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Activation of Mg-ATPase of Skeletal-Muscle Myosin by Bovine Retinal Pigment Epithelial Actin
Journal article   Peer reviewed

Activation of Mg-ATPase of Skeletal-Muscle Myosin by Bovine Retinal Pigment Epithelial Actin

Lawrence S Chan, Mahin Khatami, Weiye Li and John H Rockey
Ophthalmic research, v 21(6), pp 420-427
1989
DOI: https://doi.org/10.1159/000266932
PMID: 2533975
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Original Paper
The morphology and function of actin in cultured bovine retinal pigment epithelial (RPE) cells were studied. Filamentous actin was identified with a fluorescent mushroom toxin, nitrobenzoxadiazole (NBD)-phallacidin, specific for actin. Dark-field microscopy of cultured RPE cells revealed numerous pigment granules; fluorescent microscopy identified scattered lipofuscin granules. One-dimensional SDS polyacrylamide gel electrophoresis of urea-soluble proteins extracted from RPE cells showed a 46,000-dalton protein band which comigrated with authentic muscle actin. Densitometric scanning showed that this protein band comprised 7.6% of the total urea-soluble proteins. An actin-activated skeletal-muscle myosin Mg-ATPase assay, using skeletal-muscle heavy meromyosin as enzyme and [γ-32P]-ATP as substrate, demonstrated functional actin in RPE cell extracts after DEAE-cellulose anion exchange chromatography. The actin-containing protein fractions were eluted at ionic strengths between 0.19 and 0.36 M KCl. The activation of myosin ATPase by actin in RPE cells provides a molecular basis for the phagocytic activity which is important in maintaining the integrity of retinal photoreceptor cells.

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Web of Science research areas
Ophthalmology
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