Structural features of the α-type filaments of the inner root sheath cells of the guinea pig hair follicle

Steinert, Peter M.

doi:10.1021/bi00616a029

Cited by 27 publications

(34 citation statements)

References 36 publications

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“…7D). Using an established mathematical modeling algorithm (48) with amino acid composition data of IRS tryptic peptides (23,26), this composite consists of an approximate 1:2 ratio of THH:KIF. The ease with which morphologically intact KIF can be harvested from IRS cells (35) implies that most cross-links occur between THH molecules.…”

Section: Recovery and Identification Of Cross-links In Thh-8 -mentioning

confidence: 99%

“…These include the following: the type 1 enzyme that is expressed in the epidermis and uterus, type 2 enzyme that is expressed ubiquitously, and type 3 enzyme that is expressed in the hair follicle (20 -22). A large body of indirect data have implicated THH as a major target for PAD activity in these tissues (16,19,(23)(24)(25)(26)(27). Recently, we have shown that a bacterially expressed shorter form of human THH (THH domain 8, THH-8) is a substrate for the type 2 PAD enzyme (28), the substrate specificity of which has been shown to be very similar to that of the type 3 enzyme (20).…”

mentioning

confidence: 99%

“…Apparently, proteolysis cleaves sequences on the end domains of the constituent KIF chains that are adjoined by cross-links between KIF and the interfilamentous THH (26). This releases morphologically intact KIF (although with somewhat pruned chains) and solubilized peptides highly enriched in cross-link and citrulline with a THH-like amino acid composition (26).…”

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confidence: 99%

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The Fate of Trichohyalin

Tarcsa

Marekov

Andreoli

et al. 1997

Journal of Biological Chemistry

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135

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Trichohyalin (THH) is a major structural protein of the inner root sheath cells and medulla layer of the hair follicle and, to a lesser extent, of other specialized epithelia. THH is a high molecular weight insoluble ␣-helixrich protein that forms rigid structures as a result of postsynthetic modifications by two Ca 2؉ -dependent enzymes, transglutaminases (TGases) (protein cross-linking) and peptidyl-arginine deiminase (conversion of arginines to citrullines with loss of organized structure). The modified THH is thought to serve as a keratin intermediate filament matrix protein and/or as a constituent of the cell envelope. In this paper, we have explored in vitro the order of processing of THH to fulfill these functions, using an expressed truncated, more soluble form THH-8. THH-8 is a complete substrate for three known TGases expressed in epithelia, but the kinetic efficiency with TGase 3 is by far the greatest. Following maximal conversion of its arginines to citrullines, THH-8 is cross-linked even more efficiently by TGase 3, using most glutamines partially and all lysines. In addition, we show that insoluble aggregates of THH-8 or native pig tongue THH can be solubilized following peptidyl-arginine deiminase modification. Together, these data suggest an in vivo model in which THH located in insoluble cytoplasmic droplets is first modified by peptidyl-arginine deiminase which denatures it and makes it more soluble. This renders it available for efficient cross-linking by TGase 3 to form highly crosslinked rigid structures in the cells. This temporal order of reaction is supported by the observation that THH is expressed in hair follicle cells before the TGase 3 enzyme.

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Section: Recovery and Identification Of Cross-links In Thh-8 -mentioning

confidence: 99%

mentioning

confidence: 99%

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confidence: 99%

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The Fate of Trichohyalin

Tarcsa

Marekov

Andreoli

et al. 1997

Journal of Biological Chemistry

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135

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“…Upon stratification, these epithelial cell types diverge, and each expresses a unique set of keratins that are tissue-specific for their particular program of differentiation (Fuchs and Green, 1980;Viac et al, 1980;Woodcock-Mitchell et al, 1982;Skerrow and Skerrow, 1983;Crewther et al, 1983;van Muijen et al, 1986;Schermer et al, 1986). The expression of these new sets of keratins is frequently associated with an increase in bundling of keratin filaments (Steinert, 1978;Eichner et al, 1986).…”

mentioning

confidence: 99%

“…In the hair follicle, the programs of differentiation and patterns of keratin expression are far more complex than in other stratified squamous epithelia (Steinert and Rogers, 1973;Steinert, 1978;Crewther et al, 1980;Baden, 1981;Moll et al, 1982bMoll et al, , 1988Lane et al, 1985;French and Hewish, 1986;Ito et al, 1986;Lynch et al, 1986;Heid et al, 1986Heid et al, , 1988aStark et al, 1987). Surrounding the hair shaft are two sheaths, an outer (ORS) ~ and an inner ORS) root sheath (Fig.…”

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confidence: 99%