Vmac: a novel protein associated with vimentin-type intermediate filament in podocytes of rat kidney

Biochem Biophys Res Commun. 2004 Mar 19;315(4):1120-5. doi: 10.1016/j.bbrc.2004.01.169.

Abstract

Vimentin-type intermediate filaments (IFs) play an important role in cytoskeletal organization and cell morphology. We identified here a novel protein associated with vimentin-type IFs and named it vimentin-type IF-associated coiled-coil protein (Vmac). Vmac consists of 171 amino acids with a calculated Mr of 18,844 and has a coiled-coil domain in its N-terminal region and the PDZ-binding tetrapeptide consensus motif in its C-terminal region. Northern blotting showed that the Vmac mRNA was expressed in many rat tissues examined but most abundantly expressed in the kidney. Immunofluorescence microscopy revealed that Vmac was highly concentrated at podocytes of renal glomeruli. Podocytes are highly specialized epithelial cells characterized by a large cell body and numerous foot processes, and express vimentin-type IFs that are distributed in the cell body and the major processes. Immunoelectron microscopy revealed that Vmac was associated with vimentin-type IFs of podocytes. These results indicate that Vmac is a novel protein associated with vimentin-type IF in podocytes of rat kidney.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cryoultramicrotomy / methods
  • Epithelial Cells / metabolism
  • Humans
  • Immunohistochemistry
  • Intermediate Filament Proteins / genetics
  • Intermediate Filament Proteins / metabolism*
  • Intermediate Filaments / metabolism*
  • Kidney Glomerulus / cytology
  • Kidney Glomerulus / metabolism*
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Rats
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Staining and Labeling / methods
  • Subcellular Fractions / metabolism
  • Tissue Distribution
  • Vimentin / genetics

Substances

  • Intermediate Filament Proteins
  • Vimentin