Материал: Донсков С.И., Мороков В.А. Группы крови человека. Руководство по иммуносерологии

Внимание! Если размещение файла нарушает Ваши авторские права, то обязательно сообщите нам

Антитела анти-Р у женщин с фенотипом P k не вызывали угнетения беременности и лишь в редких случаях служили причиной легких форм ГБН (Nakagima

и соавт. [126],Yamaguchi и соавт. [174]).

Антитела анти-Р, ассоциированные с привычными выкидышами, были описаны у японской женщины с фенотипом P2 k и женщины с фенотипом P1 k жительницы Кувейта (Shirey и соавт. [150], Yoshida и соавт. [176]). У 1-й женщины было 4 самопроизвольных выкидыша, у 2-й – 13. Ни та, ни другая не имели детей. В дальнейшем обеим женщинам с 5–6 недели очередной беременности проводили плазмаферез с целью снижения титра антител. Обе женщины родили жизнеспособных детей, не нуждающихся в каком-либо специальном лечении, кроме фототерапии. В сыворотке крови женщины из Кувейта присутствовали IgM, IgG (главным образом IgG3) и IgA; такие же анти-Р-антитела были элюированы из тканей плаценты. Плазму японской женщины адсорбировали Р-положительными эритроцитами, после чего производили реинфузию (Yoshida и соавт. [176]). Имеются другие сообщения об эффективном применении плазмафереза у женщин, имеющих р-фенотип и страдающих невынашиванием бе-

ременности (Fernandez-Jimenez и соавт. [43], Rydberg и соавт. [140], Shechter [147],Yoshida и соавт. [177]).

Необычные антитела выявили Vos и соавт. [167] в Перте (Западная Австралия) у женщин с привычным невынашиванием беременности. Эти антитела вызывали гемолиз, но не агглютинировали эритроциты Р1 и Р2; тесты с эритроцитами р были отрицательными. Женщины имели фенотип Р1. Гемолизины обнаруживали в сыворотках крови только в момент самопроизвольного выкидыша, вне беременности антитела не обладали гемолитической активностью. Гемолитическая активность не была опосредована комплементом. Vos и соавт. [164–167], обследовавшие женщин, не нашли какого-либо объяснения указанному феномену.

У женщин Канады, США и Венгрии, страдавших невынашиванием беременности, подобных гемолизинов не обнаружено (Horvath и соавт. [63], Vos et al [167]).

Список литературы

1.Пискунова Т.М., Ичаловская Т.А. Фенотип крови Джей (Tj) и его взаимоотношения с групповой системой крови Р // Пробл. гематол. – 1975. – № 7. – С. 30–33.

2.AdinolfiM.,PolleyM.J.,HunterD.A.,MollisonP.L.Classificationofblood-groupantibodies as β2M or gamma globulin // Immunology. – 1962. – V. 5. – P. 566–579.

3.Allen F.H., Marsh W.L., Jensen L., Fink J. Anti-IP: an antibody defining another product of interaction between the genes of the I and P blood group systems // Vox Sang. – 1974. – V. 27. – P. 442–446.

4.Almeida R., Amado M., David L. et al. A family of human β4-galactosyltransferases: cloning and expression of two novel UDP-galactose: β-N-acetylglucosamine β1, 4-galactosyltransferases, β4Gal-T3 // J. Biol. Chem. – 1997. – V. 272. – P. 31979–31991.

516

5.Amado M., Almeida R., Carneiro F. et al. A family of human β3-galactosytransferases. Characterization of four members of a UDP-galactose:β-N-acetylglucosamine / β-N-acetyl- galactosamine β-1,3-galactosyltransferase family // J. Biol. Chem. – 1998. – V. 273. – P. 12770– 12778.

6.Anstee D.J. Blood group-active surface molecules of the human red blood cells // Vox Sang. – 1990. – V. 58. – P. 1–20.

7.Anstee D.J., Holt P.D.J., Pardoe G.J. Agglutinins from fish ova defining blood groups B and P// Vox Sang. – 1973. – V. 25. – P. 347–360.

8.Anstee D.J., Tanner M.J.A. The distribution of blood-group antigens on butanol extraction of human erythrocyte ‘ghosts’// Biochem. J. – 1974. – V. 138. – P. 381–386.

