Structure of the human hexabrachion (tenascin) gene.

Abstract

The structure of the gene encoding human hexabrachion (tenascin) has been determined from overlapping clones isolated from a human genomic bacteriophage library. The genomic inserts were characterized by restriction mapping, Southern blot analysis, PCR, and DNA sequencing. The coding region of the hexabrachion gene spans 80 kilobases of DNA and consists of 27 exons separated by 26 introns. The exon-intron structure supports a hypothesis based on the cDNA sequence that the hexabrachion gene is an assembly of DNA modules that are also found elsewhere in the genome.

Tenascin-C: Form versus function

“…For example, all vertebrate tenascin-C contains 13.5 EGF-L repeats, with the exception of mammals which possess 14.5 EGF-L repeats. 30 Furthermore, tenascin-C from humans, rats, mice and chickens each contain 8 constitutive FNIII repeats, with an additional cassette of FNIII which may be alternatively spliced between FNIII domains 5 and 6. However, the number of alternatively spliced FNIII repeats varies by species; with chickens and mice, rats, and humans having 6, 7 and 9 respectively.…”

Transcriptional Regulation of the Endogenous Danger Signal Tenascin-C: A Novel Autocrine Loop in Inflammation

“…The entire coding region (exons 2-30) is restricted to a ∼7.5-kbp segment of this locus; this constitutes only 3.6% of the overall gene, which spans ∼211 kbp. The exons range in size from 90 to 1410 bp and the introns from 578 to 26,827 bp (42). The proximal 220 bp upstream of the transcription start site in exon 1 is sufficient for the basal expression of tenascin-C gene reporter constructs indiscriminately in cell lines producing (SK-MEL-28 human melanoma) or not producing (hamster R1-G9 glucagonoma and human FL ovary carcinoma) endogenous tenascin-C (39).…”

Breast cancer molecular subtypes and the metastatic microenvironment: Review of literature

“…Other extracellular matrix components include Tenascin C, which is an oligomeric glycoprotein composed of individual polypeptides with molecular weights ranging from 180 to ~300kDa. These protein modules are lined up like beads on a string and give rise to long and extended molecules [54] . Tenascin-C has been shown to interact with fibronectin in order to modify cell adhesion [55] .…”