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Actin in cultured bovine retinal capillary pericytes: Morphological and functional correlation
Journal article   Peer reviewed

Actin in cultured bovine retinal capillary pericytes: Morphological and functional correlation

Lawrence S. Chan, Weiye Li, Mahin Khatami and John H. Rockey
Experimental eye research, v 43(1)
1986
PMID: 2942415

Abstract

actin culture diabetic retinopathy pericyte
Actin in cultured bovine retinal capillary pericytes was identified and partially characterized biochemically. The filamentous actin was localized in bovine retinal capillary pericytes using a fluorescent mushroom toxin (nitrobenzoxadiazole-phallacidin) specific for actin. One-dimensional SDS-polyacrylamide-gel electrophoresis of urea-extracted proteins from bovine retinal capillary pericytes revealed a 46000 MW protein band corresponding to an actin standard, which comprised 7·3% of the total urea-soluble proteins. Actin-activated skeletal muscle myosin Mg 2+-ATPase assay, using [γ- 32P]-ATP as substrate, demonstrated functional actin in bovine retinal capillary pericyte extracts after DEAE-cellulose anion-exchange chromatography. The actin-containing protein fractions were eluted at ionic strengths between 0·25 and 0·35 m KCl. The presence of functional actin in pericytes indicated the ability to generate contractile force. This contractiongenerating ability may allow pericytes to regulate microvessel caliber and to maintain the integrity of the capillary wall. A lack of this function when pericytes are preferentially lost in diabetic retinal microangiopathy could destabilize the microvessel wall and predispose the capillary to further pathologic changes.

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Ophthalmology
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