Molecular characterization of human tensin

H. Chen, A. Ishii, W. K. Wong, L. B. Chen, Su Hao Lo

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

Tensin is a focal-adhesion molecule that binds to actin filaments and interacts with phosphotyrosine-containing proteins. To analyse tensin's function in mammals, we have cloned tensin cDNAs from human and cow. The isolated approx. 7.7-kb human cDNA contains an open reading frame encoding 1735 amino acid residues. The amino acid sequence of human tensin shares 60% identity with chicken tensin, and contains all the structural features described previously in chicken tensin. This includes the actin-binding domains, the Src homology domain 2, and the region similar to a tumour suppressor, PTEN. Two major differences between human and chicken tensin are (i) the lack of the first 54 residues present in chicken tensin, and (ii) the addition of 34- and 38-residue inserts in human and bovine tensin. In addition, our interspecies sequencing data have uncovered the presence of a glutamine/CAG repeat that appears to have expanded in the course of evolution. Northern-blot analysis reveals a 10-kb message in most of the human tissues examined. An additional 9-kb message is detected in heart and skeletal muscles. The molecular mass predicted from the human cDNA is 185 kDa, although both endogenous and recombinant human tensin migrate as 220-kDa proteins on SDS/PAGE. The discrepancy is due to the unusually low electrophoretic mobility of the central region of the tensin polypeptide (residues 306-981). A survey of human prostate and breast cancer cell lines by Western-blot analysis shows a lack of tensin expression in most cancer cell lines, whereas these lines express considerable amounts of focal-adhesion molecules such as talin and focal-adhesion kinase. Finally, tensin is rapidly cleaved by a focal-adhesion protease, calpain II. Incubation of cells with a calpain inhibitor, MDL, prevented tensin cleavage and induced morphological change in these cells, suggesting that cleavage of tensin and other focal-adhesion constituents by calpain disrupts maintenance of normal cell shape.

Original languageEnglish (US)
Pages (from-to)403-411
Number of pages9
JournalBiochemical Journal
Volume351
Issue number2
DOIs
StatePublished - Oct 15 2000

Fingerprint

Adhesion
Calpain
Complementary DNA
Cells
Actins
Talin
Amino Acids
Focal Adhesions
Focal Adhesion Protein-Tyrosine Kinases
Electrophoretic mobility
Phosphotyrosine
Molecules
Mammals
Molecular mass
Glutamine
Chickens
Muscle
Tumors
Proteins
Peptide Hydrolases

Keywords

  • Calpain
  • Focal adhesion
  • Glutamine repeat

ASJC Scopus subject areas

  • Biochemistry

Cite this

Molecular characterization of human tensin. / Chen, H.; Ishii, A.; Wong, W. K.; Chen, L. B.; Lo, Su Hao.

In: Biochemical Journal, Vol. 351, No. 2, 15.10.2000, p. 403-411.

Research output: Contribution to journalArticle

Chen, H, Ishii, A, Wong, WK, Chen, LB & Lo, SH 2000, 'Molecular characterization of human tensin', Biochemical Journal, vol. 351, no. 2, pp. 403-411. https://doi.org/10.1042/0264-6021:3510403
Chen, H. ; Ishii, A. ; Wong, W. K. ; Chen, L. B. ; Lo, Su Hao. / Molecular characterization of human tensin. In: Biochemical Journal. 2000 ; Vol. 351, No. 2. pp. 403-411.
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