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. Author manuscript; available in PMC: 2015 Jan 1.
Published in final edited form as: Matrix Biol. 2013 Aug 15;33:47–53. doi: 10.1016/j.matbio.2013.08.003

Figure 3. Collagen V is tethered to the cell surface by HS GAG-independent interactions.

Figure 3

(A, E) The collagen V in the cultured cells is processed and in the mature form. (A) Further, presence of the α1 collagen V band in cell-surface biotinylated or “+ bio” (and absence in unbiotinylated or “− bio”) material from a streptavidin pull-down indicates that collagen V is a cell surface molecule of tendon fibroblasts. (B)This material is also shown blotted with streptavidin-HRP to show the full labeled complement of the numerous cell surface molecules. We further see that HS chains are not responsible for retaining collagen V at the cell surface; (C, D) even with efficient digestion of HS chains, as evidenced by reaction of the digested HSPGs perlecan (pericellular) and syndecan-1 (integral to the membrane) in panel C with the Δ-HS stub antibody in blot D, collagen V is still retained in the cell layer (panel E). Demarcations between panels indicate different exposures of a single gel to optimize signal for a specific protein. Separately bordered panels indicate different gels.