9.Arndt P.A., Garratty G., Marfoe R.A., Zeger G.D. An acute hemolytic transfusion reaction caused by anyi-P1 that reacted at 37  oC // Transfusion. – 1998. – V. 38. – P. 373–377.

10.Bailly P., Bouhours J.-F. P blood group and related antigens // Blood Cell Biochemistry / J.-P. Cartron, P. Rouger, eds. – N.Y.: Plenum Press. – 1995. – V.6. – P. 299–329.

11.Bailly P., Chevaleyre J., Sondag D. et al. Characterization of a murine monoclonal antibody specific for the human P1 blood group antigen // Mol. Immunol. – 1987. –

V.24. – P. 171–176.

12.Beck M.L. ed. Third International Workshop and Symposium on Monoclonal Antibodies Against Human Red Blood Cells an Related Antigens // Transfus. Clin. Biol. – 1997. –

V.4. – P. 13–54 (8 papers).

13.Ben-IsmailR.,RougerP.,CarmeB.etal.Comparativeautomatedassayofanti-P1 antibodies in acute hepatic distomiasis (fasciolasis) and in hydatidosis // Vox Sang. – 1980. – V. 38. –

P.165–168.

14.Bevan B., Hammond W., Clarke R.I. Anti-P1-associated with liver-fluke infection // Vox Sang. – 1970. – V. 18. – P. 188–189.

15.Bono R., Cartron J.P., Mulet C. et al. Selective expression of blood group antigens on human teratocarcinoma cells // Rev. Franc. Transfus. Immunohemat. – 1981. – V. 24. –

P.97–107.

16.Booth P.B.Anti-I TP1: an antibody showing a further association between the I and P blood group systems // Vox Sang. – 1970. – V. 19. – P. 85–90.

17.BouhoursD.,BouhoursJ.F.,WikkemC.etal.OverexpressionoftheP1bloodgroupantigen on red cells from CDAII patient [Abstract] //Vox Sang. – 1994. –V. 67 (Suppl. 2). – P. 118.

18.BrodinN.T.,DahmenJ.,NilssonB.etal.Monoclonalantibodiesproducedbyimmunization with neoglycoproteins containing Galα1- 4Galβ1-4Glcβ-O and Galα14Galβ1- 4GlcNAcβ-O residues: useful immunochemical and cytochemical reagents for blood group Pantigens and a differentiation marker in Burkitt lymphoma and other B-cell malignancies // Int. J. Cancer. – 1988. – V. 42. – P. 185–194.

19.Brown K.E. Haematological consequences of parvovirus B19 infection // Bailliere Best Pract. Res. Clin. Haematol. – 2000. – V. 13. – P. 245–259.

20.Brown K.E., Anderson S.M., Young N.S. Erythrocyte P antigen: cellular receptor for B19 parvovirus // Science. – 1993. – V. 262. – P. 114–117.

21.Brown K.E., Hibbs J.R., Gallinella G. et al. Resistance to parvovirus B19 infection due to lack of virus receptor (erythrocyte P antigen) // N. Engl. J. Med. – 1994. – V. 330. –

P.1192–1196.

22.Bruce M., Watt A., Gabra G.S. et al. LKE red cell antigen and its relationship to P1 and P k: serological study of a large family // Vox Sang. – 1985. – V. 55. – P. 237–240.

23.Cameron G.L., Staveley J.M. Blood group P substance in hydratid cyst fluids // Nature. – 1957. – V. 179. – P. 147–148.

24.Cantin G., Lyonnais J. Anti-PP1P k and early abortion // Transfusion. – 1983. – V. 23. –

P.350–351.

517

25.Catino M.L., Busch S., Huestis D.W., Stern K. Transmission of the blood group genotype pp (Tj a-negative) in a kinship with multiple consanguineous marriages // Amer. J. Hum. Genet. – 1965. – V. 17. – P. 36–41.

26.Cedergren B. Population studies in northern Sweden. IV. Frequency of the blood type P // Hereditas. – 1973. – V. 73. – P. 27–30.

27.Chandeysson P.L., Flye M.W., Simpkins S.M., Holland P.V. Delayed hemolytic transfusion reaction caused by anti-P1 antibody // Transfusion. – 1981. – V. 21. – P. 77–82.

28.ChengM.S.Potentanti-P1 followingbloodtransfusion//Transfusion.–1984.–V.24.–P.183.

