Collagen XII and XIV, New Partners of Cartilage Oligomeric Matrix Protein in the Skin Extracellular Matrix Suprastructure

Research output: Contribution to journalArticle

Standard

Collagen XII and XIV, New Partners of Cartilage Oligomeric Matrix Protein in the Skin Extracellular Matrix Suprastructure. / Agarwal, Pallavi; Zwolanek, Daniela; Keene, Douglas R.; Schulz, Jan-Niklas; Blumbach, Katrin; Heinegård, Dick; Zaucke, Frank; Paulsson, Mats; Krieg, Thomas; Koch, Manuel; Eckes, Beate.

In: Journal of Biological Chemistry, Vol. 287, No. 27, 2012, p. 22549-22559.

Research output: Contribution to journalArticle

Harvard

Agarwal, P, Zwolanek, D, Keene, DR, Schulz, J-N, Blumbach, K, Heinegård, D, Zaucke, F, Paulsson, M, Krieg, T, Koch, M & Eckes, B 2012, 'Collagen XII and XIV, New Partners of Cartilage Oligomeric Matrix Protein in the Skin Extracellular Matrix Suprastructure', Journal of Biological Chemistry, vol. 287, no. 27, pp. 22549-22559. https://doi.org/10.1074/jbc.M111.335935

APA

Agarwal, P., Zwolanek, D., Keene, D. R., Schulz, J-N., Blumbach, K., Heinegård, D., Zaucke, F., Paulsson, M., Krieg, T., Koch, M., & Eckes, B. (2012). Collagen XII and XIV, New Partners of Cartilage Oligomeric Matrix Protein in the Skin Extracellular Matrix Suprastructure. Journal of Biological Chemistry, 287(27), 22549-22559. https://doi.org/10.1074/jbc.M111.335935

CBE

Agarwal P, Zwolanek D, Keene DR, Schulz J-N, Blumbach K, Heinegård D, Zaucke F, Paulsson M, Krieg T, Koch M, Eckes B. 2012. Collagen XII and XIV, New Partners of Cartilage Oligomeric Matrix Protein in the Skin Extracellular Matrix Suprastructure. Journal of Biological Chemistry. 287(27):22549-22559. https://doi.org/10.1074/jbc.M111.335935

MLA

Vancouver

Author

Agarwal, Pallavi ; Zwolanek, Daniela ; Keene, Douglas R. ; Schulz, Jan-Niklas ; Blumbach, Katrin ; Heinegård, Dick ; Zaucke, Frank ; Paulsson, Mats ; Krieg, Thomas ; Koch, Manuel ; Eckes, Beate. / Collagen XII and XIV, New Partners of Cartilage Oligomeric Matrix Protein in the Skin Extracellular Matrix Suprastructure. In: Journal of Biological Chemistry. 2012 ; Vol. 287, No. 27. pp. 22549-22559.

RIS

TY - JOUR

T1 - Collagen XII and XIV, New Partners of Cartilage Oligomeric Matrix Protein in the Skin Extracellular Matrix Suprastructure

AU - Agarwal, Pallavi

AU - Zwolanek, Daniela

AU - Keene, Douglas R.

AU - Schulz, Jan-Niklas

AU - Blumbach, Katrin

AU - Heinegård, Dick

AU - Zaucke, Frank

AU - Paulsson, Mats

AU - Krieg, Thomas

AU - Koch, Manuel

AU - Eckes, Beate

N1 - The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151)

PY - 2012

Y1 - 2012

N2 - The tensile and scaffolding properties of skin rely on the complex extracellular matrix (ECM) that surrounds cells, vasculature, nerves, and adnexus structures and supports the epidermis. In the skin, collagen I fibrils are the major structural component of the dermal ECM, decorated by proteoglycans and by fibril-associated collagens with interrupted triple helices such as collagens XII and XIV. Here we show that the cartilage oligomeric matrix protein (COMP), an abundant component of cartilage ECM, is expressed in healthy human skin. COMP expression is detected in the dermal compartment of skin and in cultured fibroblasts, whereas epidermis and HaCaT cells are negative. In addition to binding collagen I, COMP binds to collagens XII and XIV via their C-terminal collagenous domains. All three proteins codistribute in a characteristic narrow zone in the superficial papillary dermis of healthy human skin. Ultrastructural analysis by immunogold labeling confirmed colocalization and further revealed the presence of COMP along with collagens XII and XIV in anchoring plaques. On the basis of these observations, we postulate that COMP functions as an adapter protein in human skin, similar to its function in cartilage ECM, by organizing collagen I fibrils into a suprastructure, mainly in the vicinity of anchoring plaques that stabilize the cohesion between the upper dermis and the basement membrane zone.

AB - The tensile and scaffolding properties of skin rely on the complex extracellular matrix (ECM) that surrounds cells, vasculature, nerves, and adnexus structures and supports the epidermis. In the skin, collagen I fibrils are the major structural component of the dermal ECM, decorated by proteoglycans and by fibril-associated collagens with interrupted triple helices such as collagens XII and XIV. Here we show that the cartilage oligomeric matrix protein (COMP), an abundant component of cartilage ECM, is expressed in healthy human skin. COMP expression is detected in the dermal compartment of skin and in cultured fibroblasts, whereas epidermis and HaCaT cells are negative. In addition to binding collagen I, COMP binds to collagens XII and XIV via their C-terminal collagenous domains. All three proteins codistribute in a characteristic narrow zone in the superficial papillary dermis of healthy human skin. Ultrastructural analysis by immunogold labeling confirmed colocalization and further revealed the presence of COMP along with collagens XII and XIV in anchoring plaques. On the basis of these observations, we postulate that COMP functions as an adapter protein in human skin, similar to its function in cartilage ECM, by organizing collagen I fibrils into a suprastructure, mainly in the vicinity of anchoring plaques that stabilize the cohesion between the upper dermis and the basement membrane zone.

U2 - 10.1074/jbc.M111.335935

DO - 10.1074/jbc.M111.335935

M3 - Article

C2 - 22573329

VL - 287

SP - 22549

EP - 22559

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 1083-351X

IS - 27

ER -