Molecular variants of fibronectin and laminin: structure, physiological occurrence and histopathological aspects

Kosmehl, Hartwig; Berndt, Alexander; Katenkamp, D.

doi:10.1007/bf00198435

Cited by 118 publications

(89 citation statements)

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“…First, the mRNA in situ hybridization for ED-B fibronectin was performed as described. Second, after thorough rinsing in Tris buffer the PAP procedure for α-smooth muscle actin or Von Willebrand factor visualization was carried out (Kosmehl et al, 1996).…”

Section: Double Staining Procedures For α-Smooth Muscle Actin/von Willmentioning

confidence: 99%

“…The laminins represent a continuously growing family of proteins (Kosmehl et al, 1996;Miner et al, 1997), whose members are endowed with different biological functions (Strassburger et al, 1998). Because skin and oral squamous epithelia bear structural and functional resemblances, their similar laminin chain composition is not surprising (Rousselle et al, 1991;Sollberg et al, 1992).…”

Section: Laminin Chains In the Normal Oral Squamous Epitheliummentioning

confidence: 99%

“…Recent results have given rise to a new definition of laminin and fibronectin as molecule families (Mandel et al, 1994;Kosmehl et al, 1996). Laminin is a heterotrimeric molecule with an α, β and γ chain.…”

mentioning

confidence: 99%

“…Variants of cellular fibronectin arise from further alternative splicing or de novo O-linked glycosylation in the IIICS domain. In contrast to the ubiquitously distributed common cellular fibronectin, the ED-A and the ED-B fibronectin as well as the de novo glycosylated fibronectin isoforms are limited to areas with structural tissue modulation, embryonic tissues, reparative processes and neoplasias (Loridon-Rosa et al, 1990;Xia and Culp, Distribution of laminin and fibronectin isoforms in oral mucosa and oral squamous cell carcinoma 1995; Kornblihtt et al, 1996;Kosmehl et al, 1996;Burton-Wurster et al, 1997). The isoforms are identifiable using specific monoclonal antibodies (Borsi et al, 1987;Mandel et al, 1992;Carnemolla et al, 1996).…”

mentioning

confidence: 99%

“…The isoforms are identifiable using specific monoclonal antibodies (Borsi et al, 1987;Mandel et al, 1992;Carnemolla et al, 1996). Extracellular matrix molecules influence differentiation, proliferation, migration, and have stabilizing and separating functions (Kosmehl et al, 1996). To our knowledge, a comparative study focusing on the modulation of the laminin chain pattern in fetal, normal adult, hyperproliferative, or dysplastic oral epithelium and in OSCC of different malignancy grade has not yet been conducted.…”

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confidence: 99%

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Distribution of laminin and fibronectin isoforms in oral mucosa and oral squamous cell carcinoma

et al. 1999

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SummaryThe expression of laminin and fibronectin isoforms varies with cellular maturation and differentiation and these differences may well influence cellular processes such as adhesion and motility. The basement membrane (BM) of fetal oral squamous epithelium contains the laminin chains, α2, α3, α5, β1, β2, β3, γ1 and γ2. The BM of adult normal oral squamous epithelium comprises the laminin chains, α3, α5, β1, β3, γ1 and γ2. A re-expression of the laminin α2 and β2 chains could be shown in adult hyperproliferative, dysplastic and carcinomatous lesions.In dysplasia and oral squamous cell carcinoma (OSCC), multifocal breaks of the BM are present as indicated by laminin chain antibodies. These breaks correlate to malignancy grade in their extent. Moreover, in the invasion front the α3 and γ2 chain of laminin-5 can immunohistochemically be found outside the BM within the cytoplasm of budding carcinoma cells and in the adjacent stroma. The correlation between the morphological pattern of invasive tumour clusters and a laminin-5 immunostaining in the adjacent stroma may suggest, first, that a laminin-5 deposition outside the BM is an immunohistochemical marker for invasion and second, that OSCC invasion is guided by the laminin-5 matrix. Expression of oncofetal fibronectins (IIICS de novo glycosylated fibronectin and ED-B fibronectin) could be demonstrated throughout the stromal compartment. However, the ED-B fibronectin synthesizing cells (RNA/RNA in situ hybridization) are confined to small stroma areas and to single stroma and inflammatory cells in the invasion front. A correlation of the number of ED-B fibronectin synthesizing cells to malignancy grade could not be seen. ED-B fibronectin mRNA-positive cells seem to be concentrated in areas of fibrous stroma recruitment with a linear alignment of stromal fibro-/myofibroblasts (desmoplasia). Double staining experiments (ED-B fibronectin in situ hybridization and α-smooth muscle actin immunohistochemistry) indicated that the stroma myofibroblasts are a preferential source of ED-B fibronectin. In conclusion, in OSCC, a fetal extracellular matrix conversion is demonstrable. Tumour cells (laminin α2 and β2 chain) and recruited stromal myofibroblasts (oncofetal ED-B fibronectin) contribute to the fetal extracellular matrix milieu.

