Cell binding properties of collagen type XIV for human hematopoietic cells.

Abstract

Collagen XIV, which belongs to the subclass of fibril-associated collagens with interrupted triple helices (FACITs), is a homotrimeric molecule consisting of three alpha 1 (XIV) chains. Collagen type XIV is strongly expressed in the native human bone marrow, as shown by immunofluorescence staining and immunoblotting with an affinity-purified antibody. Hematopoietic cell lines of myeloid (KG1a, U937, K562) and lymphoid (U266, IM-9) origin were able to attach firmly to purified human collagen XIV preparations. Attachment of these cells was shown to be concentration-dependent. However, other hematopoietic cell lines tested were unable to adhere to collagen XIV, indicating restriction of this cellular interaction. The cellular receptors involved in cell binding to collagen type XIV are probably membrane-bound heparansulfate proteoglycans, since only the the addition of heparin inhibited attachment of the hematopoietic cells to collagen XIV in a concentration-dependent manner. Antibodies against the beta 1-integrin subunit could not interfere with binding to collagen type XIV. Using purified fragments of collagen XIV, it could be demonstrated that at least two different heparin-sensitive adhesion sites are present in the N-terminal globular domain and in the triple-helical domain. These data indicate that collagen XIV represents another collagen type expressed in human bone marrow with strong cell binding properties for defined populations of hematopoietic cells.