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doi: 10.15389/agrobiology.2025.2.382eng

UDC: 636.28:619:615.36

 

STRUCTURE AND FUNCTIONAL STATE OF HEMOGLOBIN IN HYPOTROPHIC CALVES (Bos taurus) AS INFLUENCED BY INTERAMIN, A COMPLEX DRUG

S.V. Shabunin, G.A. Vostroilova , P.A. Parshin, V.Yu. Sulin, A.V. Martynova, N.A. Khokhlova, D.I. Shabanov, Yu.S. Parkhomenko, A.A. Veli

All-Russian Research Veterinary Institute of Pathology, Pharmacology and Therapy, 114-b, ul. Lomonosova, Voronezh, 394087 Russia, e-mail vnivipat@mail.ru, gvostroilova@mail.ru ( corresponding author), infovnivipat@mail.ru, sulinvu@mail.ru, marti.alla@mail.ru, nina_xoxlova@mail.ru, am7d@mail.ru, yuliyasp21@mail.ru, aymenayad4@gmail.com

ORCID:
Shabunin S.V. orcid.org/0000-0002-2689-6998
Khokhlova N.A. orcid.org/0000-0001-6861-2554
Vostroilova G.A. orcid.org/0000-0002-2960-038X
Shabanov D.I. orcid.org/0000-0002-1574-1317
Parshin P.A. orcid.org/0000-0002-8790-0540
Parkhomenko Yu.S. orcid.org/0000-0002-1460-5022
Sulin V.Yu. orcid.org/000-0001-9668-6702
Veli A.A. orcid.org/000-0002-9494-1148
Martynova A.V. orcid.org/000-0002-7460-5024

Final revision received April 04, 2024

Accepted June 13, 2024

Correction of morphofunctional immaturity of calves with signs of antenatal hypotrophy and comorbid pathologies remains one of the urgent problems in animal husbandry. Structural and functional changes in hemoglobin (Hb) serve as important diagnostic criteria for the physiological state of an animal during growth. Hypotrophic calves have disorders of metabolic and oxygen transport function of the blood, which can lead to a slowdown in the replacement of fetal hemoglobin (HbF) with definitive hemoglobin (HbA) of adult animals. Correction of such conditions using various drugs and their mechanisms of action continue to be the subject of study. We have revealed for the first time the effect of the preparation Interamin, containing hydrophilic cryofraction of cattle spleen, recombinant species-specific (bovine) alpha- and gamma-interferons (IFN-a and IFN-γ) and vitamins A, E, on the state of the hematopoietic system in hypotrophic calves, which was assessed by the spectral characteristics of hemoglobin in the hemolysate of peripheral blood. Using the Uniprot database, a comparative analysis of aromatic amino acid residues in the primary structure of β- and γ-subunits of Bos taurus hemoglobin was carried out and a difference in the quantitative content of tryptophan in both molecules was established. As a result of the study, changes in the maximum light absorption in the UV range of hemoglobin in hypotrophic calves were established for the first time when using interamin. When interamin was administered subcutaneously to newborn hypotrophic calves at a dose of 1 ml/10 kg of animal weight, a shift in the local maximum of hemoglobin light absorption in the UV range from 270 nm to 275 nm was registered for the first time. Moreover, such a change in local maxima was observed already on the 7th day in hypotrophic calves that began to be administered the complex drug. While the use of the comparison drug Biferon B to hypotrophic calves in the same scheme induced a shift in the local maximum of hemoglobin light absorption only by the 30th day of neonatal development and was not observed by this time in hypotrophic calves without the use of drugs. Based on literature data, hypothetical mechanisms of the observed phenomena are proposed. It is possible that interamin, due to its immunomodulatory effect, accelerates the replacement of fetal hemoglobin with definitive hemoglobin in hypotrophic calves and has a corrective effect on the oxygen-transport function of the blood.

Keywords: hypotrophic calves, fetal hemoglobin, UV absorption spectra, immunomodulation, tissue preparations, recombinant interferons, Interamin, aromatic amino acids.