29.Chester M.A., Johnson U., Lundblad A. et al. // Proc. 2-nd. Int. Workshop and Symposium on MonoclonalAntibodiesAgainstHumanRedBloodCellsanRelatedAntigens.,1990.–P.86–92.

30.CohenD.W.,NelsonL.Auto-anti-Preactingonlybylow-ionic-strengthsolutionsinapatient with hemolysis // Transfusion. – 1983. – V. 23. – P. 79–80.

31.Contreras M., Tippett P. The Lu(a −b −) syndrome and an apparent upset of P1 inheritance // Vox Sang. – 1974. – V. 27. – P. 369–371.

32.Cooling L.L.W., Zhang D., Koerner T.A.W. Human platelets express gangliosides with LKE activity andABH blood group activity // Transfusion. – 2001. – V. 41. – P. 504–516.

33.Cory H.T., Yates A.D., Donald A.S.R. et al. The nature of the human blood group P1 determinant // Biochem. Biophys. Res. Commun. – 1974. – V. 61. – P. 1289–1296.

34.Cowles J.W., Blumberg N. Neutralization of P blood group antibodies by synthetic solidphase antigens // Transfusion. – 1987. – V. 27. – P. 272–275.

35.CoxM.T.,RobertsM.,LaJoieJ.etal.AnapparentprimaryimmuneresponseinvolvingantiJk a and anti-P1 detected 10 days after transfusion // Transfusion. – 1992. – V. 32. – P. 874.

36.Crawford M.N., Tippett P., Sanger R.AntigensAu, I and P1 of cells of the dominant type of Lu(a −b −) // Vox Sang. – 1974. – V. 26. – P. 283–287.

37.Daniels G.L. Human Blood Groups. – 2-nd. ed. – Oxford: Blackwell Science, 2002. – 560 p.

38.DiNapoli J.B., Nichols M.E., Marsh W.L. et al. Hemolytic transfusion reaction caused by IgG anti-P1 [Abstract] // Transfusion. – 1978. – V. 18. – P. 383.

39.Dunstan R.A. Status of major red cell blood group antigens on neutrophils, lymphocytes and monocytes // Brit. J. Haemat. – 1986. – V. 62. – P. 301–309.

40.Elder A.F., Spitalnik S.L. Blood group antigens as receptors for pathogens // Molecular Biology and Evolution of Blood Group and MHC Antigens in Primates / A. Blancher, J. Kein, W.W. Socha eds. – Berlin: Springer-Verlag, 1997. – P. 268–304.

41.Engelfriet C.P., von Beckers D., dem Borne A.E.G.K. et al. Haemolysins probably recognizing the antigen p // Vox Sang. – 1971. – V. 23. – P. 176–181.

42.Fellous M., Gerbal M., Nobillot G., Weils J. Studies on the biosynthetic pathway of human

Perythrocyte antigen using genetic complementation tests between fibroblasts from rare, p and P k phenotype donors // Vox Sang. – 1977. – V. 32. – P. 262–268.

43.Fernandez-Jimenez M.C., Jimenez-Marco M.T., Hernandez D. et al. Treatment with

plasmapheresis and intravenous immunoglobulin in pregnancies complicated with anti-PP1P k or anti-K immunization: a report of two patients // Vox sang. – 2000. – V. 80. – P. 117–120.

44.Fisher R. The variation in strength of the human blood group P // Heredity. – 1953. – V. 7. – P. 81–89.

45.Fletcher K.S., Brener E.G. Schwarting G.A. Pblood group regulation of glycosphingolipid level in human erythrocytes // J. Biol. Chem. – 1979. – V. 254. – P. 11196–11198.

46.Francois-GerardC.,BrocteurJ.,AndreA.etal.Demonstrationoftheexistenceofaspecific blood-group P1 antigenic determinant in turtle-dove ovomucoid // Rev. Franc. Transfus. Immunohemat. – 1980. – V. 23. – P. 579–588.

47.Francois-GerardC.,BrocteurJ.,AndreA.Turtledove:anewsourceofP1-likematerialcross- reacting with the human erythrocyte antigen //Vox Sang. – 1980. –V. 39. – P. 141–148.

518

48.Francois-Gerard C., Gerday C., Beeley J.G. Turtle-dove ovomucoid, a glycoprotein proteinase inhibitor with P1-blood group antigen activity // Biochem. J. – 1979. – V. 177. –

P.679–685.

49.Furukawa K. Properties of P blood group antigen and antibodies // Jpn. J. Hum. Genet. – 1975. – V. 20. – P. 32–33.

