Hagfish Slime Gland Thread Cells. II. Isolation and Characterization of Intermediate Filament Components Associated with the Thread

The slime glands of hagfish have two major cell types, gland thread cells (GTCs) and gland mucous cells (GMCs), both of which upon contact with water contribute to the formation of an abundant quantity of viscous mucus. In previous studies we reported a method for the isolation of GTCs and showed th...

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Bibliographic Details
Published in:The Journal of cell biology 1984-02, Vol.98 (2), p.670-677
Main Authors: Spitzer, Robert H., Downing, Stephen W., Koch, Elizabeth A., Salo, Wilmar L., Saidel, Leo J.
Format: Article
Language:English
Subjects:
Amino acids
Amino Acids - analysis
Animals
Biological and medical sciences
Carbohydrates - analysis
Cell Fractionation - methods
Cell structures and functions
Cells
Chromatography
Cytoskeleton - ultrastructure
Cytoskeleton, cytoplasm. Intracellular movements
Electrophoresis, Polyacrylamide Gel
Epidermal cells
Fishes
Fundamental and applied biological sciences. Psychology
Gels
Intermediate filaments
Keratins
Macromolecular Substances
Molecular and cellular biology
Molecular Weight
Mucus
Proteins - analysis
Sebaceous Glands - cytology
Sebaceous Glands - ultrastructure
Ungulates
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Summary:The slime glands of hagfish have two major cell types, gland thread cells (GTCs) and gland mucous cells (GMCs), both of which upon contact with water contribute to the formation of an abundant quantity of viscous mucus. In previous studies we reported a method for the isolation of GTCs and showed that each ellipsoidal thread cell normally contains a single tapered thread which is uniquely coiled into a space-saving conformation and occupies most of the cell volume. Subsequently, the developing thread was found to consist mainly of intermediate filaments (IFs) aligned in parallel not only to one another but also to a far fewer number of interspersed microtubules (see accompanying paper). In the present report, urea extracts of GTCs were purified and characterized to establish the properties of thread components. One major (α) and two minor (β, γ) components prepared by anion exchange chromatography were shown to have similar apparent molecular weights of 63,500 ± 500 daltons but different isoelectric pH values (α, 7.56; β, 5.67; γ, 5.31). Although the amino acid content of α differed significantly from β and γ, each of the three was highest in Gly, relatively high in Glx, Ser, Thr, Asx, Ala, Val, and Leu, and relatively low in Cys/2 and Trp. The amino acid compositions of β and γ were very similar, and only β showed evidence of carbohydrate. The threonine content of the α component was higher than has been reported for IFs of different origin, and the high content of hydroxyamino acids (18, 19 residues per 100) in α, β, and γ has been approached only by several IF polypeptides from human or bovine epidermal keratins. Mixtures of the purified components formed 9-11-nm filaments in vitro. The results indicate that the hagfish thread cell is a rich source of IFs, which have a structure that facilitates formation of macrofibrils within the cell.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.98.2.670