Abstract：
:Dystrophin and utrophin are known to link the intracellular cytoskeleton to the extracellular matrix via a transmembraneous glycoprotein complex. Four short C-terminal isoforms (Dp71, Dp116, Dp140, and Dp260) are described for dystrophin and three for utrophin (Up71, Up113, and Up140). We describe here for the first time the existence of a 3.7-kb transcript and a 62-kDa protein in C6 glioma cells representing a short N-terminal isoform unique for utrophin (N-utrophin). More than 20 clones covering the entire coding region of utrophin were isolated from a rat C6 glioma cell cDNA library. Two clones were found to code for a protein with 539 amino acids. Its sequence is identical to that of the full-length utrophin, except for the last residue where Cys is replaced by Val. This isoform contains the actin binding domain (consisting of two calponin homology subdomains), followed by two spectrin-like repeats. A recombinant fragment corresponding to N-utrophin binds to F-actin in vitro with an equilibrium constant (affinity) K of 4.5 x 10(5) M(-1) and a stoichiometry of one fragment per around five actin monomers. Immunocytochemical staining of C6 glioma cells with antisera specific for different utrophin regions localised full-length utrophin in the submembraneous cortical actin layer as revealed by confocal microscopy. A distinct staining pattern for the N-utrophin was not detectable, although it was expected to localise at the actin stress fibers. It is assumed that it co-localises via the two spectrin-like repeats with the full-length utrophin at the cell membrane.
journal_name
J Cell Biochemjournal_title
Journal of cellular biochemistryauthors
Zuellig RA,Bornhauser BC,Knuesel I,Heller F,Fritschy JM,Schaub MCdoi
10.1002/(sici)1097-4644(20000601)77:3<418::aid-jcbsubject
Has Abstractpub_date
2000-04-01 00:00:00pages
418-31issue
3eissn
0730-2312issn
1097-4644pii
10.1002/(SICI)1097-4644(20000601)77:3<418::AID-JCBjournal_volume
77pub_type
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