genetic and racial differences in the vitamin D Endocrine System. Endocrinol. Metab Clin North Am. 2017;46(4):1119–1135. doi: https://doi.org/10.1016/j.ecl.2017.07.014</mixed-citation></ref><ref id="B20"><label>20.</label><mixed-citation>Haughton MA, Mason RS. Immunonephelometric assay of vitamin D-binding protein. Clin Chem. 1992;38(9):1796–1801.</mixed-citation></ref><ref id="B21"><label>21.</label><mixed-citation>Jørgensen CS, Christiansen M, Nørgaard-Pedersen E, et al. Gc globulin (vitamin D-binding protein) levels: An inhibition ELISA assay for determination of the total concentration of Gc globulin in plasma and serum. Scand J Clin Lab Invest. 2004;64(2):157–166. doi: https://doi.org/10.1080/00365510410001149</mixed-citation></ref><ref id="B22"><label>22.</label><mixed-citation>Henderson CM, Lutsey PL, Misialek JR, et al. Measurement by a novel LC-MS/MS methodology reveals similar serum concentrations of vitamin D binding protein in blacks and whites. Clin Chem. 2017;62(1):179–187. doi: https://doi.org/10.1373/clinchem.2015.244541</mixed-citation></ref><ref id="B23"><label>23.</label><mixed-citation>Kilpatrick LE, Phinney K.W. Quantification of total vitamin-D-binding protein and the glycosylated isoforms by liquid chromatography − isotope dilution mass spectrometry. J Proteome Res. 2017;16(11):4185–4195. doi: https://doi.org/10.1021/acs.jproteome.7b00560</mixed-citation></ref><ref id="B24"><label>24.</label><mixed-citation>Cooke NE, Haddad JG. Vitamin D binding protein (GC-globulin). Endocr. Rev. 1989;10(3):294–307. doi: https://doi.org/10.1210/edrv-10-3-294</mixed-citation></ref><ref id="B25"><label>25.</label><mixed-citation>Duchow EG, Cooke NE, Seeman J, et al. Vitamin D binding protein is required to utilize skin-generated vitamin D. Proc Natl Acad Sci USA. 2019;116(49):24527–24532. doi: https://doi.org/10.1073/pnas.1915442116</mixed-citation></ref><ref id="B26"><label>26.</label><mixed-citation>Bikle DD, Gee E, Halloran B, et al. Assessment of the free fraction of 25-hydroxyvitamin. J Clin Endocrinol Metab. 1986;63(4):954–959. doi: https://doi.org/10.1210/jcem-63-4-954</mixed-citation></ref><ref id="B27"><label>27.</label><mixed-citation>Heureux N, Lindhout E, Swinkels L. A direct assay for measuring free 25-hydroxyvitamin D. J AOAC Int. 2017;100(5):1318–1322. doi: https://doi.org/10.5740/jaoacint.17-0084</mixed-citation></ref><ref id="B28"><label>28.</label><mixed-citation>Nielson CM, Jones KS, Chun RF, et al. Free 25-hydroxyvitamin D: impact of vitamin D binding protein assays on racial-genotypic associations. J Clin Endocrinol Metab. 2016;101(5):2226–2234. doi: https://doi.org/10.1210/jc.2016-1104</mixed-citation></ref><ref id="B29"><label>29.</label><mixed-citation>Nielson CM, Jones KS, Bouillon R, et al. Role of assay type in determining free 25-hydroxyvitamin D levels in diverse populations. N Engl J Med. 2016;374(17):1695–1696. doi: https://doi.org/10.1056/NEJMc1513502</mixed-citation></ref><ref id="B30"><label>30.</label><mixed-citation>Bouillon R, van Assche FA, van Baelen H, et al. Influence of the vitamin D-binding protein on the serum concentration of 1,25-dihydroxyvitamin D3. Significance of the free 1,25-dihydroxyvitamin D3 concentration. J Clin Invest. 1981;67(3):589–596. doi: https://doi.org/10.1172/JCI110072</mixed-citation></ref><ref id="B31"><label>31.</label><mixed-citation>Chun RF, Lauridzen AL, Suon L, et al. Vitamin D-binding protein directs monocyte responses to 25-hydroxy- and 1,25-dihydroxyvitamin D. J Clin Endocrinol Metab. 2010;95(7):3368–3376. doi: https://doi.org/10.1210/jc.2010-0195</mixed-citation></ref><ref id="B32"><label>32.</label><mixed-citation>Zella LA, Shevde NK, Hollis BW, et al. Vitamin D-binding protein influences total circulating levels of 1,25-dihydroxyvitamin D3 but does not directly modulate the bioactive levels of the hormone in vivo. Endocrinology. 