Collagenase activity in cervical tissue of the non-pregnant and pregnant human cervix.
Collagen degradation has been suggested to play an important role in the process of cervical ripening at term. After giving informed consent tissue samples were taken from the posterior lip of 10 non-pregnant women of child-bearing age, 10 women having a termination of pregnancy at 9-12 weeks' gestation and 12 women who had had normal spontaneous deliveries at term. Collagenase activity was measured by a specific technique using native, triple helical collagen. Proteolytic activity was determined with commercially available 14C-methaemoglobin as substrate. For identification of collagen fragments SDS-polyacrylamid-gel-electrophoresis was performed using a modified Laemmli-technique. Collagenase and protease activity were found in all extracts of the different groups. There was a marked increase in enzymatic activities in the postpartum tissue samples suggesting that significant collagen breakdown had taken place. The absence of typical collagen fragments in the SDS-electrophoresis seemed to be due to a very rapid further degradation of the fragments by proteases into small peptides which then readily left the cervix. The present findings confirm the essential role of proteolytic enzymes in cervical dilatation at term.
Rath
W
W
Department of Obstetrics and Gynaecology, University of Goettingen, FRG.
Adelmann-Grill
B C
BC
Pieper
U
U
Kuhn
W
W
Osmers
R
R
D000328:Adult; D002584:Cervix Uteri / Q000201:enzymology*; D003094:Collagen / Q000302:isolation & purification; D005260:Female; D006801:Humans; D003012:Microbial Collagenase / Q000378:metabolism*; D008970:Molecular Weight; D011247:Pregnancy / Q000378:metabolism*; D011261:Pregnancy Trimester, First; D012016:Reference Values
D003094:Collagen; D003012:Microbial Collagenase