Identification and characterization of multiple species of tenascin-X in human serum

D. F. Egging; A. C.T.M. Peeters; N. Grebenchtchikov; A. Geurts-Moespot; C. G.J. Sweep; M. Den Heijer; J. Schalkwijk

doi:https://doi.org/10.1111/j.1742-4658.2007.05671.x

Identification and characterization of multiple species of tenascin-X in human serum

D. F. Egging, A. C.T.M. Peeters, N. Grebenchtchikov, A. Geurts-Moespot, C. G.J. Sweep, M. Den Heijer, J. Schalkwijk

Internal Medicine (VUmc)

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

14 Citations (Scopus)

Abstract

We analysed the diversity of tenascin-X (TNX) species in serum and studied parameters that could affect determination of TNX levels in serum. Using western blot analysis we identified at least seven distinct TNX species, ranging from 75 kDa to the presumably full-length 450 kDa form. Purification of serum TNX followed by sequence analysis positively identified two major TNX species of 75 and 140 kDa. We found that serum TNX binds to tropoelastin but not to fibrillar collagens. We conclude that serum TNX is composed of distinct molecular species that retain functional activity.

Original language	English
Pages (from-to)	1280-1289
Number of pages	10
Journal	FEBS journal
Volume	274
Issue number	5
DOIs	https://doi.org/10.1111/j.1742-4658.2007.05671.x
Publication status	Published - Mar 2007

Keywords

Collagen
Ehlers-Danlos syndrome
Elastin
Serum
Tenascin-X

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https://doi.org/10.1111/j.1742-4658.2007.05671.x

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abstract = "We analysed the diversity of tenascin-X (TNX) species in serum and studied parameters that could affect determination of TNX levels in serum. Using western blot analysis we identified at least seven distinct TNX species, ranging from 75 kDa to the presumably full-length 450 kDa form. Purification of serum TNX followed by sequence analysis positively identified two major TNX species of 75 and 140 kDa. We found that serum TNX binds to tropoelastin but not to fibrillar collagens. We conclude that serum TNX is composed of distinct molecular species that retain functional activity.",

keywords = "Collagen, Ehlers-Danlos syndrome, Elastin, Serum, Tenascin-X",

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AU - Egging, D. F.

AU - Peeters, A. C.T.M.

AU - Grebenchtchikov, N.

AU - Geurts-Moespot, A.

AU - Sweep, C. G.J.

AU - Den Heijer, M.

AU - Schalkwijk, J.

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AB - We analysed the diversity of tenascin-X (TNX) species in serum and studied parameters that could affect determination of TNX levels in serum. Using western blot analysis we identified at least seven distinct TNX species, ranging from 75 kDa to the presumably full-length 450 kDa form. Purification of serum TNX followed by sequence analysis positively identified two major TNX species of 75 and 140 kDa. We found that serum TNX binds to tropoelastin but not to fibrillar collagens. We conclude that serum TNX is composed of distinct molecular species that retain functional activity.

KW - Collagen

KW - Ehlers-Danlos syndrome

KW - Elastin

KW - Serum

KW - Tenascin-X

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Identification and characterization of multiple species of tenascin-X in human serum

Abstract

Keywords

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