 

REFERENCES

  1. Shabunin S.V., Alekhin Yu.N., Nezhdanov A.G. Veterinariya, 2015, 1: 3-10 (in Russ.).
  2. Savrasov D.A., Parshin P.A., Vostroilova G.A. Uchenye zapiski Uchrezhdeniya obrazovaniya Vitebskaya ordena «Znak Pocheta» gosudarstvennaya akademiya veterinarnoy meditsiny, 2020, 56(4): 64-68 (in Russ.).
  3. Savrasov D.A., Parshin P.A., Vostroilova G.A. Uchenye zapiski Uchrezhdeniya obrazovaniya Vitebskaya ordena «Znak Pocheta» gosudarstvennaya akademiya veterinarnoy meditsiny, 2020, 56(4): 68-72 (in Russ.).
  4. de Vasconcellos J.F., Tumburu L., Byrnes C., Terry Lee Y., Xu P.C., Li M., Rabel A., Clarke B.A., Guydosh N.R., Proia R.L., Miller J.L. IGF2BP1 over expression causes fetal-like hemoglobin expression patterns in cultured human adult erythroblasts. Proceedings of the National Academy of Sciences of the United States of America, 2017, 114(28): 5664-5672 CrossRef
  5. Baymishev M. Kh. Morfofunktsional’nye osobennosti novorozhdennykh telyat i ikh bolezni [Morphofunctional features of newborn calves and their diseases]. Kinel’, 2016 (in Russ.).
  6. Grimes R.M., Duncan C.W., Lassitter C.A. Bovine fetal hemoglobin. I. Postnatal persistence and relation to adult hemoglobins. Michigan Agricultural Experiment Station, 1958, 2183: 1527-1533 CrossRef
  7. Bauer D.E., Kamran S.C., Orkin, S.H. Reawakening fetal hemoglobin: prospects for new therapies for the β-globin disorders. Blood, 2012, 120(15): 2945-2953 CrossRef
  8. Volkova V.V., Veli A.A., Sulin V.Yu., Martynova A.V., Lavrinenko I.A., Vashanov G.A., Parshin P.A., Vostroilova G.A., Khamdan N. Uchenye zapiski Uchrezhdeniya obrazovaniya Vitebskaya ordena «Znak Pocheta» gosudarstvennaya akademiya veterinarnoy meditsiny, 2020, 56(4): 150-154 (in Russ.).
  9. Alekhin Yu. N., Zhukov M.S., Tyurina E.V., Kashirina L.N. Veterinariya, zootekhniya i biotekhnologiya, 2017, 8: 43-49 (in Russ.).
  10. Novikov V.E., Levchenkova O.S. Obzory po klinicheskoy farmakologii i lekarstvennoy terapii, 2013, 11(2): 8-16 (in Russ.).
  11. Levchenkova O.S., Novikov V.E. Rossiyskiy mediko-biologicheskiy vestnik imeni akademika I.P. Pavlova, 2014, 22(2): 133-143 (in Russ.).
  12. Nikulina D.M., Dyakova O.N., Agapova A., Panova T.N., Kriventcev Y., Bisalieva R., Bachmutova L., Lapeko S., Ogul L., Zaklyakova L., Ivanov P. Diagnostic potential of fetal and embryonic hemoglobins as a markers of hypoxia, fetal development and hemoblastosis. The FEBS Journal, 2013, 280(51): 283.
  13. Levitan B., Skvortsov V., Kasyanova T., Vozniuk M. The diagnostic role of fetal hemoglobin and blood oxygen saturation in chronic liver diseases. Archiv Euromedica, 2021, 11(4): 77-78 CrossRef
  14. Golbeck L., Cohrs I., Scheu T., Grünberg W. Changes of the erythrocyte phenotype and blood biochemistry in dairy calves during the first ten weeks of age. PeerJ, 2019, 7: e7248 CrossRef
  15. Lavrinenko I.A., Vashanov G.A., Ruban M.K. Analysis of the contribution of chromophores in side groups of amino acids to the absorption spectrum of hemoglobin. Journal of Applied Spectroscopy, 2014, 80: 899-904 CrossRef
  16. Smith E.C., Luc S., Croney D.M., Woodworth M.B., Greig L.C., Fujiwara Y., Nguyen M., Sher F., Macklis J.D., Bauer D.E., Orkin S.H. Strict in vivo specificity of the Bcl11a erythroid enhancer. Blood, 2016, 128(19): 2338-2342 CrossRef
  17. Herholz M., Cepeda E., Baumann L., Kukat A., Hermeling J., Maciej S., Szczepanowska K., Pavlenko V., Frommolt P., Trifunovic A. KLF-1 orchestrates a xenobiotic detoxification program essential for longevity of mitochondrial mutants. Nature Communications, 2019, 10: 3323 CrossRef
  18. Xu J., Sankaran V.G., Ni M., Menne T.F., Puram R.V., Kim W., Orkin S.H. Transcriptional silencing of g-globin by BCL11A involves long-range interactions and cooperation with SOX6. Genes & Development, 2010, 24(8): 783-798 CrossRef