2008;149(7):3656–3667. doi: https://doi.org/10.1210/en.2008-0042</mixed-citation></ref><ref id="B33"><label>33.</label><mixed-citation>Chun RF, Peercy BE, Orwol ES, et al. Vitamin D and DBP: The free hormone hypothesis revisited. J Steroid Biochem Mol Biol. 2014;144 (Pt A):132–137. doi: https://doi.org/10.1016/j.jsbmb.2013.09.012</mixed-citation></ref><ref id="B34"><label>34.</label><mixed-citation>Nykjaer A, Fyfe JC, Kozyraki R, et al. Cubilin dysfunction causes abnormal metabolism of the steroid hormone 25(OH) vitamin D3. Proc. Natl. Acad Sci U S A. 2001;98(24):13895–13900. doi: https://doi.org/10.1073/pnas.241516998</mixed-citation></ref><ref id="B35"><label>35.</label><mixed-citation>Leheste JR, Melsen F, Wellner М, et al. Hypocalcemia and osteopathy in mice with kidney-specific megalin gene defect. FASEB J. 2003;17(2):247–249. doi: https://doi.org/10.1096/fj.02-0578fje</mixed-citation></ref><ref id="B36"><label>36.</label><mixed-citation>Safadi FF, Thornton P, Magiera H, et al. Osteopathy and resistance to vitamin D toxicity in mice null for vitamin D binding protein. J Clin Invest. 1999;103(2):239–251. doi: https://doi.org/10.1172/JCI5244</mixed-citation></ref><ref id="B37"><label>37.</label><mixed-citation>Kongsbak M, Von Essen MR, Levring TB, et al. Vitamin D-binding protein controls T cell responses to vitamin D. BMC Immunol. 2014;15:35. doi: https://doi.org/10.1186/s12865-014-0035-2</mixed-citation></ref><ref id="B38"><label>38.</label><mixed-citation>Henderson CM, Fink SL, Bassyouni H, et al. Vitamin D-binding protein deficiency and homozygous deletion of the GC gene. N Engl J Med. 2019;380(12):1150–1157. doi: https://doi.org/10.1056/NEJMoa1807841</mixed-citation></ref><ref id="B39"><label>39.</label><mixed-citation>Dueland S, Nenseter MS, Drevon C. Uptake and degradation of filamentous actin and vitamin D-binding protein in the rat. Biochem J. 1991;274(1):237–241. doi: https://doi.org/10.1042/bj2740237</mixed-citation></ref><ref id="B40"><label>40.</label><mixed-citation>Dahl B, Schiødt FV, Gehrchen PM, et al. Gc-globulin is an acute phase reactant and an indicator of muscle injury after spinal surgery. Inflamm Res. 2001;50(1):39–43.</mixed-citation></ref><ref id="B41"><label>41.</label><mixed-citation>Horváth-szalai Z, Kustán P, Szirmay B, et al. Predictive value of serum gelsolin and Gc globulin in sepsis — a pilot study. Clin Chem Lab Med. 2018;56(8):1373–1382. doi: https://doi.org/10.1515/cclm-2017-0782</mixed-citation></ref><ref id="B42"><label>42.</label><mixed-citation>Gressner OA, Gao C, Siluschek M, et al. Inverse association between serum concentrations of actin-free vitamin D-binding protein and the histopathological extent of fibrogenic liver disease or hepatocellular carcinoma. Eur J Gastroenterol Hepatol. 2009;21(9):990–995. doi: https://doi.org/10.1097/MEG.0b013e3283293769</mixed-citation></ref><ref id="B43"><label>43.</label><mixed-citation>Lind SE, Smith DB, Janmey PA, Stossel TP. Depression of gelsolin levels and detection of gelsolin-actin complexes in plasma of patients with acute lung injury. Am Rev Respir Dis. 1988;138(2):429–434. doi: https://doi.org/10.1164/ajrccm/138.2.429</mixed-citation></ref><ref id="B44"><label>44.</label><mixed-citation>Tannetta DS, Redman CW, Sargent IL. Investigation of the actin scavenging system in pre-eclampsia. Eur J Obstet Gynecol Reprod Biol. 2014;172(100):32–35. doi: https://doi.org/10.1016/j.ejogrb.2013.10.022</mixed-citation></ref><ref id="B45"><label>45.</label><mixed-citation>Behrouz GF, Farzaneh GS, Leila J, et al. Presence of auto-antibody against two placental proteins, annexin A1 and vitamin D binding protein, in sera of women with pre-eclampsia. J Reprod Immunol. 2013;99(1–2):10–16. doi: https://doi.org/10.1016/j.jri.2013.04.007</mixed-citation></ref><ref id="B46"><label>46.</label><mixed-citation>Dinsdale RJ, Hazeldine J, Al Tarrah K, et al. Dysregulation of the actin scavenging system and inhibition of DNase activity following severe thermal injury. Br J Surg. 2020;107(4):391–401. doi: https://doi.org/10.1002/bjs.11310</mixed-citation></ref><ref id="B47"><label>47.