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Противовоспалительный фактор слизистых – секретоглобин SCGB1A1

https://doi.org/10.18093/0869-0189-2015-25-4-492-496

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Аннотация

Секретоглобин SCGB1A1 – белок, синтезируемый секреторными клетками эпителия воздухоносных путей (клубными клетками, или клетками Клара), а также другими эпителиальными клетками дыхательного и урогенитального тракта. Семейство секретоглобинов участвует в обеспечении гомеостаза при окислительном повреждении, воспалении, аутоиммунных процессах и канцерогенезе. Первый член семейства – секретоглобин SCGB1A1 – многофункциональный белок с выраженными противовоспалительными, иммуномодулирующими свойствами. В дополнение к его противовоспалительной функции он также проявляет антихемотактические, противоаллер гические, противоопухолевые свойства, а также оказывает ростостимулирующий эффект на преимплантированный эмбрион. Генетический полиморфизм гена SCGB1A1 связан с частотой развития ряда воспалительных и аутоиммунных заболеваний. Эти свойства предполагают возможность его использования для диагностики и лечения воспалительных, аутоиммунных и аллергических заболеваний.

Об авторах

Н. К. Малая
ГУ "Крымский государственный медицинский университет им. С.И.Георгиевского": 295006, Россия, Республика Крым, Симферополь, бр Ленина, 5 / 7
Россия

аспирант кафедры педиатрии с курсом физиотерапии ФПО ГУ "Крымский государственный медицинский университет им. С.И.Георгиевского"; тел.: (978) 8483121



Н. Н. Каладзе
ГУ "Крымский государственный медицинский университет им. С.И.Георгиевского": 295006, Россия, Республика Крым, Симферополь, бр Ленина, 5 / 7
Россия

д. м. н., профессор, зав. кафедрой педиатрии с курсом физиотерапии ФПО ГУ "Крымский государственный медицинский университет им. С.И.Георгиевского"; тел.: 38 (0652) 276626



К. Д. Малый
ГУ "Крымский государственный медицинский университет им. С.И.Георгиевского": 295006, Россия, Республика Крым, Симферополь, бр Ленина, 5 / 7
Россия

к. м. н., ст. преподаватель кафедры биофизики ГУ "Крымский государственный медицинский университет им. С.И.Георгиевского"; тел.: (978) 8483117



Список литературы

1. Mucherjee A.B., Zhang Z., Chilton B.S. Uteroglobin: a steroid inducible immunomodulatory protein that founded the secreto globin superfamily. Endocrin. Rev. 2007; 28 (7): 707–725.

2. Wong A.P., Keating A., Waddell T.K. Airway regeneration: The role of the Clara cell secretory protein and the cells that express it. Cytotherapy. 2009; 11: 676–687.

3. Krishnan R.S., Daniel J.C. Jr. Blastokinin: Inducer and regulator of blastocyst development in the rabbit uterus. Science. 1967; 158: 490–492.

4. Beier H.M. Uteroglobin: A hormone sensitive endometrial protein involved in blastocyst development. Biochem. Biophys. Acta. 1968; 160: 289–291.

5. Kundu G.C., Zhang Z., Mantile Selvaggi G. et al. Uteroglobin binding proteins: regulation of cellular motility and invasion in normal and cancer cells. Ann. NY Acad. Sci. 2001; 923: 234–248.

6. Singh G., Katyal S.L., Gottron S.A. Antigenic, molecular and functional heterogeneity of Clara cell secretory proteins in the rat. Biochim. Biophys. Acta. 1985; 829: 156–163.

7. Bernard A.M., Dumont X., Roels H. et al. The molecular mass and concentrations of protein 1 or Clara cell protein in biological fluids: a reappraisal. Clin. Chim. Acta. 1993; 223:189–191.

8. Klug J., Beier H.M., Bernard A. et al. Uteroglobin / Clara cell 10 kDa family of proteins: nomenclature committee report. Ann. NY Acad. Sci. 2000; 923: 348–354.

9. Nie W., Xue C., Chen J. et al. Secretoglobin 1A member 1 (SCGB1A1) +38A/G polymorphism is associated with asthma risk: a meta analysis. Gene. 2013; 528 (2): 304–308.

10. http://www.genecards.org/cgibin/carddisp.pl?gene=SCGB1A1

11. Chen C., Schilling K., Hiipakka R.A. et al. Prostate α protein. Isolation and characterization of the polypeptide components and cholesterol binding. J. Biol. Clem. 1982; 256: 116–121.

12. Fleming T.P., Watson M.A. Mammaglobin, a breast specific gene, and its utility as a marker for breast cancer. Ann. NY Acad. Sci. 2000; 923: 78–89.

13. Ni J., Kalff Sucke M., Gentz R. et. al. All human genes of uteroglobin family are localized on chromosome 11q12.2 and form a dense cluster. Ann. NY Acad. Sci. 2000; 923: 25–42.

