Escherichia coli induced matrix metalloproteinase-9 activity and type IV collagen degradation is regulated by progesterone in human maternal decidual

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2024年10月4日

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Gerardo Bautista-Bautista,
Santos Salguero-Zacarias,
Graciela Villeda-Gabriel,
Guadalupe García-López,
Mauricio Osorio-Caballero,
Martha Leticia Palafox-Vargas,
Ricardo Josué Acuña-González,
Irlando Lara-Pereyra,
Oscar Díaz-Ruíz,
Hector Flores-Herrera

摘要

Background

Escherichia coli (E. coli) is one of the main bacteria associated with preterm premature rupture of membranes by increasing pro-matrix metalloproteinase 9 (proMMP-9) and degradation of type IV collagen in human feto-maternal interface (HFMi). proMMP-9 is regulated by progesterone (P4) but it is unclear whether P4 inhibits proMMP in human maternal decidual (MDec). This study aimed to determine a role of P4 on proMMP-2 and − 9 and type IV collagen induced by E. coli infection in MDec.

Methods

Nine HFMi were mounted in a Transwell system. MDec was stimulated with P4 or E. coli for 3-, 6-, or 24-hours. proMMP-2, -9 and type IV collagen were assessed.

Results

Gelatin zymography revealed an increase in proMMP-9 after 3, 6, and 24 h of stimulating MDec with E. coli. Using immunofluorescence, it was confirmed the increase in the HFMi tissue and a reduction on the amount of type IV collagen leading to the separation of fetal amniochorion and MDEc. The degradative activity of proMMP-9 was reduced by 20% by coincubation with P4.

Conclusions

P4 modulates the activity of proMMP-9 induced by E. coli stimulation but it was unable to completely reverse the degradation of type IV collagen in human MDec tissue.