</label><mixed-citation>Madden K, Feldman HA, Chun RF, et al. Critically ill children have low vitamin D binding protein, influencing bioavailability of vitamin D. Ann Am Thorac Soc. 2015;12(11):1654–1661. doi: https://doi.org/10.1513/AnnalsATS.201503-160OC</mixed-citation></ref><ref id="B48"><label>48.</label><mixed-citation>Waldron JL, Ashby HL, Cornes MP, et al. Vitamin D: A negative acute phase reactant. J Clin Pathol. 2013;66(7):620–622. doi: https://doi.org/10.1136/jclinpath-2012-201301</mixed-citation></ref><ref id="B49"><label>49.</label><mixed-citation>Wang HH, Cheng BL, Chen QX, et al. Time course of plasma gelsolin concentrations during severe sepsis in critically ill surgical patients. Crit Care. 2008;12(4):R106. doi: https://doi.org/10.1186/cc6988</mixed-citation></ref><ref id="B50"><label>50.</label><mixed-citation>Dahl B, Schiødt FV, Rudolph S, et al. Trauma stimulates the synthesis of Gc-globulin. Intensive Care Med. 2001;27(2):394–399. doi: https://doi.org/10.1007/s001340000837</mixed-citation></ref><ref id="B51"><label>51.</label><mixed-citation>Schiødt FV, Ott P, Bondesen S, Tygstrup N. Reduced serum Gc-globulin concentrations in patients with fulminant hepatic failure: association with multiple organ failure. Crit Care Med. 1997Aug;25(8):1366–1370. doi: https://doi.org/10.1097/00003246-199708000-00025</mixed-citation></ref><ref id="B52"><label>52.</label><mixed-citation>Leaf DE, Waikar SS, Wolf M, et al. Dysregulated mineral metabolism in patients with acute kidney injury and risk of adverse outcomes. Clin Endocrinol (Oxf). 2013;79(4):491–498. doi: https://doi.org/10.1111/cen.12172</mixed-citation></ref><ref id="B53"><label>53.</label><mixed-citation>Swamy N, Ray R. Fatty acid-binding site environments of serum vitamin D-binding protein and albumin are different. Bioorg Chem. 2008;36(3):165–168. doi: https://doi.org/10.1016/j.bioorg.2008.02.002</mixed-citation></ref><ref id="B54"><label>54.</label><mixed-citation>Ena JM, Esteban C, Perez MD, et al. Fatty acids bound to vitamin D-binding protein (DBP) from human and bovine sera. Biochem Int. 1989;19(1):1–7.</mixed-citation></ref><ref id="B55"><label>55.</label><mixed-citation>Bouillon R, Xiang DZ, Convents R, van Baelen H. Polyunsaturated fatty acids decrease the apparent affinity of vitamin D metabolites for human vitamin D-binding protein. J Steroid Biochem Mol Biol. 1992;42(8):855–861. doi: https://doi.org/10.1016/0960-0760(92)90094-y</mixed-citation></ref><ref id="B56"><label>56.</label><mixed-citation>Ravnsborg T, Olsen DT, Thysen AH, et al. The glycosylation and characterization of the candidate Gc macrophage activating factor. Biochim Biophys Acta. 2010;1804(4):909–917. doi: https://doi.org/10.1016/j.bbapap.2009.12.022</mixed-citation></ref><ref id="B57"><label>57.</label><mixed-citation>Borges CR, Rehder DS. Glycan structure of Gc protein-derived macrophage activating factor as revealed by mass spectrometry. Arch Biochem Biophys. 2016;606:167–179. doi: https://doi.org/10.1016/j.abb.2016.08.006</mixed-citation></ref><ref id="B58"><label>58.</label><mixed-citation>Mohamad SB, Nagasawa H, Uto Y, Hori H. Tumor cell alpha-N-acetylgalactosaminidase activity and its involvement in GcMAF-related macrophage activation. Comp Biochem Physiol A Mol Integr Physiol. 2002;132(1):1–8. doi: https://doi.org/10.1016/s1095-6433(01)00522-0</mixed-citation></ref><ref id="B59"><label>59.</label><mixed-citation>Schneider GB, Grecco KJ, Safadi FF, Popoff SN. The anabolic effects of vitamin D-binding protein-macrophage activating factor (DBP-MAF) and a novel small peptide on bone. Crit Rev Eukaryot Gene Expr. 2003;13(2–4):277–284. doi: https://doi.org/10.1615/critreveukaryotgeneexpr.v13.i24.190</mixed-citation></ref><ref id="B60"><label>60.