Skip to main content Accessibility help
×
Home
Hostname: page-component-79b67bcb76-c2bf7 Total loading time: 0.189 Render date: 2021-05-16T10:02:59.537Z Has data issue: true Feature Flags: { "shouldUseShareProductTool": true, "shouldUseHypothesis": true, "isUnsiloEnabled": true, "metricsAbstractViews": false, "figures": false, "newCiteModal": false, "newCitedByModal": true, "newEcommerce": true }

Collagen Matrix Alignment Using Inkjet Printer Technology

Published online by Cambridge University Press:  01 February 2011

Sandra Deitch
Affiliation:
sdeitch@clemson.edu, Clemson University, Bioengineering, 811 Issaqueena Trail Apt. 2216, Central, SC, 29630, United States
Catherine Kunkle
Affiliation:
cakunkle@mail.presby.edu, Presbyterian College, Clinton, SC, 29325, United States
Xiaofeng Cui
Affiliation:
xiaofec@clemson.edu, Clemson University, Bioengineering, Clemson, SC, 29634, United States
Thomas Boland
Affiliation:
tboland@clemson.edu, Clemson University, Bioengineering, Clemson, SC, 29634, United States
Delphine Dean
Affiliation:
finou@clemson.edu, 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.

References

1. Kleinman, H. K., Luckenbill-Edds, L., and, F. W. Cannon Sephel, G. C., Anal. Biochem. 166, 113 (1987).CrossRefGoogle Scholar
2. Martin, G. R. and Kleinman, H. K., Hepatology. 1, 264266 (1981).CrossRefGoogle Scholar
3. Kadler, K. E., Holmes, D. F., Trotter, J. A. and Chapman, J. A., Biochem. J. 316, 111 (1996).CrossRefGoogle Scholar
4. Ottani, V., Martini, D., Franchi, M., Ruggeri, A. and Raspanti, M., Micron. 33, 587596 (2002).CrossRefGoogle 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).CrossRefGoogle Scholar
7. Matsumoto, N., Horibe, S., Nakamura, N., Senda, T., Shino, K. and Ochi, T., Arch. Orthop. Trauma Surg. 117, 215221 (1998).CrossRefGoogle Scholar
8. Borg, T. K., Rubin, K., Lundgren, E., Borg, K. and Obrink, B., Dev. Biol. 104, 8696 (1984).CrossRefGoogle 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).CrossRefGoogle Scholar
10. Walsh, K. B., Sweet, J. K., Parks, G. E. and Long, K. J., J. Mol. Cell Cardiol. 33, 12331247 (2001).CrossRefGoogle Scholar
11. Lee, P., Lin, R., Moon, J. and Lee, L. P., Biomed. Microdevices. 8, 3541 (2006).CrossRefGoogle 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).CrossRefGoogle Scholar
14. Kotani, H., Iwasaka, M., Ueno, S. and Curtis, A., J. Appl. Phys. 87, 61916193 (2000).CrossRefGoogle 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).CrossRefGoogle Scholar
17. Roth, E. A., Xu, T., Das, M., Gregory, C., Hickman, J. J. and Boland, T., Biomaterials. 25, 37073715 (2004).CrossRefGoogle Scholar
18. Hartgerink, J.D., Beniash, E., Stupp, S. I., Science, 294, 16841688 (2001)CrossRefGoogle 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

Send article to Kindle

To send this article to your Kindle, first ensure no-reply@cambridge.org is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about sending to your Kindle. Find out more about sending to your Kindle.

Note you can select to send to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be sent to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

Collagen Matrix Alignment Using Inkjet Printer Technology
Available formats
×

Send article to Dropbox

To send this article to your Dropbox account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your <service> account. Find out more about sending content to Dropbox.

Collagen Matrix Alignment Using Inkjet Printer Technology
Available formats
×

Send article to Google Drive

To send this article to your Google Drive account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your <service> account. Find out more about sending content to Google Drive.

Collagen Matrix Alignment Using Inkjet Printer Technology
Available formats
×
×

Reply to: Submit a response


Your details


Conflicting interests

Do you have any conflicting interests? *