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  • 1
    Electronic Resource
    Electronic Resource
    Morphological evidence for the role of suprabasal keratinocytes in wound reepithelialization (2005)
    Oxford, UK; Malden, USA : Blackwell Science Inc
    Wound repair and regeneration 13 (2005), S. 0 
    Details
    ISSN: 1524-475X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The process by which wounds reepithelialize remains controversial. Two models have been proposed to describe reepithelialization: the “sliding” model and the “rolling” model. In the “sliding” model, basal keratinocytes are the principal cells responsible for migration and wound closure. In this model, basal and suprabasal keratinocytes remain strongly attached to leading edge basal keratinocytes and are then passively dragged along as a sheet. The “rolling” model postulates that basal keratinocytes remain strongly attached to the basement membrane zone while suprabasal keratinocytes at the wound margin are activated to roll into the wound site. The purpose of this study was to determine which populations of keratinocytes are actively involved in reepithelialization. We evaluated expression of keratins K14, K15, K10, K2e, and K16 as well as the proliferation marker Ki67 in the migrating tongue of normal human incisional 1-hour to 28-day wounds and normal human 3 mm diameter excisional 1- to 7-day wounds. Our results show dramatic changes in phenotype and protein expression of keratins K10, K2e, K14, K15, and K16 in suprabasal keratinocytes in response to injury. We conclude that this large population of suprabasal keratinocytes actively participates in wound closure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1067-1927.2005.00067.x
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation of galactoprotein a from hamster embryo fibroblasts and characterization of the carbohydrate unit (1979)
    s.l. : American Chemical Society
    Biochemistry 18 (1979), S. 730-738 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00571a027
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of subunits from the predominant form of Dolichos biflorus lectin (1975)
    s.l. : American Chemical Society
    Biochemistry 14 (1975), S. 2685-2689 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00683a019
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation and characterization of cyanogen bromide fragments and a glycopeptide from the Dolichos biflorus lectin (1975)
    s.l. : American Chemical Society
    Biochemistry 14 (1975), S. 5118-5122 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00694a015
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  • 5
    Electronic Resource
    Electronic Resource
    CHEMICAL COMPOSITION, GROSS STRUCTURE, AND ORGANIZATION OF TRANSFORMATION-SENSITIVE GLYCOPROTEINS (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 312 (1978), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1978.tb16801.x
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  • 6
    Electronic Resource
    Electronic Resource
    Expression of VLA-integrins and their related basement membrane ligands in gingiva from patients of various periodontitis categories (1999)
    Munksgaard : Munksgaard International Publishers
    Journal of clinical periodontology 26 (1999), S. 0 
    Details
    ISSN: 1600-051X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract. Periodontitis is characterized by destruction of dento-gingival fibers and apical migration of the junctional epithelium. Tissue destruction may be associated with altered interactions between epithelium and connective tissue mediated by integrins localized in the basement membrane zone. We examined the expression of α2β1, α3β1, α4/α5β1, α6β4 and their related extracellular matrix (ECM) ligands: laminin-1, laminin-5, and collagen type IV in untreated periodontitis sites of various categories. The expression and location of ECM proteins along the basement membrane were found to be similar between clinically healthy and periodontitis affected tissues. However, ECM proteins were more diffusely distributed in connective tissue (CT) of periodontitis tissues as streak-like/fibrillar/granular stainings, particularly beneath the pocket epithelium (PE) and around the blood vessels. This may reflect an increase in inflammatory cell migration. The more widespread distribution of integrins α2β1, α3β1 in PE of periodontitis specimens may be related to disease activity and increased rate of keratinocyte proliferation and migration. Moreover, the weaker expression of α6β4 in junctional epithelium (JE) of periodontitis affected tissues may be related to the epithelial detachment from the tooth surface. Clarification of expressions of integrins and their ligands in relation to known clinical disease susceptibility factors may provide information on the onset and progression mechanisms of periodontal disease destruction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1034/j.1600-051X.1999.260404.x
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  • 7
    Electronic Resource
    Electronic Resource
    The carbohydrate structure of human fibronectins: A comparison between normal embryonic lung fibroblasts WI-38 and the SV40 virus transformed cell line VA13 (1984)