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Section: Double Staining Procedures For α-Smooth Muscle Actin/von Willmentioning

confidence: 99%

Section: Laminin Chains In the Normal Oral Squamous Epitheliummentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Distribution of laminin and fibronectin isoforms in oral mucosa and oral squamous cell carcinoma

et al. 1999

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Divergence of smooth muscle target and sympathetic pathway cell phenotypes in the orbit of the developing rat

1999

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The periorbital sheath serves as a major pathway for sympathetic nerves traveling to distal orbital targets in the rat. This tissue accommodates sympathetic fiber sprouting in the neonate but becomes impassable by postnatal day 30 (PND 30). In contrast, smooth muscle target remains receptive to sympathetic ingrowth. To determine the attributes of receptive and nonreceptive tissues, we compared periorbital pathway and target tissue phenotypes prior to (PND 5 and PND 15) and after (PND 30 and PND 60) the period when pathway receptivity is lost. Both pathway cells and superior tarsal smooth muscle cells expressed α‐smooth muscle actin and smooth muscle myosin heavy chain throughout development. At PND 5–15, both tissues also expressed vimentin, collagen IV, laminin 1 and laminin β2, whereas fibronectin was detected only in pathway tissue. At PND 30, vimentin, collagen IV, and fibronectin were absent in tarsal muscle but were robust in pathway tissue. Laminin 1 and laminin β2 expression was maintained in muscle; however, in pathway cells, laminin 1 declined modestly, and laminin β2 decreased precipitously to barely detectable levels. Quantitative competitive polymerase chain reaction showed that nerve growth factor mRNA was present in the pathway throughout development at levels that were greater than both surrounding connective tissue and tarsal muscle. We conclude that the loss of pathway receptivity to sympathetic nerve ingrowth is associated with a transition from a phenotype similar to fetal smooth muscle cells to one that is more consistent with myofibroblast‐like cells. J. Comp. Neurol. 408:352–364, 1999. © 1999 Wiley‐Liss, Inc.

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Frequency‐Dependent Alternating‐Current Scanning Electrochemical Microscopy (4D AC‐SECM) for Local Visualisation of Corrosion Sites

Eckhard

Erichsen

Stratmann

et al. 2008

Chemistry A European J

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For a better understanding of the initiation of localised corrosion, there is a need for analytical tools that are capable of imaging corrosion pits and precursor sites with high spatial resolution and sensitivity. The lateral electrochemical contrast in alternating-current scanning electrochemical microscopy (AC-SECM) has been found to be highly dependent on the frequency of the applied alternating voltage. In order to be able to obtain data with optimum contrast and high resolution, the AC frequency is swept in a full spectrum at each point in space instead of performing spatially resolved measurements at one fixed perturbation frequency. In doing so, four-dimensional data sets are acquired (4D AC-SECM). Here, we describe the instrument set-up and modus operandi, along with the first results from the imaging of corroding surfaces. Corrosion precursor sites and local defects in protective organic coatings, as well as an actively corroding pit on 304 stainless steel, have been successfully visualised. Since the lateral electrochemical contrast in these images varies with the perturbation frequency, the proposed approach constitutes an indispensable tool for obtaining optimum electrochemical contrast.

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Molecular variants of fibronectin and laminin: structure, physiological occurrence and histopathological aspects

Cited by 118 publications

References 100 publications

Distribution of laminin and fibronectin isoforms in oral mucosa and oral squamous cell carcinoma

Distribution of laminin and fibronectin isoforms in oral mucosa and oral squamous cell carcinoma

Divergence of smooth muscle target and sympathetic pathway cell phenotypes in the orbit of the developing rat

Frequency‐Dependent Alternating‐Current Scanning Electrochemical Microscopy (4D AC‐SECM) for Local Visualisation of Corrosion Sites

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