Literature DB >> 7197221

Disassembly of synthetic 10-nm desmin filaments from smooth muscle into protofilaments.

M H Stromer, T W Huiatt, R L Richardson, R M Robson.   

Abstract

Synthetic 10-nm filaments formed from highly purified turkey gizzard desmin have a helically oriented substructure and disassemble into 2 to 2.5 nm protofilaments and 3.5 to 5 nm subfilaments after treatment with 1 or 2 M urea or with low-ionic-strength buffer (8 mM Tris, pH 8.2). SDS-gels of 10-nm filaments treated with these solutions show that a single 55 000-dalton band is present before and after all treatments and indicate that the newly revealed substructure is not caused by proteolysis. Antibodies to electrophoretically purified desmin react, in immunodiffusion, only with the antigen and decorate both the subfilamentous particles and the synthetic 10-nm filaments. These studies indicate that a synthetic 10-nm desmin filament is a rope-like structure constructed from the 2 to 2.5 nm diameter protofilaments.

Entities:  

Mesh:

Substances:

Year:  1981        PMID: 7197221

Source DB:  PubMed          Journal:  Eur J Cell Biol        ISSN: 0171-9335            Impact factor:   4.492


  6 in total

1.  Determination of the critical concentration required for desmin assembly.

Authors:  R G Chou; M H Stromer; R M Robson; T W Huiatt
Journal:  Biochem J       Date:  1990-11-15       Impact factor: 3.857

2.  Effect of cations and temperature on kinetics of desmin assembly.

Authors:  M H Stromer; M A Ritter; Y Y Pang; R M Robson
Journal:  Biochem J       Date:  1987-08-15       Impact factor: 3.857

3.  The fibrillar substructure of keratin filaments unraveled.

Authors:  U Aebi; W E Fowler; P Rew; T T Sun
Journal:  J Cell Biol       Date:  1983-10       Impact factor: 10.539

4.  Differential extraction of keratin subunits and filaments from normal human epidermis.

Authors:  R Eichner; M Kahn
Journal:  J Cell Biol       Date:  1990-04       Impact factor: 10.539

5.  Identification of a calcium-regulated insulinoma cell phosphoprotein as an islet cell keratin.

Authors:  U K Schubart; K L Fields
Journal:  J Cell Biol       Date:  1984-03       Impact factor: 10.539

6.  Molecular interactions in paracrystals of a fragment corresponding to the alpha-helical coiled-coil rod portion of glial fibrillary acidic protein: evidence for an antiparallel packing of molecules and polymorphism related to intermediate filament structure.

Authors:  M Stewart; R A Quinlan; R D Moir
Journal:  J Cell Biol       Date:  1989-07       Impact factor: 10.539

  6 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.