50.Furukawa K., Iwamura K., Uchikawa M. et al. Molecular basis for the p phenotype: identification of distinct and multiple mutations in the α1,4-Galactosyltransferase-gene in Swedish and Japanese individuals // J. Biol. Chem. – 2000. – V. 275. – P. 37752–37756.

51.GrahamH.A.,WilliamsA.N.AgeneticmodelfortheinheritanceoftheP,P1 andP k antigens

//Immunol. Commun. – 1980. – V. 9. – P. 191–201.

52.Green D.A. P1 blood group and haemolytic uraemic syndrome // Clin. Lab. Haemat. – 2000. – V. 22. – P. 55.

53.Haataja S., Tikkanen K., Liukkonen J. et al. Characterization of a novel bacterial adhesin specificity of Streptococcus suis recognizing blood group P receptor oligosaccharides //

J.Biol. Chem. – 1993. – V. 268. – P. 114–117.

54. Hammache D., Yahi N., Maresca M. et al. Human erythrocytes glycosphingolipids as alternative cofactor for human immunodeficiency virus type 1 (HIV-1) gp120 and reconstituted membrane microdomains o glycosphingolipids (Gb3 and GM3) // J. Virol. – 1999. – V. 73. – P. 5244–5248.

55.Hansson G.C., Wasniowska K., Rock J.A. et al. The glycosphingolipid composition of the placenta of a blood group Pfetus delivered by a blood group P1 k woman and analysis of the anti-globoside antibodies found in maternal serum // Arch. Biochem. Biophys. – 1988. –

V.260. – P. 168–176.

56.Hayashida Y., Waanabe A. A case of p Taiwanese woman delivered of an infant with hemolytic disease of the newborn // Jpn. J. Legal. Med. – 1968. – V. 22. – P. 10–15.

57.Heddle N.M. Acute paroxysmal cold hemoglobinuria // Transfus. Med. Rev. – 1989. –

V.3. – P. 219–229.

58.Heiken A. Observations on the blood group receptor P1 and its development in children // Hereditas. – 1966. – V. 56. – P. 83–98.

59.HellbergA.,PooleJ.,OlssonM.L.Molecularbasisofthegloboside-deficientP k bloodgroup phenotype.IdentificationoffourinactivatingmutationsintheUDP-N-acetylgalactosamine: 6globotriaosylceramide 3-β-N-acetylgalactosaminyltransferase gene // J. Biol. Chem. – 2002. – V. 277. – P. 29455–29459.

60.Henningsen K. Etude d’ensemble du facreur sanguin P // Rev. Hemat. – 1950. – V. 5. –

P.76–284.

61.Henningsen K.InvestigationsonthebloodfactorP//ActaPath.Microbiol.Scand.–1949.–

V.26. – P. 639–654.

62.Henningsen K. On the heredity of blood factor P //Acta Path. Microbiol. Scand. – 1949. –

V.26. – P. 769–785.

63.Horvath E., Paisz I.Absence of anti-Tj a-like hemolysin in pregnant aborters in Budapest // Transfusion. – 1966. – V. 6. – P. 499–500.

64.Iizuka S., Chen S.-H., Yoshida A. Studies on the human blood group Psystem: an existence of UDP-Gal: Lactosylceramide α1→4 galactosyltransferase in the small p type cells // Biochem. Biophys. Res. Commun. – 1986. – V. 137. – P. 1187–1195.

65.Ikin E.W., Kay H.E.M., Playfair J.H.L., Mourant A.E. P1 antigen in the human foetus // Nature. – 1961. – V. 192. – P. 883.

66.Inglis G., Fraser R.H., Mitchell A.A.B. et al. Serological characterization of a mouse monoclonal anti-P-like antibody // Vox Sang. – 1987. – V. 52. – P. 79–82.

67.Issitt C.H., Duckett J.B., Osborne B.M. et al. Another example of an antibody reactive optimally with p red cells // Brit. J. Haemat. – 1976. – V. 34. – P.19–23.

519

68.Issitt P.D., Anstee D.J. Applied Blood Group Serology. – 4-th ed. – Durham, NC, USA: Montgomery Sc. Publ., 1998. – 1208 p.

69.Issitt P.D., Tegoli J., Jackson V. et al.Anti-IP1: antibodies that show an association between I and Pblood group systems // Vox Sang. – 1968. – V. 14. – P. 1–8.

