<?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="other" dtd-version="1.2" xml:lang="en"><front><journal-meta><journal-id journal-id-type="publisher-id">Russian Journal of Physiology</journal-id><journal-title-group><journal-title xml:lang="en">Russian Journal of Physiology</journal-title><trans-title-group xml:lang="ru"><trans-title>Российский физиологический журнал им. И.М. Сеченова</trans-title></trans-title-group></journal-title-group><issn publication-format="print">0869-8139</issn><issn publication-format="electronic">2658-655X</issn><publisher><publisher-name xml:lang="en">The Russian Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="publisher-id">651550</article-id><article-id pub-id-type="doi">10.31857/S0869813923070051</article-id><article-id pub-id-type="edn">XMAGUM</article-id><article-categories><subj-group subj-group-type="toc-heading" xml:lang="en"><subject>EXPERIMENTAL ARTICLES</subject></subj-group><subj-group subj-group-type="toc-heading" xml:lang="ru"><subject>ЭКСПЕРИМЕНТАЛЬНЫЕ СТАТЬИ</subject></subj-group><subj-group subj-group-type="article-type"><subject></subject></subj-group></article-categories><title-group><article-title xml:lang="en">Reaction of Kidney Medullary Laminin to Prolonged Dehydration of Rats</article-title><trans-title-group xml:lang="ru"><trans-title>Реакция ламинина мозгового вещества почки на продолжительную дегидратацию крыс</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author"><name-alternatives><name xml:lang="en"><surname>Khegay</surname><given-names>I. I.</given-names></name><name xml:lang="ru"><surname>Хегай</surname><given-names>И. И.</given-names></name></name-alternatives><email>khegay@bionet.nsc.ru</email><xref ref-type="aff" rid="aff1"/></contrib></contrib-group><aff-alternatives id="aff1"><aff><institution xml:lang="en">Federal Research Center Institute of Cytology and Genetics,
Siberian Branch of Russian Academy of Sciences</institution></aff><aff><institution xml:lang="ru">Федеральный исследовательский центр Институт цитологии и генетики Сибирского отделения Российской академии наук</institution></aff></aff-alternatives><pub-date date-type="pub" iso-8601-date="2023-07-01" publication-format="electronic"><day>01</day><month>07</month><year>2023</year></pub-date><volume>109</volume><issue>7</issue><fpage>946</fpage><lpage>953</lpage><history><date date-type="received" iso-8601-date="2025-02-01"><day>01</day><month>02</month><year>2025</year></date></history><permissions><copyright-statement xml:lang="en">Copyright ©; 2023, И.И. Хегай</copyright-statement><copyright-statement xml:lang="ru">Copyright ©; 2023, И.И. Хегай</copyright-statement><copyright-year>2023</copyright-year><copyright-holder xml:lang="en">И.И. Хегай</copyright-holder><copyright-holder xml:lang="ru">И.И. Хегай</copyright-holder></permissions><self-uri xlink:href="https://journals.eco-vector.com/0869-8139/article/view/651550">https://journals.eco-vector.com/0869-8139/article/view/651550</self-uri><abstract xml:lang="en"><p id="idm45181325438192">Laminin is the main water-soluble protein in the basement membrane of epithelial tissue. The content of laminin in the renal parenchyma was studied in rats that were on an alternative water diet for 60 h with excessive water intake or a complete lack of drinking water in the food. It has been shown that the osmotic concentration of urine, which develops as a result of water deprivation, is accompanied by a quantitative change in the composition of laminin. It has been established that the amount of laminin beta chain increases in the kidney medulla of dehydrated rats. This effect is observed only in WAG rats with normally expressed vasopressin gene and is absent in mutant Brattleboro rats unable to synthesize the hormone. The increase in the level of beta-laminin also does not extend to the cortical substance. Based on the original and new data, it is assumed that laminin, as a key regulatory element in the basement membrane of the tubular epithelium, participates in the adaptive reaction of the concentrating system of the kidney to conditions of prolonged dehydration. Hyperhydration does not affect the level of laminin in the renal parenchyma.