Platelet monoamine oxidase and erythrocyte ATPases as biomarkers of necrotizing enterocolitis


如何引用文章

全文:

开放存取 开放存取
受限制的访问 ##reader.subscriptionAccessGranted##
受限制的访问 订阅或者付费存取

详细

Introduction: The diagnosis of necrotizing enterocolitis (NEC) is complex and often ineffective. Biomarkers reflecting key links in the pathogenesis of the disease may serve as early predictors of development, progression, and severe course of NEC.

Materials and Methods: The study was conducted in two stages and included 28 children who were treated at the Chelyabinsk regional children's clinical hospital from November 2021 to December 2022. The first stage involved the examination of premature newborns, among whom a group of newborns with NEC IIIB-IIIAB was identified. Venous blood was used for the study. The second stage included the study of intestinal specimens obtained during surgical interventions in newborns with surgical pathology.

Results and discussion: Children with NEC showed a significant decrease in the specific activity of platelet monoamine oxidase (MAO), which correlated with the activity of MAO in gut specimens obtained during surgery. A decrease in the activity of Mg-ATPase in erythrocytes was established at 50-100% of the maximum enzyme activity in the control group, while the activity of Na-K-ATPase decreased by 4 times from the maximum values in the control group. There was a significant increase in the activity of Ca-ATPase in erythrocytes of preterm infants with necrotizing enterocolitis. The obtained data suggest that platelet monoamine oxidase (MAO) in preterm newborns may potentially serve as an indicator of tissue and organ immaturity, rather than a marker of inflammation and oxidative damage. The results of erythrocyte ATPase activity for the group of preterm infants with surgical stages of necrotizing enterocolitis indicate a hypoxic, hypoenergetic state, accompanied by high concentrations of intracellular calcium.

Conclusion: The obtained data are promising in terms of developing new methods for the diagnosis/prognosis of necrotizing enterocolitis in newborns.

作者简介

P. Vinel

ФГБОУ ВО ЮУГМУ Минздрава России

Email: vinelpolina@icloud.com
ORCID iD: 0000-0002-3745-3690
SPIN 代码: 6298-8131
俄罗斯联邦

V. Tsareva

ФГБОУ ВО ЮУГМУ Минздрава России
ГАУЗ "Челябинская областная детская клиническая больница"

Email: semenovatsareva@mail.ru
ORCID iD: 0000-0002-6695-7388
SPIN 代码: 7966-9068
俄罗斯联邦

P. Baboshko

ГАУЗ "Челябинская областная детская клиническая больница"

Email: 904306008@mail.ru
ORCID iD: 0009-0009-2627-0459
俄罗斯联邦

A. Sinitskii

ФГБОУ ВО ЮУГМУ Минздрава России

Email: Sinitskiyai@yandex.ru
ORCID iD: 0000-0001-5687-3976
SPIN 代码: 3681-1816
俄罗斯联邦

