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Collagen type VI in the human bone marrow microenvironment: a strong
cytoadhesive component
G Klein, CA Muller, E Tillet, ML Chu and R Timpl
Department of Internal Medicine, University Medical Clinic, Tubingen,
Germany.
Collagen type VI, which forms characteristic microfibrillar structures, is
assembled from three individual alpha(VI) chains that form a short triple
helix and two adjacent globular domains. Expression of all three alpha (VI)
collagen chains in the human bone marrow (BM) microenvironment could be
detected by chain-specific antibodies in tissue sections and in the
adherent stromal layer of long-term BM cultures. In functional studies,
collagen type VI was shown to be a strong adhesive substrate for various
hematopoietic cell lines and light-density BM mononuclear cells. The
adhesive site within the molecule seems to be restricted to the triple
helical domain of all three alpha (VI) chains, because individual alpha
(VI) chains were not active in the attachment assays. Adhesion of the
hematopoietic cell lines to collagen VI was dose-dependent and could be
inhibited by heparin. Although the triple helix contains several RGD
sequences, adhesion of the hematopoietic cell types to collagen VI could be
blocked neither by RGD-containing peptides nor by a neutralizing antibody
to the beta 1 integrin subunit. In combination with an antiadhesive
substrate, the binding properties of collagen VI could be downregulated.
These data suggest that this collagen type may play an important role in
the adhesion of hematopoietic cells within the BM microenvironment.
Volume 86,
Issue 5,
pp. 1740-1748,
09/01/1995
Copyright © 1995 by The American Society of Hematology
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