The effects of genetic and seasonal factors on reproductive success

Fertility and Sterility

Volumn 89, Issue 5, 2008, Pages 1090-1094

  Gloria Bottini, Fulvia ^a   Bottini, Nunzio ^a   La Torre, Mauro ^b   Magrini, Andrea ^a   Bergamaschi, Antonio ^c   Bottini, Egidio ^a  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

^b S Massimo Hospital   (Italy)

^c CATHOLIC UNIVERSITY   (Italy)

Author keywords

ACP1; environment; haptoglobin; Human fertility; solar cycle

Indexed keywords

ACP1 ENZYME; HAPTOGLOBIN; PROTEIN TYROSINE PHOSPHATASE;

ARTICLE; CONCEPTION; CONTROLLED STUDY; FEMALE; GENETIC ANALYSIS; GENETIC POLYMORPHISM; HOMOZYGOSITY; HUMAN; PHENOTYPE; PRIORITY JOURNAL; REPRODUCTION; SEASONAL VARIATION; SOLAR CYCLE;

FEMALE; FERTILITY; FERTILIZATION; HAPTOGLOBINS; HUMANS; ITALY; PHENOTYPE; POLYMORPHISM, GENETIC; PREGNANCY; PROTEIN TYROSINE PHOSPHATASES; PROTO-ONCOGENE PROTEINS; SEASONS;

EID: 43649093519     PISSN: 00150282     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fertnstert.2007.04.030     Document Type: Article

References (33)

