MMP-2 and MMP-9 and their tissue inhibitor in preterm human milk

Ronit Lubetzky1, Dror Mandel, Francis B Mimouni

  • 1Department of Pediatrics, Tel Aviv Sourasky Medical Center, Tel Aviv, Israel.

Abstract

Insights

Human milk contains matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). TIMP-1 levels were higher and increased over time in preterm infant milk compared to term infant milk.

Area of Science:

  • Biochemistry
  • Neonatal research
  • Immunology

Background:

  • Matrix metalloproteinases (MMPs) degrade extracellular matrix.
  • Tissue inhibitors of metalloproteinases (TIMPs) are natural MMP inhibitors.
  • MMPs may contribute to tissue damage in necrotizing enterocolitis.

Purpose of the Study:

  • To compare matrix metalloproteinase (MMP) activity and tissue inhibitor of metalloproteinase (TIMP-1) expression in human milk (HM) for preterm and term infants.
  • To investigate temporal changes in MMPs and TIMP-1 in HM from both groups.

Main Methods:

  • Prospective observational study.
  • Compared MMP-2, MMP-9, and TIMP-1 in HM from 18 preterm and 13 term infants.
  • Collected samples at 72 hours, 1 week, and 2 weeks postpartum.

Main Results:

  • MMP-2 and MMP-9 activities were similar between preterm and term HM and did not change over time.
  • TIMP-1 was significantly higher in preterm HM compared to term HM.
  • TIMP-1 expression increased significantly over time in preterm HM only.

Conclusions:

  • Significant differences exist in TIMP-1 expression between preterm and term infant milk.
  • TIMP-1 expression in preterm HM changes from colostrum to mature milk.