A. Kozhevnikov

ФГБОУ ВО ЮУГМУ Минздрава России

Email: vk_523@mail.ru
ORCID iD: 0009-0008-5400-3043
俄罗斯联邦

A. Grunin

ФГБОУ ВО ЮУГМУ Минздрава России

编辑信件的主要联系方式.
Email: sasha_grunin@mail.ru
ORCID iD: 0009-0007-9327-7779
俄罗斯联邦

参考

  1. Tan X., Zhou Y., Xu L., Zhang L., Wang J., Yang W. The predictors of necrotizing enterocolitis in newborns with low birth weight: A retrospective analysis. Medicine. 2022; 101(7).
  2. Mustala O., Solatunturi E., Tarpila S. Monoamine oxidase activity in the human small intestine. Acta Medica Scandinavica. 1969; 185(1‐6):145-46.
  3. Gershon M. D., Sherman D. L., Pintar J. E. Type‐specific localization of monoamine oxidase in the enteric nervous system: Relationship to 5‐hydroxytryptamine, neuropeptides, and sympathetic nerves. Journal of comparative neurology. 1990; 301(2): 191-213.
  4. Nicotra A., Pierucci F., Parvez H., Senatori O. Monoamine oxidase expression during development and aging. Neurotoxicology. 2004; 25(1-2): 155-65.
  5. Lewinsohn R., Glover V., Sandler M. Development of benzylamine oxidase and monoamine oxidase A and B in man. Biochemical pharmacology. 1980; 29(9): 1221-230.
  6. Ramsay R. R., Albreht A. Kinetics, mechanism, and inhibition of monoamine oxidase. Journal of Neural Transmission. 2018; 125(11): 1659-83.
  7. Bond P. A., Cundall R. L. Properties of monoamine oxidase (MAO) in human blood platelets, plasma, lymphocytes and granulocytes. Clinica Chimica Acta. 1977; 80(2): 317-26.
  8. Bonuccelli U., Piccini P., Del Dotto P., Pacifici G. M., Corsini G. U., Muratorio A. Platelet monoamine oxidase B activity in parkinsonian patients. Journal of Neurology, Neurosurgery & Psychiatry. 1990; 53(10): 854-55.
  9. Oreland L. Platelet monoamine oxidase, personality and alcoholism: the rise, fall and resurrection. Neurotoxicology. 2004; 25(1-2): 79-89.
  10. Shulhan J., Dicken B., Hartling L., Larsen B. M. Current knowledge of necrotizing enterocolitis in preterm infants and the impact of different types of enteral nutrition products. Advances in nutrition. 2017; 8(1): 80-91.
  11. Vinel P. K., Grobovoy S. I., Sinitskii A. I., Kolesnikov, O. L. Modification of a spectrophotometric method for assessment of monoamine oxidase activity with 2, 4-dinitrophenylhydrazine as a derivatizing reagent. Analytical Biochemistry. 2021; 629: 114294.
  12. Bartolommei G., Moncelli M. R., Tadini-Buoninsegni F. A method to measure hydrolytic activity of adenosinetriphosphatases (ATPases). PLOS one. 2013; 8(3): e58615.
  13. Roth J. A., Young J. G., Cohen D. J. Platelet monoamine oxidase activity in children and adolescents. Life Sciences. 1976; 18(9): 919-24.
  14. Cawthon R. M., Pintar J. E., Haseltine F. P., Breakefield X. O. Differences in the structure of A and B forms of human monoamine oxidase. Journal of neurochemistry. 1981; 37(2): 363-72.
  15. Sostek A. J., Sostek A. M., Murphy D. L., Martin E. B., Born, W. S. Cord blood amine oxidase activities relate to arousal and motor functioning in human newborns. Life Sciences. 1981; 28(22): 2561-68.
  16. Jones J. B., Southgate J. Platelet Monoamine Oxidase Activity in the Human Fetus. Developmental Medicine & Child Neurology. 1976; 18(5): 640-42.
  17. Lewinsohn R., Sandler M. Monoamine-oxidizing enzymes in human pregnancy. Clinica Chimica Acta. 1982; 120(3): 301-312.
  18. Oreland L., Shaskan E. G. Monoamine oxidase activity as a biological marker. Trends in Pharmacological Sciences. 1983; 4: 339-41.
  19. Stillwell, W. An introduction to biological membranes: composition, structure and function. Elsevier. 2016.
  20. Bistritzer T., Berkovitch M., Rappoport M. J., Evans S., et al. Sodium potassium adenosine triphosphatase activity in preterm and term infants and its possible role in sodium homeostasis during maturation. Archives of Disease in Childhood-Fetal and Neonatal Edition. 1999; 81(3): F184-F187.
  21. Tian J., Xie Z. J. The Na-K-ATPase and calcium-signaling microdomains. Physiology. 2008; 23(4): 205-11.
  22. Auland M. E., Morris M. B., Roufogalis B. D. Separation and characterization of two Mg2+-ATPase activities from the human erythrocyte membrane. Archives of biochemistry and biophysics. 1994; 312(1): 272-77.
  23. Beleznay Z., Zachowski A., Devaux P. F., Ott, P. Characterization of the correlation between ATP‐dependent aminophospholipid translocation and Mg2+‐ATPase activity in red blood cell membranes. European journal of biochemistry. 1997; 243(1‐2): 58-65.
  24. Nozadze E., Arutinova N., Tsakadze L., et al. Molecular mechanism of Mg-ATPase activity. The Journal of Membrane Biology. 2015; 248(2): 295-300.
  25. Bogdanova A., Makhro A., Wang J., Lipp P., Kaestner L. Calcium in red blood cells—a perilous balance. International journal of molecular sciences. 2013; 14(5): 9848-872.
  26. Zylinska L., Gulczynska E., Kozaczuk A. Changes in erythrocyte glutathione and plasma membrane calcium pump in preterm newborns treated antenatally with MgSO4. Neonatology. 2008; 94(4): 272-78.
  27. Ogbodo U. C., Emeh J. K., Neboh E. E., Ocheni S., Maduka I. C., Ikekpeazu E. J. Estimation of intracellular magnesium concentrations and membrane atpase activities in the red blood cells of normal and sickle cell subjects in Enugu, Southeast Nigeria. Int J Biol Med Res. 2010; 1(4): 149-152.
  28. Bogdanova A., Makhro A., Wang J., Lipp P., Kaestner L. Calcium in red blood cells—a perilous balance. International journal of molecular sciences. 2013; 14(5): 9848-72.

补充文件

附件文件
动作
1. JATS XML

版权所有 © Vinel P.K., Tsareva V.V., Baboshko P.G., Sinitskii A.I., Kozhevnikov A.S., Grunin A.V.,

##common.cookie##