Document Detail


Cervical softening during pregnancy: regulated changes in collagen cross-linking and composition of matricellular proteins in the mouse.
MedLine Citation:
PMID:  21248285     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A greater understanding of the parturition process is essential in the prevention of preterm birth, which occurs in 12.7% of infants born in the United States annually. Cervical remodeling is a critical component of this process. Beginning early in pregnancy, remodeling requires cumulative, progressive changes in the cervical extracellular matrix (ECM) that result in reorganization of collagen fibril structure with a gradual loss of tensile strength. In the current study, we undertook a detailed biochemical analysis of factors in the cervix that modulate collagen structure during early mouse pregnancy, including expression of proteins involved in processing of procollagen, assembly of collagen fibrils, cross-link formation, and deposition of collagen in the ECM. Changes in these factors correlated with changes in the types of collagen cross-links formed and packing of collagen fibrils as measured by electron microscopy. Early in pregnancy there is a decline in expression of two matricellular proteins, thrombospondin 2 and tenascin C, as well as a decline in expression of lysyl hydroxylase, which is involved in cross-link formation. These changes are accompanied by a decline in both HP and LP cross-links by gestation Days 12 and 14, respectively, as well as a progressive increase in collagen fibril diameter. In contrast, collagen abundance remains constant over the course of pregnancy. We conclude that early changes in tensile strength during cervical softening result in part from changes in the number and type of collagen cross-links and are associated with a decline in expression of two matricellular proteins thrombospondin 2 and tenascin C.
Authors:
Meredith L Akins; Katherine Luby-Phelps; Ruud A Bank; Mala Mahendroo
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2011-01-19
Journal Detail:
Title:  Biology of reproduction     Volume:  84     ISSN:  1529-7268     ISO Abbreviation:  Biol. Reprod.     Publication Date:  2011 May 
Date Detail:
Created Date:  2011-04-21     Completed Date:  2011-08-23     Revised Date:  2013-06-30    
Medline Journal Info:
Nlm Unique ID:  0207224     Medline TA:  Biol Reprod     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1053-62     Citation Subset:  IM    
Affiliation:
Department of Obstetrics and Gynecology, The Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, TX, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cervical Ripening / metabolism*
Collagen / chemistry*,  genetics,  metabolism*,  ultrastructure
Extracellular Matrix Proteins / chemistry,  metabolism*,  ultrastructure
Female
Fibrillar Collagens / chemistry,  genetics,  metabolism,  ultrastructure
Gene Expression Regulation, Developmental
Isoenzymes / genetics,  metabolism
Mice
Mice, 129 Strain
Mice, Inbred C57BL
Microscopy, Electron, Transmission
Pregnancy
Pregnancy Proteins / chemistry*,  genetics,  metabolism*,  ultrastructure
Procollagen / chemistry,  genetics,  metabolism,  ultrastructure
Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase / genetics,  metabolism
Protein Processing, Post-Translational
RNA, Messenger / metabolism
Tenascin / genetics,  metabolism
Thrombospondins / genetics,  metabolism
Grant Support
ID/Acronym/Agency:
R01 HD043154/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Extracellular Matrix Proteins; 0/Fibrillar Collagens; 0/Isoenzymes; 0/Pregnancy Proteins; 0/Procollagen; 0/RNA, Messenger; 0/Tenascin; 0/Thrombospondins; 0/thrombospondin 2; 9007-34-5/Collagen; EC 1.14.11.4/Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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