Document Detail


Dynamic changes in cervical glycosaminoglycan composition during normal pregnancy and preterm birth.
MedLine Citation:
PMID:  22529214     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Glycosaminoglycans (GAG) have diverse functions that regulate macromolecular assembly in the extracellular matrix. During pregnancy, the rigid cervix transforms to a pliable structure to allow birth. Quantitative assessment of cervical GAG is a prerequisite to identify GAG functions in term and preterm birth. In the current study, total GAG levels increased at term, yet the abundance, chain length, and sulfation levels of sulfated GAG remained constant. The increase in total GAG resulted exclusively from an increase in hyaluronan (HA). HA can form large structures that promote increased viscosity, hydration, and matrix disorganization as well as small structures that have roles in inflammation. HA levels increased from 19% of total GAG in early pregnancy to 71% at term. Activity of the HA-metabolizing enzyme, hyaluronidase, increased in labor, resulting in metabolism of large to small HA. Similar to mice, HA transitions from high to low molecular weight in term human cervix. Mouse preterm models were also characterized by an increase in HA resulting from differential expression of the HA synthase (Has) genes, with increased Has1 in preterm in contrast to Has2 induction at term. The Has2 gene but not Has1 is regulated in part by estrogen. These studies identify a shift in sulfated GAG dominance in the early pregnant cervix to HA dominance in term and preterm ripening. Increased HA synthesis along with hyaluronidase-induced changes in HA size in mice and women suggest diverse contributions of HA to macromolecular changes in the extracellular matrix, resulting in loss of tensile strength during parturition.
Authors:
Yucel Akgul; Roxane Holt; Mark Mummert; Ann Word; Mala Mahendroo
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-04-23
Journal Detail:
Title:  Endocrinology     Volume:  153     ISSN:  1945-7170     ISO Abbreviation:  Endocrinology     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-06-25     Completed Date:  2012-09-20     Revised Date:  2013-07-02    
Medline Journal Info:
Nlm Unique ID:  0375040     Medline TA:  Endocrinology     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3493-503     Citation Subset:  AIM; IM    
Affiliation:
Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center, Dallas Texas 75390-9032, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cervix Uteri / metabolism*
Female
Gene Expression Profiling
Gene Expression Regulation, Enzymologic
Glucuronosyltransferase / biosynthesis
Glycosaminoglycans / metabolism*
Humans
Hyaluronic Acid / metabolism
Mice
Mice, Inbred C57BL
Parturition / metabolism*
Pregnancy
Premature Birth / metabolism*
Receptors, Estrogen / metabolism
Tissue Distribution
Grant Support
ID/Acronym/Agency:
5-PO1-HD011149/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Glycosaminoglycans; 0/Receptors, Estrogen; 9004-61-9/Hyaluronic Acid; EC 2.4.1.-/HAS2 protein, human; EC 2.4.1.-/Has2 protein, mouse; EC 2.4.1.17/Glucuronosyltransferase; EC 2.4.1.17/HAS1 protein, human; EC 2.4.1.212/hyaluronan synthase
Comments/Corrections

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