Hostname: page-component-586b7cd67f-rdxmf Total loading time: 0 Render date: 2024-11-24T22:58:58.191Z Has data issue: false hasContentIssue false

Collagen Matrix Alignment Using Inkjet Printer Technology

Published online by Cambridge University Press:  01 February 2011

Sandra Deitch
Affiliation:
[email protected], Clemson University, Bioengineering, 811 Issaqueena Trail Apt. 2216, Central, SC, 29630, United States
Catherine Kunkle
Affiliation:
[email protected], Presbyterian College, Clinton, SC, 29325, United States
Xiaofeng Cui
Affiliation:
[email protected], Clemson University, Bioengineering, Clemson, SC, 29634, United States
Thomas Boland
Affiliation:
[email protected], Clemson University, Bioengineering, Clemson, SC, 29634, United States
Delphine Dean
Affiliation:
[email protected], Clemson University, Bioengineering, Clemson, SC, 29634, United States
Get access

Abstract

Collagen fiber orientation plays an important role in many cell properties and actions in vivo. Collagen and other matrix proteins are aligned in many tissues during normal functioning. For example, cardiomyocytes align in the heart to produce a synchronously beating tissue. The extra-cellular matrix environment, including collagen, is aligned along the cells. This matrix helps with cell adhesion and the alignment of the fibers also contributes to the anisotropic mechanical property of the tissue. While it is easy to replicate randomly oriented collagen in vitro, it is much more difficult to create aligned collagen matrices for cell culture. In this work, a novel inkjet printer-based collagen alignment technique was established. A 1 mg/ml rat tail collagen type I solution was printed, using a modified HP DeskJet 500 printer, onto plasma cleaned and UV sterilized glass slides. The collagen was printed in an eight line pattern, designed in Microsoft Word with 87.5 μm by 23.1 mm lines. The pattern was printed three successive times on each slide to complete the alignment. Immunofluorescence imaging of primary antibodies specific to collagen type I indicated that the heat involved in the printing process was not great enough to denature the collagen. The extent of collagen alignment was quantified using atomic force microscopy and compared to random collagen films and collagen films aligned using a mechanical scraping method. Additionally, neonatal rat cardiomyocytes were cultured on the aligned matrices. These cells require extracellular matrix alignment to maintain their in vivo-like phenotype during in vitro culture. The cells grew along the lines of collagen and coordinated beating, indicating the success of the aligned matrix. This collagen alignment technique is cheap, fast, precise, and easy to use in comparison to other current techniques. It can be used to align collagen on any type of substrate, such as a gel, which makes it a useful tool in many applications. This technique may also be used to align other extra-cellular matrix proteins and could even be used to create a three dimensional construct with varying fiber orientations.

Type
Research Article
Copyright
Copyright © Materials Research Society 2008

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1. Kleinman, H. K., Luckenbill-Edds, L., and, F. W. Cannon Sephel, G. C., Anal. Biochem. 166, 113 (1987).Google Scholar
2. Martin, G. R. and Kleinman, H. K., Hepatology. 1, 264266 (1981).Google Scholar
3. Kadler, K. E., Holmes, D. F., Trotter, J. A. and Chapman, J. A., Biochem. J. 316, 111 (1996).Google Scholar
4. Ottani, V., Martini, D., Franchi, M., Ruggeri, A. and Raspanti, M., Micron. 33, 587596 (2002).Google Scholar
5. Gelman, R. A., Williams, B. R., Piez, K. A., J. Biological Chem. 254, 180186 (1979).Google Scholar
5. Komai, Y. and Ushiki, T., Invest. Ophthalmol. Visual Sci. 32, 22442258 (1991).Google Scholar
6. Glass-Brudzinski, J., Perizzolo, D. and Brunette, D. M., J. Biomed. Mater. Res. 61, 608618 (2002).Google Scholar
7. Matsumoto, N., Horibe, S., Nakamura, N., Senda, T., Shino, K. and Ochi, T., Arch. Orthop. Trauma Surg. 117, 215221 (1998).Google Scholar
8. Borg, T. K., Rubin, K., Lundgren, E., Borg, K. and Obrink, B., Dev. Biol. 104, 8696 (1984).Google Scholar
9. Simpson, D. C., Terracio, L., Terracio, M., Price, R. L., Turner, D. C. and Borg, T. K., J. Cell Physiol. 161, 89105 (1994).Google Scholar
10. Walsh, K. B., Sweet, J. K., Parks, G. E. and Long, K. J., J. Mol. Cell Cardiol. 33, 12331247 (2001).Google Scholar
11. Lee, P., Lin, R., Moon, J. and Lee, L. P., Biomed. Microdevices. 8, 3541 (2006).Google Scholar
12. Guido, S. and Tranquillo, R. T., J. Cell Sci. 105, 317331 (1993).Google Scholar
13. Dickinson, R. B., Guido, S. and Tranquillo, R. T., Ann. Biomed. Eng. 22, 342356 (1994).Google Scholar
14. Kotani, H., Iwasaka, M., Ueno, S. and Curtis, A., J. Appl. Phys. 87, 61916193 (2000).Google Scholar
15. Torbet, J. and Ronziere, M. C., Biochem. J. 219, 10571059 (1984).Google Scholar
16. Guo, C., Kaufman, L. J., Biomaterials. 28, 11051114 (2007).Google Scholar
17. Roth, E. A., Xu, T., Das, M., Gregory, C., Hickman, J. J. and Boland, T., Biomaterials. 25, 37073715 (2004).Google Scholar
18. Hartgerink, J.D., Beniash, E., Stupp, S. I., Science, 294, 16841688 (2001)Google Scholar
19. Nakamura, M., Kobayashi, A., Takagi, F., Watanabe, A., Hiruma, Y., Ohuchi, K., Iwasaki, Y., Horie, M., Morita, I. and Takatani, S., Tissue Engineering. 11, 16581666 (2005).Google Scholar
20. Pardo, L., Wilson, W. C. and Boland, T., Langmuir. 19, 14621466 (2003).Google Scholar
21. Gay, S. and Fine, J. D., Methods in Enzymology. 145, 148167 (1987).Google Scholar