Functional complexity of intermediate filament cytoskeletons: From structure to assembly to gene ablation

Herrmann, Harald; Hesse, Michael; Reichenzeller, Michaela; Aebi, Ueli; Magin, Thomas M.

doi:10.1016/s0074-7696(05)23003-6

Cited by 186 publications

(159 citation statements)

References 376 publications

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“…Thawed tissues were dounced and sonicated in 50 mM mannitol, 2 mM Tris-HCl (pH 7.2). TG activity is based on [1,[4][5][6][7][8][9][10][11][12][13][14] …”

Section: Animal Experiments and Tg2 Activitymentioning

confidence: 99%

Pharmacologic transglutaminase inhibition attenuates drug‐primed liver hypertrophy but not Mallory body formation

Strnad¹,

Siegel²,

Toivola³

et al. 2006

FEBS Letters

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Mallory bodies (MBs) are characteristic of several liver disorders, and consist primarily of keratins with transglutaminase-generated keratin crosslinks. We tested the effect of the transglutaminase-2 (TG2) inhibitor KCC009 on MB formation in a mouse model fed 3,5-diethoxycarbonyl-1,4-dihydrocollidine (DDC). KCC009 decreased DDC-induced liver enlargement without affecting MB formation or extent of liver injury. TG2 protein and activity increased after DDC feeding and localized within and outside hepatocytes. KCC009 inhibited DDC-induced hepatomegaly by affecting hepatocyte cell size rather than proliferation. Hence, TG2 is a potential mediator of injury-induced hepatomegaly via modulation of hepatocyte hypertrophy, and KCC009-mediated TG2 inhibition does not affect mouse MB formation.

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“…Thawed tissues were dounced and sonicated in 50 mM mannitol, 2 mM Tris-HCl (pH 7.2). TG activity is based on [1,[4][5][6][7][8][9][10][11][12][13][14] …”

Section: Animal Experiments and Tg2 Activitymentioning

confidence: 99%

Pharmacologic transglutaminase inhibition attenuates drug‐primed liver hypertrophy but not Mallory body formation

Strnad¹,

Siegel²,

Toivola³

et al. 2006

FEBS Letters

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“…Presently, at least 65 members of the intermediate filament protein family have been identified (Herrmann et al 2003;Oshima 2007), and their expression is sensitively reflected in the cell differentiation occurring in histogenesis and disease (Albers and Fuchs 1992;Iwatsuki 1999;Herrmann et al 2007;Iwatsuki and Suda 2007). Therefore, they have been utilized as valuable histochemical markers of cell differentiation .…”

Section: Introductionmentioning

confidence: 99%

Transient expression of keratin during neuronal development in the adult rabbit spinal ganglion

Iwatsuki

Suda

2009

Anat Sci Int

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A few neurons of the adult rabbit spinal ganglion express keratin. To examine the characters of these keratin-positive neurons, six kinds of intermediate filament proteins, namely keratin 8, keratin 14, nestin, vimentin, neurofilament 68 (NF-L) and glial fibrillary acidic protein (GFAP), were investigated immunohistochemically in developing and adult rabbit spinal ganglia. At 15 days of gestation, the spinal ganglion increased rapidly in volume and mainly consisted of three kinds of cells: small cells expressing vimentin, spindle-shaped cells co-expressing vimentin and nestin, and ovoid cells with an eccentric nucleus expressing nestin. Since some ovoid cells coexpressed nestin with either NF-L or GFAP, the ovoid cell may be considered to be an embryonic neural stem cell of the ganglion. In addition, a few keratin-positive polymorphic cells could be observed among these three kinds of cells. These polymorphic cells expressed five kinds of intermediate filament proteins, namely keratin 8, keratin 14, nestin, NF-L and GFAP. These cells were also detected in newborn and adult ganglia. A few neurons in the adult ganglion also expressed these five kinds of proteins as a Golgi-associated network. However, neurons expressing these proteins could not be detected in embryonic and newborn ganglia. Therefore, it may be considered that the keratin-positive polymorphic cell is a postnatal neural stem cell of the ganglion and that neurons transiently express keratin when polymorphic cells differentiate into neurons.

