TEM8 Interacts with the Cleaved C5 Domain of Collagen α3(VI)

Akash Nanda; Eleanor B. Carson-Walter; Steven Seaman; Thomas D. Barber; Jason Stampfl; Sujay Singh; Bert Vogelstein; Kenneth W. Kinzler; Brad St. Croix

doi:10.1158/0008-5472.CAN-03-2408

TEM8 Interacts with the Cleaved C5 Domain of Collagen α3(VI)

Akash Nanda, Eleanor B. Carson-Walter, Steven Seaman, Thomas D. Barber, Jason Stampfl, Sujay Singh, Bert Vogelstein, Kenneth W. Kinzler, Brad St. Croix

Research output: Contribution to journal › Article › peer-review

150 Scopus citations

Abstract

Tumor endothelial marker (TEM)8 was uncovered as a gene expressed predominantly in tumor endothelium, and its protein product was recently identified as the receptor for anthrax toxin. Here, we demonstrate that TEM8 protein is preferentially expressed in endothelial cells of neoplastic tissue. We used the extracellular domain of TEM8 to search for ligands and identified the α3 subunit of collagen VI as an interacting partner. The TEM8-interacting region on collagen α3(VI) was mapped to its COOH-terminal C5 domain. Remarkably, collagen α3(VI) is also preferentially expressed in tumor endothelium in a pattern concordant with that of TEM8. These results suggest that the TEM8/C5 interaction may play an important biological role in tumor angiogenesis.

Original language	English (US)
Pages (from-to)	817-820
Number of pages	4
Journal	Cancer Research
Volume	64
Issue number	3
DOIs	https://doi.org/10.1158/0008-5472.CAN-03-2408
State	Published - Feb 1 2004

ASJC Scopus subject areas

Oncology
Cancer Research

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title = "TEM8 Interacts with the Cleaved C5 Domain of Collagen α3(VI)",

abstract = "Tumor endothelial marker (TEM)8 was uncovered as a gene expressed predominantly in tumor endothelium, and its protein product was recently identified as the receptor for anthrax toxin. Here, we demonstrate that TEM8 protein is preferentially expressed in endothelial cells of neoplastic tissue. We used the extracellular domain of TEM8 to search for ligands and identified the α3 subunit of collagen VI as an interacting partner. The TEM8-interacting region on collagen α3(VI) was mapped to its COOH-terminal C5 domain. Remarkably, collagen α3(VI) is also preferentially expressed in tumor endothelium in a pattern concordant with that of TEM8. These results suggest that the TEM8/C5 interaction may play an important biological role in tumor angiogenesis.",

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T1 - TEM8 Interacts with the Cleaved C5 Domain of Collagen α3(VI)

AU - Nanda, Akash

AU - Carson-Walter, Eleanor B.

AU - Seaman, Steven

AU - Barber, Thomas D.

AU - Stampfl, Jason

AU - Singh, Sujay

AU - Vogelstein, Bert

AU - Kinzler, Kenneth W.

AU - St. Croix, Brad

PY - 2004/2/1

Y1 - 2004/2/1

N2 - Tumor endothelial marker (TEM)8 was uncovered as a gene expressed predominantly in tumor endothelium, and its protein product was recently identified as the receptor for anthrax toxin. Here, we demonstrate that TEM8 protein is preferentially expressed in endothelial cells of neoplastic tissue. We used the extracellular domain of TEM8 to search for ligands and identified the α3 subunit of collagen VI as an interacting partner. The TEM8-interacting region on collagen α3(VI) was mapped to its COOH-terminal C5 domain. Remarkably, collagen α3(VI) is also preferentially expressed in tumor endothelium in a pattern concordant with that of TEM8. These results suggest that the TEM8/C5 interaction may play an important biological role in tumor angiogenesis.

AB - Tumor endothelial marker (TEM)8 was uncovered as a gene expressed predominantly in tumor endothelium, and its protein product was recently identified as the receptor for anthrax toxin. Here, we demonstrate that TEM8 protein is preferentially expressed in endothelial cells of neoplastic tissue. We used the extracellular domain of TEM8 to search for ligands and identified the α3 subunit of collagen VI as an interacting partner. The TEM8-interacting region on collagen α3(VI) was mapped to its COOH-terminal C5 domain. Remarkably, collagen α3(VI) is also preferentially expressed in tumor endothelium in a pattern concordant with that of TEM8. These results suggest that the TEM8/C5 interaction may play an important biological role in tumor angiogenesis.

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TEM8 Interacts with the Cleaved C5 Domain of Collagen α3(VI)

Abstract

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