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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 14 (1975), S. 3024-3029 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Munksgaard International Publishers
    Experimental dermatology 12 (2003), S. 0 
    ISSN: 1600-0625
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The ultrastructure and constituent components of the basement membrane zone (BMZ) of the interfollicular epidermis have been well characterized. However, little is known about the junctions between dermal papilla and the surrounding epithelial cells of the hair bulb, as well as those junctions between connective tissues and epithelial cells outside the hair follicle. In the present study, immunofluorescence was used to determine the expression of various BMZ components, particularly plectin, BP230, BP180, α6β4 integrin, laminin 5 and type VII collagen, in anagen hair follicles from human scalp. All the BMZ components examined showed essentially the same immunofluorescence staining pattern. Specifically, staining of the upper portion of the hair follicle demonstrated expression of all BMZ components with a labeling intensity similar to that found in the interfollicular epidermis. Staining in the lower portion of the hair follicle, however, was markedly different: all the BMZ components showed a gradual decrease in staining intensity. Particularly, outside the hair bulb, the linear staining was diminished and even discontinuous in some areas. Finally, between dermal papilla and epithelial cells inside the hair bulb, there was a strong immunoreactivity for all the BMZ components except for BP230, which was completely negative. The present study also confirmed a previous reported ultrastructural finding that hemidesmosomes are not apparent in the hair bulb's exterior BMZ nor in the dermal papilla junctions. Instead, peculiar cloudy materials were seen in both the lamina densa and the adjacent epithelium outside the hair bulb. Taken together, the diminished expression of all the BMZ components outside the hair bulb, as well as the complete absence of BP230 at the dermal papilla junction, seem to be responsible for the incomplete ultrastructure of hemidesmosomes in these regions. Furthermore, the results in the present study led us to speculate that the expression of BMZ components inside and outside the hair bulb are markedly decreased in the transient regions of the hair follicle as compared with their expression in the permanent region, signified by the upper portion of the hair follicle. When the hair follicle moves upward in catagen or downward in anagen, the complete structure of the hemidesmosome may stabilize the upper portion to the surrounding connective tissues, while the incomplete hemidesmosome may facilitate the movement of the transient region.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The proband was a 14-year-old male with unrelated parents. He displayed typical clinical features of GABEB (Fig. 1). The parents were clinically normal, there was no family history of a blistering skin disease and the proband did not have other siblings. Immunostaining with a monoclonal antibody ...
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0886-1544
    Keywords: fibroblast ; permeabilized cell model ; Ca2+-dependent contraction ; calmodulin ; phosphorylation ; myosin light chain ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Human lung fibroblast MRC-5 cells treated with Triton X-100 (MRC-5 cell models) were able to contract in the presence of MgATP and Ca2+ of more than 1 μM. Immunofluorescence microscopy with antibodies to actin and myosin 20,000-dalton (20 Kd) light chain revealed that stress fibers were prominent in MRC-5 cell models. Use of a fluorescent actin probe, 7-nitrobenz-2-oxa-1,3-diazole-phallacidin permitted visualization of contraction of the stress fibers in the presence of MgATP and Ca2+. Of the proteins in MRC-5 cell models, only a myosin 20 Kd light chain was phosphorylated in a Ca2+-dependent manner. This Ca2+-dependent phosphorylation of the 20 Kd light chain closely corresponded with the contraction of MRC-5 cell models: 1) Both phosphorylation of the 20 Kd light chain and contraction of MRC-5 cell models were inhibited by calmodulin antagonists such as N-(6-aminohexyl)5-chloro-1-napthalene sulfonamide. 2) The threshold Ca2+ concentration for phosphorylation of the 20 Kd light chain was similar to that for contraction of MRC-5 cell models. Both were lowered by exogenous calmodulin in a concentration-dependent manner. 3) The 20 Kd light chain was thiophosphorylated by incubation of MRC-5 cell models with an ATP analogue, adenosine 5′-0-(3-thiotriphosphate) only in the presence of Ca2+. After this treatment, MRC-5 cell models lost the Ca2+-dependence for contraction. These results indicate that Ca2+-calmodulin-dependent phosphorylation of myosin 20 Kd light chain is required for contraction of MRC-5 cell models.