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Collagen type VI in the human bone marrow microenvironment: a strong cytoadhesive component
G Klein1, C A Müller, E Tillet
1Department of Internal Medicine, University Medical Clinic, Tübingen, Germany.
Blood
|September 1, 1995
Summary
Collagen type VI supports hematopoietic cell adhesion in human bone marrow (BM). Its triple helical domain is crucial for this interaction, suggesting a role in regulating cell attachment within the BM microenvironment.
Area of Science:
- Biochemistry
- Cell Biology
- Hematology
Background:
- Collagen type VI is a microfibrillar protein assembled from three alpha(VI) chains.
- It consists of a short triple helix and two globular domains.
Purpose of the Study:
- To investigate the expression and function of collagen type VI in the human bone marrow (BM) microenvironment.
- To determine the role of collagen type VI in hematopoietic cell adhesion.
Main Methods:
- Detection of alpha(VI) collagen chains using chain-specific antibodies in tissue sections and BM cultures.
- Functional studies assessing the adhesive properties of collagen type VI for hematopoietic cells.
- Inhibition assays using RGD peptides, anti-beta 1 integrin antibodies, and heparin.
Main Results:
- All three alpha(VI) collagen chains were expressed in the human BM microenvironment.
- Collagen type VI served as a strong adhesive substrate for hematopoietic cell lines and mononuclear cells.
- The triple helical domain, not individual chains, mediated adhesion.
- Adhesion was dose-dependent, inhibitable by heparin, but not by RGD peptides or anti-beta 1 integrin antibodies.
- Binding was downregulated when combined with an antiadhesive substrate.
Conclusions:
- Collagen type VI plays a significant role in hematopoietic cell adhesion within the BM microenvironment.
- The triple helical domain of collagen type VI is critical for this adhesive function.
- This interaction may be important for regulating hematopoietic cell localization and function in the BM.