Literature DB >> 3155518

Myosin from human erythrocytes.

A J Wong, D P Kiehart, T D Pollard.   

Abstract

We have purified myosin from human erythrocytes using methods similar to that for other cytoplasmic myosins with a yield of about 500 micrograms/100 ml of packed cells. It consists of a 200-kDa heavy chain and light chains of 26- and 19.5 kDa and therefore differs from the isozyme in platelets which has light chains of 20- and 15 kDa. At low ionic strength, the myosin forms short bipolar filaments like those of platelet myosin. Eight of eight monoclonal antibodies to platelet myosin also bind to erythrocyte myosin. Like most myosins, it has a high ATPase activity in the presence of Ca2+ or EDTA, but is inhibited by Mg2+. Myosin light-chain kinase transfers 1 phosphate from ATP to the 20-kDa light chain, and this stimulates the actin-activated ATPase. Thus, myosin may play a role in shape changes in the erythrocytes.

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Year:  1985        PMID： 3155518

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


  13 in total

1.  Interaction domains of neurofilament light chain and brain spectrin.

Authors:  T Frappier; F Stetzkowski-Marden; L A Pradel
Journal:  Biochem J       Date:  1991-04-15       Impact factor: 3.857

2.  Visualization of the protein associations in the erythrocyte membrane skeleton.

Authors:  T J Byers; D Branton
Journal:  Proc Natl Acad Sci U S A       Date:  1985-09       Impact factor: 11.205

3.  Erythrocyte protein 4.1 binds and regulates myosin.

Authors:  G R Pasternack; R H Racusen
Journal:  Proc Natl Acad Sci U S A       Date:  1989-12       Impact factor: 11.205

4.  Calculation of a Gap restoration in the membrane skeleton of the red blood cell: possible role for myosin II in local repair.

Authors:  C Cibert; G Prulière; C Lacombe; C Deprette; R Cassoly
Journal:  Biophys J       Date:  1999-03       Impact factor: 4.033

5.  MYH9-related disease mutations cause abnormal red blood cell morphology through increased myosin-actin binding at the membrane.

Authors:  Alyson S Smith; Kasturi Pal; Roberta B Nowak; Anastasiya Demenko; Carlo Zaninetti; Lydie Da Costa; Remi Favier; Alessandro Pecci; Velia M Fowler
Journal:  Am J Hematol       Date:  2019-04-17       Impact factor: 10.047

6.  Concanavalin A-agglutinability of membrane-skeleton-free vesicles and aged cellular remnants derived from human erythrocytes. Is the membrane skeleton required for agglutination?

Authors:  S M Gokhale; N G Mehta
Journal:  Biochem J       Date:  1987-01-15       Impact factor: 3.857

7.  Myosin IIA interacts with the spectrin-actin membrane skeleton to control red blood cell membrane curvature and deformability.

Authors:  Alyson S Smith; Roberta B Nowak; Sitong Zhou; Michael Giannetto; David S Gokhin; Julien Papoin; Ionita C Ghiran; Lionel Blanc; Jiandi Wan; Velia M Fowler
Journal:  Proc Natl Acad Sci U S A       Date:  2018-04-02       Impact factor: 11.205

8.  Cytoplasmic myosin from Drosophila melanogaster.

Authors:  D P Kiehart; R Feghali
Journal:  J Cell Biol       Date:  1986-10       Impact factor: 10.539

9.  Beta actin and its mRNA are localized at the plasma membrane and the regions of moving cytoplasm during the cellular response to injury.

Authors:  T C Hoock; P M Newcomb; I M Herman
Journal:  J Cell Biol       Date:  1991-02       Impact factor: 10.539

10.  Identification of the gene for fly non-muscle myosin heavy chain: Drosophila myosin heavy chains are encoded by a gene family.

Authors:  D P Kiehart; M S Lutz; D Chan; A S Ketchum; R A Laymon; B Nguyen; L S Goldstein
Journal:  EMBO J       Date:  1989-03       Impact factor: 11.598
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