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Updated: Jul 24, 2026

Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
Published on: April 21, 2017
Identification of the major proteoglycans from human myometrium
A Hjelm1, G Ekman-Ordeberg, K Barchan
1Department of Woman and Child Health, Division for Obstetrics and Gynecology, Karolinska Institute/Karolinska Hospital, Stockholm, Sweden.
Background:
During pregnancy and parturition a remodeling within the extracellular matrix of the cervix and the corpus uteri occurs, which is of fundamental importance to a normal labor. The aim of this study is to identify the major proteoglycans in corpus uteri of non-pregnant subjects.
Methods:
From human uterine tissue proteoglycans were extracted and purified using CsCl-density gradient centrifugation, gel and ion-exchange chromatography. The proteoglycans were quantified and identified by Alcian Blue before and after ABC-digestion and by Western blotting.
Results:
The results showed that the corpus uteri contains a substantial amount of proteoglycans, 1.825 microg/mg wet weight. Decorin is dominating, constituting 63% of the total amount of proteoglycans. Heparan sulphate proteoglycans accounted for 20% and biglycan for 16%. Less than 1% consisted of the large proteoglycan versican.
Conclusions:
Further investigations must be performed to provide more information of the biological role of the proteoglycans in the uterus, especially during labor, by the presence of heparan sulphate proteoglycans and the minute presence of versican which indicate that the proteoglycan composition and organization is different to that of the cervix.
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