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Primary and Secondary Structure of IF Protein Chains and Modes of Molecular Aggregation

  • Chapter
Cellular and Molecular Biology of Intermediate Filaments

Abstract

Five classes of intermediate filaments (IF) have been defined on the basis of the cell type from which the filaments were initially isolated and characterized. The first of these classes comprises the keratins, a heterogeneous family of protein chains with molecular weights in the range 40 to 70k; they are expressed in most epithelia. Vimentin chains have a molecular weight of 53k, and are expressed in cells of mesenchymal origin and in cell lines established in vitro. The third class comprises desmin chains of molecular weight 53k; they are expressed in smooth, cardiac, and skeletal myogenic cells. Glial fibrillary acidic protein chains, found in glial cells and astrocytes, have molecular weights of 50k and form the fourth class. The fifth class of IF protein contains neurofilament chains with molecular weights of about 62, 98, and 112k; these are expressed in varying amounts in different neuronal tissues. The limitations of this type of classification have become apparent with the observation that some cells are capable of expressing vimentin in addition to their “normal” IF protein species.

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Authors and Affiliations

  1. Department of Physics and Biophysics, Massey University, Palmerston North, New Zealand

    David A. D. Parry

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  1. David A. D. Parry
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  1. Northwestern University Medical School, Chicago, Illinois, USA

    Robert D. Goldman

  2. National Cancer Institute, National Institutes of Health, Bethesda, Maryland, USA

    Peter M. Steinert

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Parry, D.A.D. (1990). Primary and Secondary Structure of IF Protein Chains and Modes of Molecular Aggregation. In: Goldman, R.D., Steinert, P.M. (eds) Cellular and Molecular Biology of Intermediate Filaments. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9604-9_7

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  • DOI: https://doi.org/10.1007/978-1-4757-9604-9_7

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