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Section: Introductionmentioning

confidence: 99%

“…All IFs share a common prototype structure consisting of a coiled-coil ␣-helical rod domain that is interrupted by linkers and flanked by non-␣-helical N-terminal "head" and C-terminal "tail" domains (Fuchs and Cleveland, 1998;Herrmann et al, 2003;Coulombe and Wong, 2004;Herrmann and Aebi, 2004). Within the IF family, keratins are the largest subfamily, and they make up the IFs of epithelial cells, whereas other IFs are characteristic of unique cell types (e.g., desmin in myocytes, neurofilaments in neuronal cells).…”

Section: Introductionmentioning

confidence: 99%

“…Keratins (K) include the type I and type II IFs, and all epithelial cells express at least one type I and one type II keratins as obligate noncovalent heteropolymers (Moll et al, 1982;Schweizer et al, 2006). In simple-type epithelia, as found in the liver, pancreas, and intestine, the major keratins are K18/K19/K20 (type I) and K7/K8 (type II), with the K8/K18 pair being dominant depending on the tissue (Moll et al, 1982;Ku et al, 1999;Herrmann et al, 2003;Zhou et al, 2003).Keratin networks are versatile structures that undergo dynamic reorganization in response to a variety of intra-and extracellular cues. Posttranslational modifications and keratin-binding partners are essential in mediating such responses (Coulombe and Omary, 2002;Omary et al, 2006).…”

mentioning

confidence: 99%

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Reg-II Is an Exocrine Pancreas Injury-Response Product That Is Up-Regulated by Keratin Absence or Mutation

Zhong

Strnad

Toivola

et al. 2007

MBoC

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The major keratins in the pancreas and liver are keratins 8 and 18 (K8/K18), but their function seemingly differs in that liver K8/K18 are essential cytoprotective proteins, whereas pancreatic K8/K18 are dispensable. This functional dichotomy raises the hypothesis that K8-null pancreata may undergo compensatory cytoprotective gene expression. We tested this hypothesis by comparing the gene expression profile in pancreata of wild-type and K8-null mice. Most prominent among the up-regulated genes in K8-null pancreas was mRNA for regenerating islet-derived (Reg)-II, which was confirmed by quantitative reverse transcription-polymerase chain reaction and by an anti-Reg-II peptide antibody we generated. Both K8-null and wild-type mice express Reg-II predominantly in acinar cells as determined by in situ hybridization and immunostaining. Analysis of Reg-II expression in various keratin-related transgenic mouse models showed that its induction also occurs in response to keratin cytoplasmic filament collapse, absence, or ablation of K18 Ser52 but not Ser33 phosphorylation via Ser-to-Ala mutation, which represent situations associated with predisposition to liver but not pancreatic injury. In wild-type mice, Reg-II is markedly up-regulated in two established pancreatitis models in response to injury and during the recovery phase. Thus, Reg-II is a likely mouse exocrine pancreas cytoprotective candidate protein whose expression is regulated by keratin filament organization and phosphorylation. INTRODUCTIONIntermediate filaments (IFs), microfilaments, and microtubules are the three major cytoskeletal protein groups of mammalian cells (Bershadsky and Vasiliev, 1988;Ku et al., 1999). All IFs share a common prototype structure consisting of a coiled-coil ␣-helical rod domain that is interrupted by linkers and flanked by non-␣-helical N-terminal "head" and C-terminal "tail" domains (Fuchs and Cleveland, 1998;Herrmann et al., 2003;Coulombe and Wong, 2004;Herrmann and Aebi, 2004). Within the IF family, keratins are the largest subfamily, and they make up the IFs of epithelial cells, whereas other IFs are characteristic of unique cell types (e.g., desmin in myocytes, neurofilaments in neuronal cells). This tissue-specific expression reflects the involvement of IFs in a broad range of tissue-selective human diseases (Fuchs and Cleveland, 1998;Omary et al., 2004). Keratins (K) include the type I and type II IFs, and all epithelial cells express at least one type I and one type II keratins as obligate noncovalent heteropolymers (Moll et al., 1982;Schweizer et al., 2006). In simple-type epithelia, as found in the liver, pancreas, and intestine, the major keratins are K18/K19/K20 (type I) and K7/K8 (type II), with the K8/K18 pair being dominant depending on the tissue (Moll et al., 1982;Ku et al., 1999;Herrmann et al., 2003;Zhou et al., 2003).Keratin networks are versatile structures that undergo dynamic reorganization in response to a variety of intra-and extracellular cues. Posttranslational modifications and keratin-binding partners...

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Functional complexity of intermediate filament cytoskeletons: From structure to assembly to gene ablation

Cited by 186 publications

References 376 publications

Pharmacologic transglutaminase inhibition attenuates drug‐primed liver hypertrophy but not Mallory body formation

Pharmacologic transglutaminase inhibition attenuates drug‐primed liver hypertrophy but not Mallory body formation

Transient expression of keratin during neuronal development in the adult rabbit spinal ganglion

Reg-II Is an Exocrine Pancreas Injury-Response Product That Is Up-Regulated by Keratin Absence or Mutation

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