  19. Katsumura K.R., DeVilbiss A.W., Pope N.J., Johnson K.D., Bresnick E.H. Transcriptional mechanisms underlying hemoglobin synthesis. Cold Spring Harbor Perspectives in Medicine, 2013, 3(9): a015412 CrossRef
  20. Narayan A.D., Ersek A., Campbell T.A., Colón D.M., Pixley J.S., Zanjani E.D. The effect of hypoxia and stem cell source on haemoglobin switching. British Journal of Haematology, 2005, 128(4): 562-570 CrossRef
  21. Paulson R.F., Ruan B., Hao S., Chen Y. Stress erythropoiesis is a key inflammatory response. Cells, 2020, 9: 634 CrossRef
  22. Perkins A.C., Gaensler K.M., Orkin S.H. Silencing of human fetal globin expression is impaired in the absence of the adult beta-globin gene activator protein EKLF. Proceedings of the National Academy of Sciences of the United States of America, 1996, 93(22): 12267-12271 CrossRef
  23. Tewari R., Gillemans N., Wijgerde M., Nuez B., von Lindern M., Grosveld F., Philipsen S. Erythroid Krüppel-like factor (EKLF) is active in primitive and definitive erythroid cells and is required for the function of 5'HS3 of the beta-globin locus control region. EMBO Journal, 1998, 17(8): 2334-2341 CrossRef
  24. Jeong J.J., Gu X., Nie J., Sundaravel S., Liu H., Kuo W.L., Bhagat T.D., Pradhan K., Cao J., Nischal S., McGraw K.L., Bhattacharyya S., Bishop M.R., Artz A., Thirman M.J., Moliterno A., Ji P., Levine R.L., Godley L.A., Steidl U., Bieker J.J., List A.F., Saunthararajah Y., He C., Verma A., Wickrema A. Cytokine-regulated phosphorylation and activation of TET2 by JAK2 in hematopoiesis. Cancer Discovery, 2019, 9(6): 778-795 CrossRef
  25. Alekhin Yu.N., Lebedeva A.Yu., Zhukov M.S., Morgunova V.I., Kashirina L.N., Sukhanova Yu.E. Eritrocytic parameters of the blood of calves with different birth weights. KnE Life Sciences, 2019, 4(14): 782-791 CrossRef
  26. Manchinu M.F., Brancia C., Caria C.A., Musu E., Porcu S., Simbula M., Asunis I., Perseu L., Ristaldi M.S. Deficiency in interferon type 1 receptor improves definitive erythropoiesis in Klf1 null mice. Cell Death and Differentiation, 2018, 25: 589-599 CrossRef
  27. Farshdousti Hagh M., Dehghani Fard A., Saki N., Shahjahani M., Kaviani S. Molecular mechanisms of hemoglobin F induction. International Journal of Hematology-Oncology and Stem Cell Research, 2011, 1, 5(4): 5-9.
  28. Shakhov A.G., Fedosov D.V., Sashnina L.Y., Yerina T.A. Immune status of the risk group calves within the neonatal period and its correction. Advances in Bioscience and Bioengineering, 2013, 1(2): 54.
  29. Shabunin S.V., Shakhov A.G., Vostroilova G.A., Parshin P.A., Ermolova T.G., Khokhlova N.A., Bliznetsova G.N. Dostizheniya nauki i tekhniki APK, 2019, 33(7): 71-74 CrossRef (in Russ.).
  30. Dehghani Fard A., Kaviani S., Saki N., Mortaz E. The emerging role of immunomodulatory agents in fetal hemoglobin induction. InternationalJournalofHematology-OncologyandStemCellResearch, 2012, 6(4): 35-36.
  31. Mouradian G.C. Jr., Lakshminrusimha S., Konduri G.G. Perinatal hypoxemia and oxygen sensing. Comprehensive Physiology, 2021. 11(2): 1653-1677 CrossRef
  32. Kriventsev Yu.A., Kriventseva L.A. Nauchnoe obozrenie. Meditsinskie nauki, 2018, 1: 16-20 (in Russ.).
  33. Torrejón-Rodríguez L., Parra-Llorca A., Pinilla-González A., Lara-Cantón I., Albiach-Delgado A., Cernada M., Escrig R., Kuligowski J., Aguar Carrascosa M., Vento Torres M. Do lower levels of fetal hemoglobin in preterm infants relate to oxidative stress? Antioxidants and Redox Signaling, 2024, 40(7-9): 453-459 CrossRef
  34. Risso A., Fabbro D., Damante G., Antonutto G. Expression of fetal hemoglobin in adult humans exposed to high altitude hypoxia. Blood Cells, Molecules, and Diseases, 2012, 48(3): 147-153 CrossRef

 

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