Identification of t-PA as the Major Active Plasminogen Activator in Human Milk

 

PDF Download Buy Article Permissions and Reprints

Summary

Human colostrum and milk contain high levels of plasminogen activator when compared with blood. These levels are inversely related to the duration of lactation and the activity appears to be due to tissue type plasminogen activator present in multiple (65-190 Kd) molecular weight forms.

• References

• 1 Astrup T, Stemdorff I. A fibrinolytic system in human milk. Pro Soc Exp Biol Med 1953; 84: 605-609
  CrossrefPubMedGoogle Scholar
• 2 Horie N, Okamoto U, Ogawa C. Studies on the plasminogen activating system in human milk. VI. Differences in properties between milk activator and glandular kallikrein. Nippon Ketsueki Gakki Zasshi 1982; 45: 1099-1106
  PubMedGoogle Scholar
• 3 Okamoto U, Horie N, Nagamatsu Y, Yamamoto J. Distribution of plasminogen activator in human milk samples collected at various days after delivery. Acta Haematol Jap 1980; 43: 743-746
  PubMedGoogle Scholar
• 4 Okamoto U, Horie N, Nagamatsu Y, Yamamoto JI. Plasminogen activator in human early milk: its partial purification and characterisation. Thromb Haemostas 1981; 45: 121-126
  PubMedGoogle Scholar
• 5 Reiner GC, Katzenellenbogen BS, Bindal RD, Katzellenbogen JA. Biological activity and receptor binding activity of a strongly interacting estrogen in human breast cancer cells. Cancer Research 1984; 44: 2302-2308
  PubMedGoogle Scholar
• 6 Huff KK, Lippman ME. Hormonal control of plasminogen activator secretion in ZR 75-1 human breast cancer cells in culture. Endocrinology 1984; 114: 1702-1710
  CrossrefPubMedGoogle Scholar
• 7 Isotalo H, Tryggvason K, Vierikko P, Kauppila A, Vihko R. Plasminogen activators and steroid receptor concentrations in normal, benign, and malignant breast and ovarian tissue. Anticancer Res 1983; 3: 331-335
  PubMedGoogle Scholar
• 8 Butler WB, Kirkland WL, Gargala TL, Goran N, Kelsey WH, Berlinski PJ. Steroid stimulation of plasminogen activator production in a human breast cancer cell line (MCF-7). Cancer Res 1983; 43: 1637-1641
  PubMedGoogle Scholar
• 9 Reich E. Activation of plasminogen: a general mechanism for producing extracellular proteolysis. In: Molecular basis of biological degradative processes Berlin RD. et al (eds) Academic Press; New York: 1977: 155-169
• 10 Evers JL, Patel J, Madeja JM, Schneider SL, Hobika GH, Camiolo SM, Markus G. Plasminogen activator activity and composition in human breast cancer. Cancer Research 1982; 42: 219-226
  PubMedGoogle Scholar
• 11 Astrup T, Mullertz S. The fibrin plate method for estimating fibrinolytic activity. Arch Biochem Biophys 1952; 1940: 346-351
  PubMedGoogle Scholar
• 12 Granelli-Piperno A, Reich E. A study of proteases and protease-inhibitor complexes in biological fluids. J Exp Med 1978; 148: 223-234
  CrossrefPubMedGoogle Scholar
• 13 Verheijen JH, Chang GT, Kluft C. Evidence for the occurrence of a fast acting inhibitor for tissue type plasminogen activator in human plasma. Thromb Haemostas 1984; 51: 392-395
  PubMedGoogle Scholar
• 14 Thorsen S, Philips M. Isolation of tissue type plasminogen activator inhibitor complexes from human plasma: Evidence for a rapid plasminogen activator inhibitor. Biochim Biophys Acta 1984; 802: 111-118
  CrossrefPubMedGoogle Scholar
• 15 Cederholm-Williams SA. Molecular biology of plasminogen activators and recombinant DNA technology. BioEssays 1984; 1: 168-173
  CrossrefPubMedGoogle Scholar