14. Callebaut I., Poupon A., Bally R. et al. The uteroglobin fold. Ann. NY Acad. Sci. 2000; 923: 90–112.

15. Pattabiraman N., Matthews J.H., Ward K.B. et al. Crystal structure analysis of recombinant human uteroglobin and molecular modeling of ligand binding. Ann. NY Acad. Sci. 2000; 923: 113–127.

16. Ghafouri B., Stahiborn B., Tagesson C. et.al. Newly identified proteins in human nasal lavage fluid from non smokers and smokers using two dimensional gel electrophoresis and peptide mass fingerprinting. Proteomics. 2002; 2: 112–120.

17. Nieto A., Ponstingl H., Beato M. Purification and quaternary structure of the hormonally induced protein uteroglobin. Arch. Biochem. Biophys. 1997; 180: 82–92.

18. De la Cruz X., Lee B. The structural homology between utero globin and the pore forming domain of colicin A suggests a possible mechanism of action for uteroglobin. Protein. Sci. 1996; 5: 857–861.

19. Pilon A.L. Rationale for the development of recombinant human CC10 as a therapeutic for inflammatory and fibrotic disease. Ann. NY Acad. Sci. 2000; 923: 280–299.

20. Karn R.C., Laukaitis C.M. Characterization of two forms of mouse salivary androgen binding protein (ABP): Implications for evolutionary relationships and ligand binding function. Biochemistry. 2003; 42: 7162–7170.

21. Hay J.G., Danel C., Chu C.S. et al. Human CC10 gene expression in airway epithelium and subchromosomal locus suggest lincage to airway disease. Am. J. Physiol. 1995; 268 (4, Pt 1): 565–575.

22. Wolf M., Klug J., Hackenberg R. et al. Human CC10, the homologue of rabbit uteroglobin: genomic cloning, chromosomal localization and expression in endometrial cell lines. Hum. Mol. Genet. 1992; 1: 371–378.

23. Zhang Z., Zimonjic D.B., Popescu N.C. et al. Human uteroglobin gene: structure, subchromosomal localization, and polymorphism. DNA Cell Biol. 1997; 16: 73–83.

24. Chilton B.S., Mani S.K., Bullock D.W. Servomechanism of prolactin and progesterone in regulating uterine gene expression. Mol. Endocrinol. 1988; 2: 1169–1175.

25. Kikukawa T., Cowan B.D., Tejada R.I., Mukherjee A.B. Partial characterization of a uteroglobin like protein in the human uterus and its temporal relationship to prostaglandin levels in this organ. J. Clin. Endocrinol. Metab. 1988; 67: 315–321.

26. Suske G., Wenz M., Cato A.C.B., Beato M. The uteroglobin gene region: hormonal regulation, repetitive elements and complete nucleotide sequence of the gene. Nucleic. Acids Res. 1983; 11: 2257–2271.

27. Frerking I., Sengler C., Günther A. et al. Evaluation of the 26G>A CC16 polymorphism in acute respiratory distress syndrome. Crit. Care Med. 2005; 33 (10): 2404–2406.

28. Ray R., Choi M., Zhang Z. Uteroglobin Suppresses SCCA Gene Expression Associated with Allergic Asthma. J. Biol. Chem. 2005; 280: 9761–9764.

29. Ku M.S., Sun X.L., Lu K.H. The CC16 A38G polymorphism is associated with the development of asthma in children with allergic rhinitis. Clin. Exp. Allergy. 2011; 41: 794–800.

30. de Burbure C., Pignatti P., Corradi M., Malerba M. Utero globin related protein 1 and clara cell protein in induced sputum of patients with asthma and rhinitis. Chest. 2007; 131 (1): 172–179.

31. Janssen R., Sato H., Grutters J.C. et al. The Clara cell10 Adenine38Guanine polymorphism and sarcoidosis suscepti bility in Dutch and Japanese subjects. Am. J. Respir. Crit. Med. 2004; 170: 1185–1187.

32. Menegatti E., Nardacchione A., Mirella A. et al. Polymorphism of the uteroglobin gene in systemic lupus erythematosus and IgA nephropathy. Lab. Invest. 2002; 82: 543–546.

33. Chowdhury B., Zhang Z., Mukherjee A.B. Uteroglobin interacts with the heparin binding site of fibronectin and prevents fibronectin IgA complex formation found in IgA nephropathy. FEBS Lett. 2008; 582 (5): 611–615.

34. Yong D., QingQing W., Hua L. et al. Association of uteroglobin G38A polymorphism with IgA nephropathy: a metaanalysis. Am. J. Kidney Dis. 2006; 48 (1): 1–7.

35. Mansur A.H. Secretoglobin 1A1 gene and asthma predisposition: what is the evidence? Clin. Exp. Allergy. 2009; 39: 8–11.

36. Mandal A.K., Ray R., Zhang Z. et al. Uteroglobin inhibits prostaglandin F2α receptor mediated expression of genes critical for the production of proinflammatory lipid mediators. J. Biol. Chem. 2005; 280: 32897–32904.