1. Casper R.F., Erskin H.T., Armstrong D.T., Brown S.E., Daniel S.A., Graves G.R., et al. In vitro fertilization: diurnal and seasonal variation in luteinizing hormone surge onset and pregnancy rates. Fertil Steril 49 (1988) 644-648
2. Jongbloet P.H. Seasonal fluctuation of pathological and optimum conceptions, maternal sub-fecundity, gender dimorphism and survival. Coll Anthropol 16 (1992) 99-107
3. Gloria-Bottini F., Lucarini N., and La Torre M. Birth dates. Nature 379 (1996) 395
4. Gloria-Bottini F., Lucarini N., Palmarino R., La Torre M., Amante A., and Bottini E. ACP1 and human adaptability. II. Association with season of conception. Hum Genet 101 (1997) 158-164
5. Bottini E., Gloria-Bottini F., and Borgiani P. ACP1 and human adaptability. I. Association with common diseases: a case-control study. Hum Genet 96 (1995) 629-637
6. Bottini N., Bottini E., Gloria-Bottini F., and Mustelin T. Low-molecular-weight protein tyrosine phosphatase and human disease: in search of biochemical mechanisms. Archivum Immunologiae et Therapiae Experimentalis 50 (2002) 95-104
7. Smithies O. Zone electrophoresis in starch gels: grouped variations in the serum proteins of normal human adults. Biochem J 61 (1955) 629-641
8. Langlois M.R., and Delanghe J.R. Biological and clinical significance of haptoglobin polymorphism in humans. Clin Chem 42 (1996) 1589-1600
9. Javid J. The effect of haptoglobin-polymer size on haemoglobin binding capacity. Vox Sang 10 (1965) 320-325
10. Maeda N. DNA polymorphisms in the controlling region of the human haptoglobin genes: a molecular explanation for the haptoglobin 2-1 modified phenotype. Am J Hum Genet 49 (1991) 158-166
11. Jue D.M., Shim B.S., and Kang Y.S. Inhibition of prostaglandin synthase activity of sheep seminal vesicular gland by human serum haptoglobin. Mol Cell Biochem 51 (1983) 141-147
12. Miller Y.I., Altamentova S.M., and Shaklai N. Oxidation of low density lipoprotein by hemoglobin stems from a heme-initiated globin radical: antioxidant role of haptoglobin. Biochemistry 36 (1997) 12189-12198
13. Arredouani M., Matthijs P., Van Hoeyveld E., Kasran A., Baumann H., Ceuppens J.L., et al. Haptoglobin directly affects T cell and suppresses T helper cell type 2 cytokine release. Immunology 108 (2003) 144-151
14. Moison R.M.W., Palinckkx J.J.S., Roest M., Houdkamp E., and Berger H.M. Induction of lipid peroxidation of pulmonary surfactant by plasma of preterm babies. Lancet 341 (1993) 79-82
15. Bottini N., Gimelfarb A., Gloria-Bottini F., La Torre M., Lucarelli P., and Lucarini N. Haptoglobin genotype and natural fertilità in humans. Fertil Steril 72 (1999) 293-296
16. Hopkinson D.A., Spencer N., and Harris H. Red cell acid phosphatise variants: a new human polymorphism. Nature 199 (1963) 969-971
17. Ramponi G., Ruggiero M., Raugei G., Berti A., Modesti A., Degl'Innocenti D., et al. Overexpression of a synthetic phosphotyrosine protein phosphatase gene inhibits normal and transformed cell growth. Int J Cancer 51 (1992) 652-656
18. Ruggiero M., Pazzagli C., Rigacci S., Magnelli L., Raugei G., Berti A., et al. Negative growth control by a novel low Mr phosphotyrosine protein phosphatase in normal and transformed cells. FEBS Lett 326 (1993) 294-298
19. Berti A., Rigacci S., Raugei G., Degl'Innocenti D., and Ramponi G. Inhibition of cellular response to platelet-derived growth factor by low Mr phosphotyrosine protein phosphatase overexpression. FEBS Lett 349 (1994) 7-12
20. Chiarugi P., Cirri P., Marra F., Raugei G., Camici G., Manao G., et al. LMW-PTP is a negative regulator of insulin-mediated mitotic and metabolic signalling. Biochem Biophys Res Commun 238 (1997) 676-682
21. Ramponi G., Manao G., Camici G., Cappugi G., Ruggiero M., and Bottaro D.P. The 18kDa cytosolic acid phosphatase from bovine liver has phosphotyrosine phosphatase activity on the autophosphorylated epidermal growth factor receptor. FEBS Lett 250 (1989) 469-473
22. Stein E., Lane A.A., Cerretti D.P., Scoecklmann H.O., Schroff A.D., Van Etten R.L., et al. Eph receptors discriminate specific ligand oligomers to determine alternative signalling complexes, attachment, and assembly responses. Genes Dev (1998) 12:667-78
23. Bottini N., Stefanini L., Williams S., Alonso A., Merlo J., Jascur T., et al. Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMPTP). J Biol Chem 277 (2002) 24220-24224
24. Rigacci S., Degl'Innocenti D., Bucciantini M., Cirri P., Berti A., and Ramponi G. pp60v-src phosphorylates and activates low molecular weight phosphotyrosine-protein phosphatase. J Biol Chem 271 (1996) 1278-1281
25. Tailor P., Williams S., Gilman J., Couture C., and Mustelin T. Regulation of the low molecular weight phosphotyrosine phosphatase (LMPTP) by phosphorylation at tyrosines 131 and 132. J Biol Chem 272 (1997) 5371-5376
26. Boivin P., and Galand C. The human red cell acid phosphatase is a phosphotyrosine protein phosphatase which dephosphorylates the membrane protein band 3. Biochem Biophys Res Commun 134 (1986) 557-564
27. Low P.S., Allen D.P., Zioncheck T.F., Charl P., Will-Ardson B.M., Geahlen R.L., et al. Tyrosine phosphorylation of band 3 inhibits peripheral protein binding. J Biol Chem 262 (1987) 4592-4596
28. Harrison M.L., Rathnavelu P., Arese P., Geaklen R.L., and Low P.S. Role of band 3 tyrosine phosphorylation in the regulation of erythrocyte glycolysis. J Biol Chem 266 (1991) 4106-4111
29. Stefani M., Caselli A., Bucciantini M., Pazzagli L., Dolfi F., Camici G., et al. Dephosphorylation of tyrosine phosphorylated synthetic peptides by rat liver phosphotyrosine protein phosphatase isoenzymes. FEBS Lett 326 (1993) 131-134
30. Chen Z., Godfrey-Bailey L., Schiff I., and Hauser R. Impact of seasonal variation, age and smoking status on human semen parameters: the Massachusetts General Hospital experience. J Exp Clin Assist Reprod 1 (2004) 2
31. Boivin B.D., Duffy J.F., Kronauer R.E., and Czeisker C.A. Dose-response relationships for resetting of human circadian clock by light. Nature 379 (1996) 540-542
32. Berkova N., Lemay A., De Grandprè P., Goupil S., and Maheux R. Immunoblot detection of decreased antibodies to haptoglobin-like protein in the serum of infertile women with or without endometriosis. Biol Reprod 57 (1997) 178-185
33. Olson G.E., Winfrey V.P., Matrisian P.E., Melner M.H., and Hoffman L.H. Specific expression of haptoglobin mRNA in implantation-stage rabbit uterine epithelium. J Endocrinol 152 (1997) 69-80