</p></abstract><trans-abstract xml:lang="ru"><p id="idm45181325436208">Ламинин является основным водорастворимым белком базальной мембраны эпителиальной ткани. Исследовано содержание ламинина в почечной паренхиме у крыс, находившихся в течение 60 ч на альтернативной водной диете с избыточным потреблением воды либо полным отсутствием питьевой воды в пище. Показано, что осмотическое концентрирование мочи, развивающееся вследствие водной депривации, сопровождается количественным изменением состава ламинина. Установлено, что в мозговом веществе почки дегидратированных крыс возрастает количество бета-цепи ламинина. Данный эффект наблюдается только у крыс линии WAG с нормально экспрессирующимся геном вазопрессина и отсутствует у мутантных крыс линии Brattleboro, неспособных синтезировать гормон. Повышение уровня бета-ламинина также не распространяется на корковое вещество. На основании исходных и новых данных предполагается, что ламинин как ключевой регуляторный элемент в составе базальной мембраны канальцевого эпителия участвует в адаптивной реакции концентрирующей системы почки к условиям продолжительной дегидратации. Гипергидратация не влияет на уровень ламинина в почечной паренхиме.</p></trans-abstract><kwd-group xml:lang="en"><kwd>WAG</kwd><kwd>Brattleboro</kwd><kwd>dehydration</kwd><kwd>kidney</kwd><kwd>medulla</kwd><kwd>osmotic concentration</kwd><kwd>laminin</kwd><kwd>beta peptide</kwd><kwd>vasopressin</kwd></kwd-group><kwd-group xml:lang="ru"><kwd>WAG</kwd><kwd>Brattleboro</kwd><kwd>дегидратация</kwd><kwd>почка</kwd><kwd>мозговое вещество</kwd><kwd>осмотическое концентрирование</kwd><kwd>ламинин</kwd><kwd>бета-пептид</kwd><kwd>вазопрессин</kwd></kwd-group></article-meta></front><body></body><back><ref-list><ref id="B1"><label>1.</label><mixed-citation>Yurchenco PD, Cheng YS (1993) Self-assembly and calcium-binding sites in laminin. A three-arm interaction model. J Biol Chem 268(23): 17286–17299. https://doi.org/10.1016/S0021-9258(19)85334-6</mixed-citation></ref><ref id="B2"><label>2.</label><mixed-citation>MakKiM, Rena M (2017) Basement Membrane Type IV Collagen and Laminin: An Overview of Their Biology and Value as Fibrosis Biomarkers of Liver Disease. The Anatom Record 300(8): 1371–1390. https://doi.org/10.1002/ar.23567</mixed-citation></ref><ref id="B3"><label>3.</label><mixed-citation>Yamada M, Sekiguchi K (2015) Molecular Basis of Laminin-Integrin Interactions. Curr Top Membr 76: 197–229. https://doi.org/10.1016/bs.ctm.2015.07.002</mixed-citation></ref><ref id="B4"><label>4.</label><mixed-citation>Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, Engel J, Engvall E, Hohenester E, Jones JCR, Kleinman HK, Marinkovich MP, Martin GR, Mayer U, Meneguzzi G, Miner JH, Miyazaki K, Manuel M, Paulsson M, Quaranta V, Sanes JR, Sasaki T, Sekiguchi K, Sorokin LM, Talts JF, Tryggvason K, Uitto J, Virtanen I, von der Mark K, Wewer UM, Yamada Y, Yurchenco PD (2005) A simplified laminin nomenclature. Matrix Biol 24(5): 326–332. https://doi.org/10.1016/j.matbio.2005.05.006</mixed-citation></ref><ref id="B5"><label>5.</label><mixed-citation>Walter V, DeGraff DJ, Yamashita H (2022) Characterization of laminin-332 gene expression in molecular subtypes of human bladder cancer. Am J Clin Exp Urol 10(5): 311–319. eCollection 2022.</mixed-citation></ref><ref id="B6"><label>6.</label><mixed-citation>Aumailley M (2013) The laminin family. Cell AdhMigr 7(1): 48–55. https://doi.org/10.4161/cam.22826</mixed-citation></ref><ref id="B7"><label>7.</label><mixed-citation>Rousselle P, Beck K (2013) Laminin 332 processing impacts cellular behavior. Cell Adh Migr 7(1): 122–134. https://doi.org/10.4161/cam.23132</mixed-citation></ref><ref id="B8"><label>8.</label><mixed-citation>Khegay II, Ivanova LN (2015) Regression of Walker 256 carcinosarcoma in vasopressin-deficient Brattleboro rats is accompanied by a changed laminin pattern. Biochem Genet 53(1–3): 1–7. https://doi.org/10.1007/s10528-015-9665-1</mixed-citation></ref><ref id="B9"><label>9.</label><mixed-citation>Bekkevold CM, Robertson KL, Reinhard MK, Battles AH, Neil E Rowland NE (2013) Dehydration Parameters and Standards for Laboratory Mice. J Am Assoc Lab Anim Sci 52(3): 233–239.</mixed-citation></ref><ref id="B10"><label>10.</label><mixed-citation>Smit WM, Ruyter JH, van Wijk HF (1960) A new cryoscopic micro-method for the determination of molecular weights. Analyt Chim Acta 22: 8–16. https://doi.org/10.1016/S0003-2670(00)88232-X</mixed-citation></ref><ref id="B11"><label>11.