Steady‐state levels of different tenascin mRNAs in various normal human tissues.

Northern blot analysis of TN mRNA from different human tissues shows two major bands of about 6 and 8 kb which correspond to two different mRNAs generated by alternative splicing of the primary transcript. In liver, pancreas and kidney only the 6 kb TN mRNA was detectable. The highest levels of 8 kb TN mRNA were observed in placenta and skin representing 30% and 52% of total TN mRNA, respectively. In all other tissues tested the 8 kb TN mRNA represented less than 20% of total TN mRNA.

[1]  L. Zardi,et al.  Expression of different tenascin isoforms in normal, hyperplastic and neoplastic human breast tissues , 1992, International journal of cancer.

[2]  G. Edelman,et al.  Cytotactin: a morphoregulatory molecule and a target for regulation by homeobox gene products. , 1992, Trends in biochemical sciences.

[3]  J. Spring,et al.  Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues. , 1991, Cell regulation.

[4]  K. Titani,et al.  Qualitative and quantitative changes of human tenascin expression in transformed lung fibroblast and lung tumor tissues: comparison with fibronectin. , 1991, Cancer research.

[5]  A. Bhattacharyya,et al.  Tenascin in normal, reactive, hyperplastic, and neoplastic tissues: biologic and pathologic implications. , 1991, Human pathology.

[6]  B. Imhof,et al.  Tenascin Mr 220,000 isoform expression correlates with corneal cell migration. , 1991, Development.

[7]  G. Casari,et al.  Human tenascin: primary structure, pre-mRNA splicing patterns and localization of the epitopes recognized by two monoclonal antibodies. , 1991, Nucleic acids research.

[8]  P. Ekblom,et al.  Amino acid sequence of mouse tenascin and differential expression of two tenascin isoforms during embryogenesis , 1991, The Journal of cell biology.

[9]  R. Chiquet‐Ehrismann What distinguishes tenascin from fibronectin? , 1990, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[10]  J. Gulcher,et al.  An alternatively spliced region of the human hexabrachion contains a repeat of potential N-glycosylation sites. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[11]  L. Zardi,et al.  Tenascin: A hexameric adhesive glycoprotein , 1989, International journal of cancer. Supplement = Journal international du cancer. Supplement.

[12]  M. Chiquet Tenascin/J1/cytotactin: the potential function of hexabrachion proteins in neural development. , 1989, Developmental neuroscience.

[13]  H. Erickson,et al.  Tenascin: an extracellular matrix protein prominent in specialized embryonic tissues and tumors. , 1989, Annual review of cell biology.