Related Experiment Video
Updated: May 29, 2026

Isolation and Characterization of Mesenchymal Stromal Cells from Human Umbilical Cord and Fetal Placenta
Published on: April 3, 2017
Identification and localization of S100A6 in human umbilical cord
Ewelina Jurewicz1, Irena Kasacka, Edward Bańkowski
1Nencki Institute of Experimental Biology, 3 Pasteur Street, 02093 Warsaw, Poland.
Insights
S100A6, a calcium-binding protein, is present in the human umbilical cord, particularly in Wharton
Area of Science:
- Biochemistry
- Cell Biology
- Developmental Biology
Background:
- S100A6 (calcyclin) is a calcium-binding protein implicated in cellular functions.
- The role and localization of S100A6 in the human umbilical cord are not well-established.
Purpose of the Study:
- To investigate the presence and localization of S100A6 in the human umbilical cord.
- To explore potential interactions of S100A6 within the umbilical cord tissue.
Main Methods:
- Immunoblotting was used to detect S100A6 in human umbilical cord tissue.
- Immunohistochemistry was employed to visualize S100A6 localization in cellular and extracellular components.
- Affinity chromatography was utilized to identify S100A6-binding proteins in Wharton's jelly.
Main Results:
- S100A6 was detected in the human umbilical cord.
- Intensive S100A6 staining was observed in blood vessel walls and Wharton's jelly.
- S100A6 was localized to myofibroblasts and the extracellular matrix (ECM) in Wharton's jelly.
- Proteins capable of binding to S100A6 were identified in Wharton's jelly.
Conclusions:
- This study confirms the presence of S100A6 in the human umbilical cord.
- S100A6 is found in both cellular and extracellular compartments of Wharton's jelly.
- These findings suggest S100A6's involvement in intra- and extracellular signaling pathways within the umbilical cord.
Abstract:
S100A6, a calcium-binding protein also known as calcyclin, was detected in human umbilical cord by immunoblotting. Immunohistochemical studies showed an intensive reaction for S100A6 in the walls of vessels and Wharton's jelly. In the latter, S100A6 was found not only in the myofibroblasts but also in the ECM (extracellular matrix) surrounding these cells. Affinity chromatography of S100A6 resin indicated that Wharton's jelly contains some proteins that could bind to S100A6. Thus these novel results show the presence of S100A6 in umbilical cord and suggest the involvement of this protein in intra- and extra-cellular signalling pathways in this tissue.