37. Shijubo N., Itoh Y., Abe S. Anti inflammatory molecule, Clara cell 10 kilodalton protein and respiratory diseases. Rinsho Byori. 2002; 50 (4): 370–373.

38. Kundu G.C., Zhang Z., Mantile Selvaggi G. et al. Uteroglobin binding proteins: regulation of cellular motility and invasion in normal and cancer cells. Ann. NY Acad. Sci. 2000; 923: 234–248.

39. Schiffmann E., Geetha V., Pencev D. et al. Adherence and regulation of leukotaxis. Agents Actions Suppl. 1983; 12: 106–120.

40. Le Y., Murphy P.M., Wang J.M. Formyl peptide receptors revisited. Trends Immunol. 2002; 23: 541–548.

41. Ye B.Q., Geng Z.H., Ma L. et.al. Slit2 Regulates Attractive eosinophil and repulsive neutrophil chemotaxis through differential srGAP1 expression during lung inflammation. J. Immunology. 2010; 185: 6294–6305.

42. Riffo M., Gonzalez K.D., Nieto A. Uteroglobin induces the development and cellular proliferation of the mouse early embryo. J. Exp. Zool. Part A Ecol. Genet. Physiol. 2007; 307: 28–34.

43. Robinson D.H., Kirk K.L., Benos D.J. Macromolecular transport in rabbit blastocysts: evidence for a specific utero globin transport system. Mol. Cell. Endocrinol. 1989; 63: 227–237.

44. Linnoila R.I., Szabo E., Demayo F. et al. The role of CC10 in pulmonary carcinogenesis: from a marker to tumor suppression. Ann. NY Acad. Sci. 2000; 923: 249–267.

45. Zhang Z., Kundu G.C., Panda D. et al. Loss of transformed phenotype in cancer cells by overexpression of the uteroglobin gene Proc. Natl. Acad. Sci. USA. 1999; 96: 3963–3968.

46. Zhang Z, Kim SJ, Chowdhury B, et al. Interaction of utero globin with lipocalin 1 receptor suppresses cancer cell motility and invasion. Gene. 2006; 369: 66–71.

47. Moreno J.J. Effects of antiflammins on transglutaminase and phospholipase A2 activation by transglutaminase. Int. Immunopharmacol. 2006; 6: 300–303.

48. Lesur O., Bernard A., Arsalane K. Clara cell protein (CC16)induces a phospholipase A2 mediated inhibition of fibroblast migration in vitro. Am. J. Respir. Crit. Care Med. 1995; 152:290–297.

49. Mandal A.K., Zhang Z., Ray R. et al. Uteroglobin represses allergen induced inflammatory response by blocking PGD2 receptor mediated functions. J. Exp. Med. 2004; 199: 1317–1330.

50. Mariniello L., Porta R. Transglutaminases as biotechnological tools. Prog. Exp. Tumor Res. 2005; 38: 174–191.

51. Lorand L., Graham R.M. Transglutaminases: crosslinking enzymes with pleotropic functions. Nat. Rev. Mol. Cell. Biol. 2003; 4: 140–156.

52. Miele L. New weapons against inflammation: dual inhibitors of phospholipase A2 and transglutaminase. J. Clin. Invest. 2003; 111: 19–21.

53. Zhang Z., Kundu G.C., Zheng F. et al. Insight into the physiological function(s) of uteroglobin by gene knockout and antisense transgenic approaches. Ann. NY Acad. Sci. 2000;923: 210–233.

54. Chen L.C., Zhang Z., Myers A.C. et al. Cutting edge: altered pulmonary eosinophilic inflammation in mice deficient for Clara cell secretory 10 kDa protein. Immunology. 2001; 167: 3025–3028.

55. Miele L. Antiflammins. Ann. NY Acad. Sci. 2000; 293:128–140.

56. Moreno J.J. Antiflammin peptides in the regulation of inflammatory response. Ann. NY Acad. Sci. 2000; 923: 147–153.

57. Miele L., Cordella Miele E., Facchiano A. et al. Novel antiinflammatory peptides from the region of highest similarity between uteroglobin and lipocortin I. Nature. 1988; 335: 726–730.

58. Hope W.C., Patel B.J., Bolin D.R. Antiflammin 2 (HDMNKVLDL) does not inhibit phospholipase A2 activities. Agents Actions. 1991; 34: 77– 80.

59. Ye J.M., Wolfe J.L. Oxidative degradation of antiflammin 2. Pharm. Res. 1996; 13: 250–255.


Рецензия

Для цитирования:


Малая Н.К., Каладзе Н.Н., Малый К.Д. Противовоспалительный фактор слизистых – секретоглобин SCGB1A1. Пульмонология. 2015;25(4):492-496. https://doi.org/10.18093/0869-0189-2015-25-4-492-496

For citation:


Malaya N.K., Kaladze N.N., Malyy K.D. Mucosal anti6inflammatory factor secretoglobin SCGB1A1. PULMONOLOGIYA. 2015;25(4):492-496. (In Russ.) https://doi.org/10.18093/0869-0189-2015-25-4-492-496

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