Properties of the Collagen Type XVII Ectodomain

  • Areida S
  • Reinhardt D
  • Müller P
  • et al.
N/ACitations
Citations of this article
6Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

Collagen XVII is a transmembrane component of hemidesmosomal cells with important functions in epithelial-basement membrane interactions. Here we report on properties of the extracellular ectodomain of collagen XVII, which harbors multiple collagenous stretches. We have recombinantly produced subdomains of the collagen XVII ectodomain in a mammalian expression system. rColXVII-A spans the entire ectodomain from δNC16a to NC1, rColXVII-B is similar but lacks the NC1 domain, a small N-terminal polypeptide rColXVII-C encompasses domains δNC16a to C15, and a small C-terminal polypeptide rColXVII-D comprises domains NC6 to NC1. Amino acid analysis of rColXVII-A and -C demonstrated prolyl and lysyl hydroxylation with ratios for hydroxyproline/proline of 0.4 and for hydroxylysine/lysine of 0.5. A small proportion of the hydroxylysyl residues in rColXVII-C (∼3.3%) was glycosylated. Limited pepsin and trypsin degradation assays and analyses of circular dichroism spectra clearly demonstrated a triple-helical conformation for rColXVII-A, -B, and -C, whereas the C-terminal rColXVII-D did not adopt a triple-helical fold. These results were further substantiated by electron microscope analyses, which revealed extended molecules for rColXVII-A and -C, whereas rColXVII-D appeared globular. Thermal denaturation experiments revealed melting temperatures of 41 °C (rColXVII-A), 39 °C (rColXVII-B), and 35 °C (rColXVII-C). In summary, our data suggest that triple helix formation in the ectodomain of ColXVII occurs with an N- to C-terminal directionality.

Cite

CITATION STYLE

APA

Areida, S. K., Reinhardt, D. P., Müller, P. K., Fietzek, P. P., Köwitz, J., Marinkovich, M. P., & Notbohm, H. (2001). Properties of the Collagen Type XVII Ectodomain. Journal of Biological Chemistry, 276(2), 1594–1601. https://doi.org/10.1074/jbc.m008709200

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free