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Recent BP230-knockout experiments with subsequent blistering and recently identified plectin/HD1 mutations in epidermolysis bullosa simplex patients suggest that defective expression of BP230 and plectin/HD1 may predispose to blister formation in human skin. We have studied the expression of the epithelial adhesion complex as well as the basement membrane and anchoring fibril antigens in uninvolved dermatitis herpetiformis skin to find out if alterations can be detected in these structures predisposing to the blister formation typical of the disease. Ten uninvolved dermatitis herpetiformis skin specimens, which all showed clear granular deposits of IgA under the basement membrane in direct immunofluorescence and five normal skin specimens, were studied by indirect immunofluorescence technique. Six uninvolved dermatitis herpetiformis skin specimens showed distinctly decreased immunoreaction for BP230 and four uninvolved dermatitis herpetiformis skin specimens showed distinctly decreased immunoreaction for plectin/HD1. All five skin controls showed strong immunoreactions for BP230 and plectin/HD1. Other hemidesmosomal proteins including BP180 and integrin α6β4, as well as basement membrane proteins laminin-5, laminin-1, nidogen and type IV collagen, and the anchoring fibril protein type VII collagen showed a normal strong expression. Our results suggest that alterations in BP230 and plectin/HD1 may contribute or predispose to blister formation in dermatitis herpetiformis skin.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0878
    Keywords: Intermediate filaments ; Vimentin ; Pigment epithelial cells ; Epithelium formation ; Immunofluorescence ; Chicken
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Retinal pigmented epithelial cells of chicken have circumferential microfilament bundles (CMBs) at the zonula adherens region. Isolated CMBs are polygons filled with a meshwork composed primarily of intermediate filaments; they show three major components of 200000, 55000, and 42000 daltons in SDS-gel electrophoresis. Here we have characterized the 55000-dalton protein immunochemically and ultrastructurally. Immunoblotting and immunofluorescence microscopy have shown that the 55000-dalton protein is an intermediate filament protein, vimentin. Vimentin filaments changed their distribution during differentiation of pigmented epithelial cells in culture. The protein in the elongated cells showed a fibroblast-type pattern of intermediate filaments. During epithelium formation, the filaments were uniformly distributed and formed a finer meshwork at the apical level. In pigmented epithelial cells that differentiated and matured in culture, vimentin and actin exhibited their characteristic behavior after treatment with colcemid. In the central to basal region of the cell, intermediate filaments formed thick perinuclear bundles. In the apical region, however, intermediate filaments changed in organization from a nonpolarized meshwork to a polarized bundle-like structure. Simultaneously, new actin bundles were formed, running parallel to the intermediate filaments. This suggests that there is some interaction between microfilaments and intermediate filaments in the apical region of these cells.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0878
    Keywords: Retinal pigment epithelium ; Cytoskeleton ; Cytokeratins ; Vimentin ; Desmosomes ; Anura (Rana ridibunda, Xenopus laevis) ; Chicken ; Bovine ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In vertebrate tissue development a given cell differentiation pathway is usually associated with a pattern of expression of a specific set of cytoskeletal proteins, including different intermediate filament (IF) and junctional proteins, which is identical in diverse species. The retinal pigment epithelium (RPE) is a layer of polar cells that have very similar morphological features and practically identical functions in different vertebrate species. However, in biochemical and immunolocalization studies of the cytoskeletal proteins of these cells we have noted remarkable interspecies differences. While chicken RPE cells contain only IFs of the vimentin type and do not possess desmosomes and desmosomal proteins RPE cells of diverse amphibian (Rana ridibunda, Xenopus laevis) and mammalian (rat, guinea pig, rabbit, cow, human) species express cytokeratins 8 and 18 either as their sole IF proteins, or together with vimentin IFs as in guinea pig and a certain subpopulation of bovine RPE cells. Plakoglobin, a plaque protein common to desmosomes and the zonula adhaerens exists in RPE cells of all species, whereas desmoplakin and desmoglein have been identified only in RPE desmosomes of frogs and cows, including bovine RPE cell cultures in which cytokeratins have disappeared and vimentin IFs are the only IFs present. These challenging findings show that neither cytokeratin IFs nor desmosomes are necessary for the establishment and function of a polar epithelial cell layer and that the same basic cellular architecture can be achieved by different programs of expression of cytoskeletal proteins. The differences in the composition of the RPE cytoskeleton further indicate that, at least in this tissue, a specific program of expression of IF and desmosomal proteins is not related to the functions of the RPE cell, which are very similar in the various species.
    Type of Medium: Electronic Resource
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