Intermediate filaments: regulation of gene expression and assembly

Klundert, Francy A. J. M. van de; Raats, Jos; Bloemendal, H.

doi:10.1111/j.1432-1033.1993.tb17931.x

Cited by 50 publications

(5 citation statements)

References 272 publications

(188 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…PKC activation by phorbol esters is followed by a translocation of this kinase to the cytoskeleton, vimentin phosphorylation, and IF disassembly [Castagna et al, 1982;Ando et al, 1989;Zalewski et al, 1990;Klundert et al, 1993]. In this work, it was found that melatonin, like PMA, twice increased basal levels of vimentin phosphorylation, and modifies IF rearrangements.…”

Section: Discussionmentioning

confidence: 68%

“…Also, the kinase can be directly stimulated by phorbol esters, which are lipophilic compounds able to cross the lipid bilayers [Castagna et al, 1982]. Activation of PKC by either diacylglycerol or phorbol esters is followed by translocation of this enzyme from the cytosol to the membranecytoskeletal fraction [Castagna et al, 1982;Zalewski et al, 1990], as well as by vimentin phosphorylation, and IF disassembly [Ando et al, 1989;Zalewski et al, 1990;Klundert et al, 1993]. These evidences suggest the hypothesis that melatonin may modulate vimentin IF organization through activation of PKC.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

PKC activation by melatonin modulates vimentin intermediate filament organization in N1E‐115 cells

Benítez‐King

2000

Journal of Pineal Research

View full text Add to dashboard Cite

Melatonin enters cells and causes cytoskeletal rearrangements in unicellular organisms, plants and vertebrates. This pineal secretory product causes microtubule enlargement and neurite outgrowth by a calmodulin antagonism in N1E-115 cells. Recently, direct in vitro activation of protein kinase C by melatonin was described. Vimentin intermediate filaments are attached to microtubules and their organization depends on both microtubule distribution and phosphorylation of specific proteins. Protein kinase C is a serine threonine kinase which phosphorylates vimentin and through this mechanism causes intermediate filament disassembly. In this work the effects of melatonin on protein kinase C activation, content, and subcellular distribution were studied in N1E-115 cells. Also, melatonin effects on vimentin phosphorylation and subcellular distribution were explored. The results show that melatonin both activates and increases protein kinase C content in the membrane cytoskeletal fraction. Melatonin protein kinase C activation was followed by an increase in both vimentin phosphorylation and by vimentin subcellular redistribution. Moreover, staurosporine, a serine threonine kinase inhibitor, prevented increased vimentin phosphorylation elicited by melatonin. Similar effects to those caused by melatonin were obtained with the protein kinase C activator phorbol 12-myristate 13-acetate. Data support the idea that melatonin modulates vimentin organization through protein kinase C activation.

show abstract

Section: Discussionmentioning

confidence: 68%

Section: Introductionmentioning

confidence: 99%

PKC activation by melatonin modulates vimentin intermediate filament organization in N1E‐115 cells

Benítez‐King

2000

Journal of Pineal Research

View full text Add to dashboard Cite

show abstract

“…(1989, 1990) observed that the cytokeratin phenotype of perivascular epithelium is similar to that of subcapsular and a subset of medullary epithelium in mammals, where it is most frequently made up of CK 13 and 19. The thymic capillaries in N. forsteri were positively labelled with the vimentin Ab, as they are in other vertebrates (Klundert et al. 1993).…”

Section: Discussionmentioning

confidence: 73%

“…1986), or a co‐synthesis of vimentin with other cytokeratins in the thymus epithelium, as found in rat (Colić et al. 1992; Klundert et al. 1993).…”

Section: Discussionmentioning

confidence: 90%

“…In mammals and birds, type I and II intermediate filament proteins are a characteristic feature of cells from epithelial lineages in the thymus, whereas among type III intermediate filament proteins, vimentin indicates that the cells are of mesenchymal origin and desmin is present in thymic cells containing myofibrils (Klundert et al. 1993; Herrmann & Harris, 1998; Robson et al.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cytoskeletal proteins in thymic epithelial cells of the Australian lungfish Neoceratodus forsteri

2008

View full text Add to dashboard Cite

The vertebrate thymus consists of distinctive subpopulations of epithelial cells that contain a diverse repertoire of cytoskeletal proteins. In this study of the thymus in the Australian lungfish, Neoceratodus forsteri , immunohistochemistry was used to distinguish the cytoskeletal proteins present in each class of thymic epithelial cell. A panel of antibodies (Abs), each specific for a different cytoskeletal polypeptide (keratins, vimentin, desmin, actin and tubulins), was used on paraffin and ultrathin resin sections of thymus. Ab AE I (reactive against human type I cytokeratins (CK) 14, 16 and 19) selectively stained the cytoplasm of capsular, trabecular and the outermost epithelial cells of Hassall's corpuscles. Anti-CK 10 Abs strongly labelled the capsular epithelial cells and less than 20% of cortical and medullary epithelial cells. The anti-50-kDa desmin Ab did not react with any thymic cells, whereas the anti-53-kDa desmin Ab labelled some capsular, cortical and medullary thymic epithelial cells. The anti-vimentin Ab stained most of the capsular and ~60% of the cortical epithelium. Thymic nurse cells and Hassall's corpuscles were found to be devoid of actin, which was strongly detected in medullary and perivascular epithelium. Both α and β tubulins were detected in all thymic cells. This study extends the concept of thymic epithelial heterogeneity. The complexity of thymic epithelium in N. forsteri may indicate a relationship between thymic epithelial subpopulations and the thymic microenvironment. These data identify anti-keratin Abs as a valuable tool for studying differentiation and ontogeny of the thymic epithelium in N. forsteri .

show abstract