Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues

Cell Regul. 1991 Nov;2(11):927-38. doi: 10.1091/mbc.2.11.927.


In the chicken, three tenascin variants have been characterized that are generated by alternative splicing of 3 of its 11 fibronectin type III repeats. Using monoclonal antibodies that react with common regions versus extra repeats of tenascin, we could distinguish and separate tenascin variants and investigate their interaction with fibronectin using multiple experimental procedures. Interestingly, in all assays used the smallest tenascin variant bound more strongly to fibronectin than the larger ones. These biochemical data were paralleled by the observation that in chick embryo fibroblast cultures only the smallest form of tenascin could be detected in the fibronectin-rich extracellular matrix network laid down by the cells. Furthermore, each tissue present in adult chicken gizzard contained a distinct set of tenascin variants. Those tissues particularly rich in extracellular matrix, such as the tendon, contained the smallest tenascin only. Intermediate-sized tenascin was present in smooth muscle, whereas the largest form was exclusively detectable underneath the epithelial lining of the villi. Thus it appears that cell type-specific forms of tenascin exist that are appropriate for the functional requirements of the respective extracellular matrices.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Adhesion Molecules, Neuronal / genetics
  • Cell Adhesion Molecules, Neuronal / immunology
  • Cell Adhesion Molecules, Neuronal / metabolism*
  • Chick Embryo
  • Chickens
  • Edetic Acid / pharmacology
  • Epitopes
  • Extracellular Matrix / physiology*
  • Extracellular Matrix Proteins / genetics
  • Extracellular Matrix Proteins / immunology
  • Extracellular Matrix Proteins / metabolism*
  • Fibronectins / metabolism*
  • Fluorescent Antibody Technique
  • Gizzard, Avian / cytology
  • In Vitro Techniques
  • Protein Binding / drug effects
  • RNA Splicing
  • Sodium Chloride / pharmacology
  • Structure-Activity Relationship
  • Tenascin
  • Urea / pharmacology


  • Cell Adhesion Molecules, Neuronal
  • Epitopes
  • Extracellular Matrix Proteins
  • Fibronectins
  • Tenascin
  • Sodium Chloride
  • Urea
  • Edetic Acid