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Biochemical and structural studies of tenascin/hexabrachion proteins.

Publication ,  Journal Article
Taylor, HC; Lightner, VA; Beyer, WF; McCaslin, D; Briscoe, G; Erickson, HP
Published in: J Cell Biochem
October 1989

Tenascin is a large, disulfide-bonded glycoprotein of the extracellular matrix. The predominant form of tenascin observed by electron microscopy is a six-armed oligomer, termed a hexabrachion. We have determined the molecular mass of the native human hexabrachion to be 1.9 x 10(6) Da by sedimentation equilibrium analysis and by electrophoresis on non-reducing agarose gels. On reducing polyacrylamide gel electrophoresis (SDS-PAGE), human tenascin showed a single prominent band at 320 kDa and minor bands of 220 and 230 kDa. The molecular weight of the native human hexabrachion is thus consistent with a disulfide-bonded hexamer of the 320 kDa subunits. Upon treatment with neuraminidase, the apparent molecular weights of all human and chicken tenascin subunits on reducing SDS-PAGE were decreased by about 10 kDa. Prolonged incubation with alpha-mannosidase, however, caused no apparent change in the apparent molecular weight of tenascin subunits. Sedimentation in a cesium chloride gradient gave a higher buoyant density for human tenascin than for fibronectin, suggesting that it has a higher degree of glycosylation. The far-UV circular dichroism spectrum indicates a predominance of beta-structure and a lack of collagen-like or alpha-helical structure. When human hexabrachions were reduced and acetylated, the resulting fragments were single arms which sedimented at 6 S in glycerol gradients and migrated at 320 kDa on non-reducing gels. Treatment of tenascin with trypsin and alpha-chymotrypsin also produced large fragments which were fractionated by gradient sedimentation and analyzed by non-reducing SDS-PAGE and electron microscopy. We present a structural model for the assembly of the observed fragments into the elaborate native hexabrachion.

Duke Scholars

Published In

J Cell Biochem

DOI

ISSN

0730-2312

Publication Date

October 1989

Volume

41

Issue

2

Start / End Page

71 / 90

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Tenascin
  • Protein Conformation
  • Oxidation-Reduction
  • Molecular Weight
  • Microscopy, Electron
  • Humans
  • Glycoside Hydrolases
  • Glioma
  • Fibroblasts
 

Citation

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Taylor, H. C., Lightner, V. A., Beyer, W. F., McCaslin, D., Briscoe, G., & Erickson, H. P. (1989). Biochemical and structural studies of tenascin/hexabrachion proteins. J Cell Biochem, 41(2), 71–90. https://doi.org/10.1002/jcb.240410204
Taylor, H. C., V. A. Lightner, W. F. Beyer, D. McCaslin, G. Briscoe, and H. P. Erickson. “Biochemical and structural studies of tenascin/hexabrachion proteins.J Cell Biochem 41, no. 2 (October 1989): 71–90. https://doi.org/10.1002/jcb.240410204.
Taylor HC, Lightner VA, Beyer WF, McCaslin D, Briscoe G, Erickson HP. Biochemical and structural studies of tenascin/hexabrachion proteins. J Cell Biochem. 1989 Oct;41(2):71–90.
Taylor, H. C., et al. “Biochemical and structural studies of tenascin/hexabrachion proteins.J Cell Biochem, vol. 41, no. 2, Oct. 1989, pp. 71–90. Pubmed, doi:10.1002/jcb.240410204.
Taylor HC, Lightner VA, Beyer WF, McCaslin D, Briscoe G, Erickson HP. Biochemical and structural studies of tenascin/hexabrachion proteins. J Cell Biochem. 1989 Oct;41(2):71–90.
Journal cover image

Published In

J Cell Biochem

DOI

ISSN

0730-2312

Publication Date

October 1989

Volume

41

Issue

2

Start / End Page

71 / 90

Location

United States

Related Subject Headings

  • Tumor Cells, Cultured
  • Tenascin
  • Protein Conformation
  • Oxidation-Reduction
  • Molecular Weight
  • Microscopy, Electron
  • Humans
  • Glycoside Hydrolases
  • Glioma
  • Fibroblasts