    Springer
    Glycoconjugate journal 1 (1984), S. 155-169 
    Details
    ISSN: 1573-4986
    Keywords: fibronectin ; bi-antennary carbohydrates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The carbohydrates of human fibronectin released from non-transformed human fibroblasts WI-38 have been compared with those of fibronectin released from SV40 virus transformed WI-38/VA13 cells and those of fibronectin prepared from human plasma. The majority of the bi-antennary glycopeptides of fibronectin released from WI-38 fibroblasts was not sialylated at the terminal galactosyl residues, but was fucosylated at the coreN-acetylglucosaminyl residue directly linked to a peptide (structure A, below). Most of the minor sialylation detected was linked α2–3 to galactose. In contrast, the majority of the bi-antennary glycopeptides released from the transformed VA13 cells was highly sialylated at the terminal galactosyl residues with both α2–3 and α2–6 linkages, but was only partially fucosylated at the coreN-acetylglucosaminyl residue (structure B, below). This structure was similar to that of the bi-antennary glycopeptide of human plasma fibronectin which was, however, predominantly sialylated with an α2–6 linkage (structure C, below). These human fibronectins, regardless of their source, lack a high molecular weight lactosaminoglycan structure. In addition to the differences in bi-antennary structure described above, the quantity of tri- to tetra-antennary glycopeptides of fibronectin released from VA13 transformed cells was found to be much greater than the quantity of these glycopeptides of fibronectin released from normal WI-38 fibroblasts. Furthermore, there was a relatively small quantity of a glycopeptide fraction having a smaller molecular weight that did not bind to Con A-Sepharose and was separated on a Bio-Gel P-4 column. The presence of this fraction was characteristic for fibronectin released from transformed VA13 cells, and the fraction was absent in fibronectin from normal fibroblasts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01213728
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  • 8
    Electronic Resource
    Electronic Resource
    Extracellular matrix receptors, ECMRII and ECMRI, for collagen and fibronectin correspond to VLA-2 and VLA-3 in the VLA family of heterodimers (1988)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 37 (1988), S. 385-393 
    Details
    ISSN: 0730-2312
    Keywords: cell adhesion ; arg-gly-asp amino acid sequence ; VLA proteins ; integrin superfamily ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The Very Late Activation Antigen (VLA) proteins are a family of five related heterodimers, which also are part of the integrin superfamily of cell adhesion molecules. Except for the identification of VLA-5 as a fibronectin receptor structure, the functions of the VLA proteins have remained unclarified. In this paper, immuno-precipitation experiments with both anti-α and anti-β subunit antibodies showed that the previously identified cell adhesion receptor for collagen, extracellular matrix receptor II (ECMRII), is equivalent to VLA-2. At the same time a previously described multispecific cell adhesion receptor for collagen, fibroncclin, and laminin (ECMRI) has been shown to be identical to VLA-3. Although the mAb 12F1 and P1H5 both recognized VLA-2 (ECMRII), they appeared to define distinct epitopes on the α2 subunit. On the other hand, the mAb PIB5 and J143 recognized the α3 subunit of VLA-3 (ECMRI) at or near the same site. Consistent with the collagen receptor functions of VLA-2 (ECMRII) and VLA-3 (ECMRI), anti-VLA β antiserum blocked cell attachment to collagen.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240370406
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  • 9
    Electronic Resource
    Electronic Resource
    Comparison of the structures of human fibronectin and plasma cold-insoluble globulin (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 12 (1979), S. 505-516 
    Details
    ISSN: 0091-7419
    Keywords: fibronectin ; cold-insoluble globulin ; carbohydrate content ; proteoglycan ; proteolytic cleavage ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Human amniotic fluid fibronectin and plasma fibronectin (cold-incoluble globulin) are indistinguishable both immunologically and by amino acid composition. Cyanogen bromide and tryptic peptides also suggest substantial structural homology. However, carbohydrate analysis has demonstrated additional saccharides in fibronectin and an overall increase in carbohydrate content relative to coldinsoluble globulin. Furthermore, limited proteolytic cleavage of the two proteins indicates differences in primary structure or in conformation. Using affinity-purified antibodies to cold-insoluble globulin, a glucosamine-labeled pronaseresistant component, probably proteoglycan, was found to coprecipitate with fibronectin, suggesting an association between these two macromolecules in the connective tissue matrix.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400120410
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