70.Judd W.J. A pH-dependent auto-agglutinin with anti-p specificity // Transfusion. – 1975. –

V.15. – P. 373–376.

71.JuddW.J.,SteinerE.A.,CappsR.D.Autoagglutininswithapparentanti-Pspecificityreactive only by low-ionic-strength salt techniques // Transfusion. – 1982. – V. 22. – P. 185–188.

72.Källenius G., Svenson S.B., Möllby R. et al. Structure of carbohydrate part of receptor of human uroepitelial cells for pyelonephritogenic Echerichia coli // Lancet. – 1981. – V. ii. –

P.604–606.

73.Kannagi R., Cochran N.A., Ishigami F. et al. Stage-specific embryonic antigens (SSEA-3 and-4)areepitopesofuniqueglobo-seriesgangliosideisolatedfromhumanteratocarcinoma cells // EMBO J. – 1983. – V. 2. – P. 2355–2361.

74.Kannagi R., Levine P., Watanabe K., Hakomori S. Recent studies of glycolipids and

glycoprotein profiles and characterization of the major glycolipid antigen in gastric cancer of apatientofbloodgroupphenotype(Tj a-)firststudiedin1951//CancerRes.–1982.–V.42.–

P.5249–5254.

75.Kasai K., Galton J., Terasaki P.I. et al. Tissue distribution of the P k antigen as determined by a monoclonal antibody // J. Immunogenet. – V. 12. – P. 213–220.

76.Kato M., Kubo S., Naiki M. Complement fixation anti-bodies to glycosphingolipids in sera of rare blood group p and P k phenotypes // J. Immunogenet. – 1978. – V. 5. – P. 31–40.

77.KelusA., Gurner B.W., Coombs R.R.A. Blood group antigen on HeLa cells shown by mixed agglutination // Immunology. – 1959. – V. 2. – P. 262–267.

78.Kerr J.R., McQuaid S., Coyle P.V. Expression of Pantigen in parvovirus B19 infected bone marrow // N. Engl. J. Med. – 1995. – V. 332. – P. 128.

79.Keuch J.J., Manzella S.M., Nyame K.A. et al. Cloning of Gb3 synthase, the key enzyme in globo-series glycosphingolipid synthesis, predicts a family of α1,4-glycosyltransferases conserved in plants, insects and mammals // J. Biol. Chem. – 2000. – V. 275. – P. 25315– 25321.

80.Khine A.A., Firtel M., Lingwood C.A. CD77-dependent retrograde transport of CD19 to the nuclearmembrane:functionalrelationshipbetweenCD77andCD19duringterminalcenter B-cell apoptosis // J. Cell. Physiol. – 1998. – V. 176. – P. 281–292.

81.Khoo K.-H., Nieto A., Morris H.R., Deil A. Structural characterization of the N-glycans from Echinococcus granulosis hydatid cyst membrane and protoscoleces // Mol. Biol. Parasitol. – 1997. – V. 86. – P. 237–248.

82.Kijimoto-Ochiai S., Naiki M., Makita A. Defects of glycosyltransferase activities in human fibroblastsofP k andpbloodgroupphenotypes//Proc.Nat.Acad.Sci.USA.–1977.–V.74.–

P.5407–5410.

83.Kortekangas A.E., Kaarsalo E., Melartin L. et al. The red cell antigen P k and its relationship with to the P system: the evidence of three more P k families // Vox Sang. – 1965. – V. 10. –

P.385–404.

84.KortekangasA.E., Noades J., Tippett P. et al.Asecond family with the red cell antigen P k // Vox Sang. – 1959. – V. 4. – P. 337–349.

85.KoscielakJ.,Miller-ProdrazaH.,KrauzeR.,CedergrenB.Glycolipidcompositionofblood group P// FEBS Lett. – 1976. – V. 66. – P. 250–253.

86.Kundu S.K., Evans A., Rizvi J. et al. A new P k phenotype in the P blood group system //

J.Immunogenet. – 1980. – V. 7. – P. 431–439.

87.Kundu S.K., Jovall P.-A., Chardashkani S. et al. Blood group glycosphingolipid expression

in kidney of an individual with the rare blood group A1Le(a −b + )p phenotype: absence of blood group structures based on globoseries // Glycocon. J. – 1996. – V. 13. – P. 307–313.

520