</label><mixed-citation>Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227(5259): 680–685. https://doi.org/10.1038/227680a0</mixed-citation></ref><ref id="B12"><label>12.</label><mixed-citation>Sasaki T, Takagi J, Giudici C, Yamada Y, Arikawa-Hirasawa E, Deutzmann R, Timpl R, Sonnenberg A, Bächinger HP, Tonge D (2010) Laminin-121–recombinant expression and interactions with integrins. Matrix Biol 29(6): 484–493. https://doi.org/10.1016/j.matbio.2010.05.004</mixed-citation></ref><ref id="B13"><label>13.</label><mixed-citation>Koshikawa N, Minegishi T, Sharabi A, Quaranta V, Seiki M (2005) Membrane-type matrix metalloproteinase-1 (MT1-MMP) is a processing enzyme for human laminin gamma 2 chain. J Biol Chem 280(1): 88–93. https://doi.org/10.1074/jbc.M411824200</mixed-citation></ref><ref id="B14"><label>14.</label><mixed-citation>Смирнов АВ, Наточин ЮВ (2019) Нефрология: фундаментальная и клиническая. Нефрология 23 (4): 9-26. [Smirnov AV, Natochin YuV (2019) Nephrology: fundamental and clinical. Nephrology (Saint-Petersburg) 23 (4): 9–26. (In Russ)]. https://doi.org/10.24884/1561-6274-2019-23-4-9-26</mixed-citation></ref><ref id="B15"><label>15.</label><mixed-citation>Nony PA, Schnellmann RG (2003) Mechanisms of renal cell repair and regeneration after acute renal failure. J Pharmacol Exp Ther 304(3): 905–912. https://doi.org/10.1124/jpet.102.035022</mixed-citation></ref><ref id="B16"><label>16.</label><mixed-citation>Givant-Horwitz V, Davidson B, Reich R (2005) Laminin-induced signaling in tumor cells. Cancer Lett 223(1): 1–10. https://doi.org/10.1016/j.canlet.2004.08.030</mixed-citation></ref><ref id="B17"><label>17.</label><mixed-citation>Phan H-P, Sugino M, Niimi T (2009) The production of recombinant human laminin-332 in a Leishmania tarentolae expression system. Protein Expres Purificat 68(1): 79–84. https://doi.org/10.1016/j.pep.2009.07.005</mixed-citation></ref><ref id="B18"><label>18.</label><mixed-citation>Colognato H, Yurchenco PD (2000) Form and function: the laminin family of heterotrimers. Dev Dyn 218(2): 213–234. https://doi.org/10.1002/(SICI)1097-0177(200006)218:2 &lt;213::AID-DVDY1&gt;3.0.CO;2-R</mixed-citation></ref><ref id="B19"><label>19.</label><mixed-citation>Wade CE, Keil LC, Ramsay DJ (1983) Role of Volume and Osmolality in the Control of Plasma Vasopressin in Dehydrated Dogs. Neuroendocrinology 37(5): 349–353. https://doi.org/10.1159/000123574</mixed-citation></ref><ref id="B20"><label>20.</label><mixed-citation>Bouby N, Fernandes S (2003) Mild dehydration, vasopressin and the kidney: animal and human studies Eur J Clin Nutr 57(Suppl 2): S39-S46. https://doi.org/10.1038/sj.ejcn.1601900</mixed-citation></ref><ref id="B21"><label>21.</label><mixed-citation>Bankir L, Bouby N, Ritz E (2013) Vasopressin: a novel target for the prevention and retardation of kidney disease? Nat Rev Nephrol 9(4): 223–239. https://doi.org/10.1038/nrneph.2013.22</mixed-citation></ref><ref id="B22"><label>22.</label><mixed-citation>Phillips PA, Abrahams JM, Kelly JM, Mooser V, Trinder D, Johnston CI (1990)Localization of vasopressin binding sites in rat tissues using specific V1 and V2 selective ligands. Endocrinology 126(3): 1478–1484. https://doi.org/10.1210/endo-126-3-1478</mixed-citation></ref><ref id="B23"><label>23.</label><mixed-citation>Holmes CL, Landry DW, Granton JT (2003) Science review: Vasopressin and the cardiovascular system part 1–receptor physiology. Crit Care 7(6): 427–434. https://doi.org/10.1186/cc2337</mixed-citation></ref><ref id="B24"><label>24.</label><mixed-citation>Kaufmann JE, Oksche A, Wollheim CB, Gunther G, Rosenthal W, Vischer UM (2000) Vasopressin-induced von Willebrand factor secretion from endothelial cells involves V2 receptors and cAMP. J Clin Invest 106(1): 107–116. https://doi.org/1010.1172/JCI9516</mixed-citation></ref><ref id="B25"><label>25.</label><mixed-citation>Gordon AC, Russell JA, Walley KR, Singer J, Ayers D, Storms MM, Holmes CL, Hébert PC, Cooper DJ, Mehta S, Granton JT, Cook DJ, Jeffrey J, Presneill JJ (2010) The effects of vasopressin on acute kidney injury in septic shock. Intens Care Med 36(1): 83–91.https://doi.org/10.1007/s00134-009-1687-x</mixed-citation></ref></ref-list></back></article>
