Skip to main content
PMC home page
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 1991 May 2;113(4):971–978. doi: 10.1083/jcb.113.4.971

Two type XII-like collagens localize to the surface of banded collagen fibrils

PMCID: PMC2288986  PMID: 2026656

Abstract

Two recently identified collagen molecules, termed twelve-like A and twelve-like B (TL-A and TL-B) have properties similar to type XII collagen. These molecules have been localized in human and calf tissues by immunoelectron microscopy. The observations strongly suggest that both molecules are located along the surface of banded collagen fibers. The epitopes recognized by the antibodies are contained in large, nontriple-helical domains at one end of the collagen helix. The epitopes are visualized at a distance from the surface of the banded fibers roughly equal to the length of the nonhelical domains, suggesting that the nonhelical domains extend from the fibril, while the triple-helical domains are likely to bind directly to the fibril surface. Occasionally, both TL-A and TL-B demonstrate periodic distribution along the fibril surface. The period corresponds to the primary interband distance of the banded fibrils. Not all fibrils in a fiber bundle are labeled, nor is the labeling continuous along the length of labeled fibrils. Simultaneous labeling of TL-A and type VI collagen only rarely shows colocalization, suggesting that TL-A and TL- B do not mediate interactions between the type VI collagen beaded filaments and banded collagen fibrils. Also, interfibrillar distances are approximately equivalent in the presence and absence of these type XII-like molecules. While the results do not directly indicate a specific function for these molecules, the localization at the fibril surface suggests that they mediate interactions between the fibrils and other matrix macromolecules or with cells.

