The cystoskeleton of unstimulated blood platelets: Structure and composition of the isolated marginal microtubular band

D. M. Kenney, R. W. Linck

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Abstract

Detergent-insoluble, marginal microtubular band (MB) cytoskeletons were isolated from unstimulated blood platelets after pretreatment with glycerol or with Taxol. MB-cytoskeletons retained the shape of intact platelets and behaved in suspension as coherent structural units. The major structural component was a continuous coil of long microtubule(s), often with granular/amorphous material present in the centre; few typical actin filaments were observed. The coiled microtubules often had an amorphous surface coating, but no discrete inter-microtubule bridges were seen. Tubulin and actin (identified by immunochemical staining) were major polypeptides. None of the minor (>10) polypeptide components comigrated with high molecular weight microtubule-associated proteins in brain tubulin. A novel polypeptide, resolved by two-dimensional electrophoresis and designated IEF-51K, was present in MB cytoskeletons in amounts approximately equivalent to each of the tubulin polypeptides. Evidence suggests that IEF-51K is a distinct, previously undescribed component of the platelet cytoskeletal system.

Original languageEnglish (US)
Pages (from-to)1-22
Number of pages22
JournalJournal of Cell Science
VolumeVOL. 78
StatePublished - Jan 1 1985

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