</label><mixed-citation>Saburi E, Saburi A, Ghanei M. Promising role for Gc-MAF in cancer immunotherapy: From bench to bedside. Casp J Intern Med. 2017;8(4):228–238. doi: https://doi.org/10.22088/cjim.8.4.228</mixed-citation></ref><ref id="B61"><label>61.</label><mixed-citation>Yamamoto N, Ushijima N, Koga Y. Immunotherapy of HIV-Infected patients with gc protein-derived macrophage activating factor (GcMAF). J Med Virol. 2009;81(1):16–26. doi: https://doi.org/10.1002/jmv.21376</mixed-citation></ref><ref id="B62"><label>62.</label><mixed-citation>Останин А.А., Кирикович С.С., Долгова Е.В., и др. Тернистый путь макрофаг-активирующего фактора (GcMAF): от открытия к клинической практике // Вавиловский журнал генетики и селекции. — 2019. — Т. 23. — № 5. — С. 624–631. [Ostanin AA, Kirikovich SS, Dolgova EV, et al. A thorny pathway of macrophage activating factor (GcMAF): from bench to bedside. Vavilovskii Zhurnal Genetiki i Selektsii. 2019;23(5):624–631. (In Russ.)] doi: https://doi.org/10.18699/VJ19.535</mixed-citation></ref><ref id="B63"><label>63.</label><mixed-citation>Yamamoto N, Naraparaju VR, Urade M. Prognostic utility of serum α-N-acetylgalactosaminidase and immunosuppression resulted from deglycosylation of serum Gc protein in oral cancer patients. Cancer Res. 1997;57(2):295–299.</mixed-citation></ref><ref id="B64"><label>64.</label><mixed-citation>Yamamoto N, Naraparaju VR. Vitamin D3-binding protein as a precursor for macrophage activating factor in the inflammation-primed macrophage activation cascade in rats. Cell Immunol. 1996;170(2):161–167. doi: https://doi.org/10.1006/cimm.1996.0148</mixed-citation></ref><ref id="B65"><label>65.</label><mixed-citation>Safety Study of EF-022 (Modified vitamin D binding protein macrophage activator) in subjects with advanced solid tumors [Internet]. ClinicalTrials.gov: National Library of Medicine (US) [updated 2017 Jun 20; cited 2020 Jul 11]. Available from: https://clinicaltrials.gov/ct2/show/NCT02052492?term=NCT02052492&amp;draw=2&amp;rank=1</mixed-citation></ref><ref id="B66"><label>66.</label><mixed-citation>McVoy LA, Kew RR. CD44 and annexin A2 mediate the C5a chemotactic cofactor function of the vitamin D binding protein. J Immunol. 2005;175(7):4754–4760. doi: https://doi.org/10.4049/jimmunol.175.7.4754</mixed-citation></ref><ref id="B67"><label>67.</label><mixed-citation>Trujillo G, Zhang J, Habiel DM, et al. Cofactor regulation of C5a chemotactic activity in physiological fluids. Requirement for the vitamin D binding protein, thrombospondin-1 and its receptors. Mol Immunol. 2011;49(3):495–503. doi: https://doi.org/10.1016/j.molimm.2011.09.024</mixed-citation></ref><ref id="B68"><label>68.</label><mixed-citation>Binder R, Kress A, Kan G, et al. Neutrophil priming by cytokines and vitamin D binding protein (Gc-globulin): Impact on C5a-mediated chemotaxis, degranulation and respiratory burst. Mol Immunol. 1999;36(13–14):885–892. doi: https://doi.org/10.1016/s0161-5890(99)00110-8</mixed-citation></ref><ref id="B69"><label>69.</label><mixed-citation>Trujillo G, Habiel DM, Ge L, et al. Neutrophil recruitment to the lung in both C5a- and CXCL1-induced alveolitis is impaired in vitamin D-binding protein deficient-mice. J Immunol. 2013;191(2):848–856. doi: https://doi.org/10.4049/jimmunol.1202941</mixed-citation></ref><ref id="B70"><label>70.</label><mixed-citation>Shah AB, DiMartino SJ, Trujillo G, Kew RR. Selective inhibition of the C5a chemotactic cofactor function of the vitamin D binding protein by 1,25(OH)2 Vitamin D3. Mol Immunol. 2006;43(8):1109–1115. doi: https://doi.org/10.1016/j.molimm.2005.07.023</mixed-citation></ref><ref id="B71"><label>71.</label><mixed-citation>Raymond MA, Désormeaux A, Labelle A, et al. Endothelial stress induces the release of vitamin D-binding protein, a novel growth factor. Biochem Biophys Res Commun. 2005;338(3):1374–1382. doi: https://doi.org/10.1016/j.bbrc.2005.10.105.</mixed-citation></ref></ref-list></back></article>