Full Text

The Full Text of this article is available as a PDF (4.0 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Birk D. E., Fitch J. M., Babiarz J. P., Linsenmayer T. F. Collagen type I and type V are present in the same fibril in the avian corneal stroma. J Cell Biol. 1988 Mar;106(3):999–1008. doi: 10.1083/jcb.106.3.999. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Dublet B., Oh S., Sugrue S. P., Gordon M. K., Gerecke D. R., Olsen B. R., van der Rest M. The structure of avian type XII collagen. Alpha 1 (XII) chains contain 190-kDa non-triple helical amino-terminal domains and form homotrimeric molecules. J Biol Chem. 1989 Aug 5;264(22):13150–13156. [PubMed] [Google Scholar]
  3. Dublet B., van der Rest M. Type XII collagen is expressed in embryonic chick tendons. Isolation of pepsin-derived fragments. J Biol Chem. 1987 Dec 25;262(36):17724–17727. [PubMed] [Google Scholar]
  4. Engvall E., Hessle H., Klier G. Molecular assembly, secretion, and matrix deposition of type VI collagen. J Cell Biol. 1986 Mar;102(3):703–710. doi: 10.1083/jcb.102.3.703. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Eyre D. R., Apon S., Wu J. J., Ericsson L. H., Walsh K. A. Collagen type IX: evidence for covalent linkages to type II collagen in cartilage. FEBS Lett. 1987 Aug 17;220(2):337–341. doi: 10.1016/0014-5793(87)80842-6. [DOI] [PubMed] [Google Scholar]
  6. Gordon M. K., Gerecke D. R., Dublet B., van der Rest M., Olsen B. R. Type XII collagen. A large multidomain molecule with partial homology to type IX collagen. J Biol Chem. 1989 Nov 25;264(33):19772–19778. [PubMed] [Google Scholar]
  7. Gordon M. K., Gerecke D. R., Dublet B., van der Rest M., Sugrue S. P., Olsen B. R. The structure of type XII collagen. Ann N Y Acad Sci. 1990;580:8–16. doi: 10.1111/j.1749-6632.1990.tb17913.x. [DOI] [PubMed] [Google Scholar]
  8. Gordon M. K., Gerecke D. R., Olsen B. R. Type XII collagen: distinct extracellular matrix component discovered by cDNA cloning. Proc Natl Acad Sci U S A. 1987 Sep;84(17):6040–6044. doi: 10.1073/pnas.84.17.6040. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Keene D. R., Engvall E., Glanville R. W. Ultrastructure of type VI collagen in human skin and cartilage suggests an anchoring function for this filamentous network. J Cell Biol. 1988 Nov;107(5):1995–2006. doi: 10.1083/jcb.107.5.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Keene D. R., Sakai L. Y., Burgeson R. E. Human bone contains type III collagen, type VI collagen, and fibrillin: type III collagen is present on specific fibers that may mediate attachment of tendons, ligaments, and periosteum to calcified bone cortex. J Histochem Cytochem. 1991 Jan;39(1):59–69. doi: 10.1177/39.1.1983874. [DOI] [PubMed] [Google Scholar]
  11. Keene D. R., Sakai L. Y., Bächinger H. P., Burgeson R. E. Type III collagen can be present on banded collagen fibrils regardless of fibril diameter. J Cell Biol. 1987 Nov;105(5):2393–2402. doi: 10.1083/jcb.105.5.2393. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lunstrum G. P., Morris N. P., McDonough A. M., Keene D. R., Burgeson R. E. Identification and partial characterization of two type XII-like collagen molecules. J Cell Biol. 1991 May;113(4):963–969. doi: 10.1083/jcb.113.4.963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lunstrum G. P., Sakai L. Y., Keene D. R., Morris N. P., Burgeson R. E. Large complex globular domains of type VII procollagen contribute to the structure of anchoring fibrils. J Biol Chem. 1986 Jul 5;261(19):9042–9048. [PubMed] [Google Scholar]
  14. Mendler M., Eich-Bender S. G., Vaughan L., Winterhalter K. H., Bruckner P. Cartilage contains mixed fibrils of collagen types II, IX, and XI. J Cell Biol. 1989 Jan;108(1):191–197. doi: 10.1083/jcb.108.1.191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Müller-Glauser W., Humbel B., Glatt M., Sträuli P., Winterhalter K. H., Bruckner P. On the role of type IX collagen in the extracellular matrix of cartilage: type IX collagen is localized to intersections of collagen fibrils. J Cell Biol. 1986 May;102(5):1931–1939. doi: 10.1083/jcb.102.5.1931. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Olsen B. R. The next frontier: molecular biology of extracellular matrix. Connect Tissue Res. 1989;23(2-3):115–121. doi: 10.3109/03008208909002411. [DOI] [PubMed] [Google Scholar]
  17. REYNOLDS E. S. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol. 1963 Apr;17:208–212. doi: 10.1083/jcb.17.1.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Sakai L. Y., Keene D. R., Morris N. P., Burgeson R. E. Type VII collagen is a major structural component of anchoring fibrils. J Cell Biol. 1986 Oct;103(4):1577–1586. doi: 10.1083/jcb.103.4.1577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sugrue S. P., Gordon M. K., Seyer J., Dublet B., van der Rest M., Olsen B. R. Immunoidentification of type XII collagen in embryonic tissues. J Cell Biol. 1989 Aug;109(2):939–945. doi: 10.1083/jcb.109.2.939. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Vaughan L., Mendler M., Huber S., Bruckner P., Winterhalter K. H., Irwin M. I., Mayne R. D-periodic distribution of collagen type IX along cartilage fibrils. J Cell Biol. 1988 Mar;106(3):991–997. doi: 10.1083/jcb.106.3.991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Vaughan L., Winterhalter K. H., Bruckner P. Proteoglycan Lt from chicken embryo sternum identified as type IX collagen. J Biol Chem. 1985 Apr 25;260(8):4758–4763. [PubMed] [Google Scholar]
  22. van der Rest M., Mayne R. Type IX collagen proteoglycan from cartilage is covalently cross-linked to type II collagen. J Biol Chem. 1988 Feb 5;263(4):1615–1618. [PubMed] [Google Scholar]

Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES