The peanut lectin-binding glycoproteins of human epidermal keratinocytes

Morrison, Alison I.; Keeble, S.; Watt, Fiona M.

doi:10.1016/0014-4827(88)90459-4

Cited by 25 publications

(14 citation statements)

References 24 publications

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“…Sections of collagen:matrigel gels were IF double-labelled with an antibody to phosphorylated Smad 2/3 (p-Smad 2/3) and the lectin, peanut agglutinin (PNA). PNA has been shown previously to bind to carbohydrates on the plasma membrane of keratinocytes (Morrison et al, 1988 (Fig. 9B).…”

Section: Loss Of Colvii In Scc Increases Expression Of the Chemokine mentioning

confidence: 58%

Increased invasive behaviour in cutaneous squamous cell carcinoma with loss of basement-membrane type VII collagen

Martins

Vyas

Chen

et al. 2009

Journal of Cell Science

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Type VII collagen (ColVII) is the main component of anchoring fibrils, attachment structures within the lamina densa of the basement membrane that are responsible for attachment of the epidermis to the dermis in skin. Mutations in the human ColVII gene, COL7A1, cause the severe inherited blistering disorder recessive dystrophic epidermolysis bullosa (RDEB) affecting skin and mucosae, associated with a greatly increased risk of skin cancer. In this study, we examined the effect of loss of ColVII on squamous cell carcinoma (SCC) tumourigenesis using RNAi in a 3D organotypic skin model. Our findings suggest that loss of ColVII promotes SCC migration and invasion as well as regulating cell differentiation with evidence for concomitant promotion of epithelial-mesenchymal transition (EMT). Immunostaining of RDEB skin and a tissue array of sporadic cutaneous SCCs confirmed that loss of ColVII correlates with decreased involucrin expression in vivo. Gene-expression-array data and immunostaining demonstrated that loss of ColVII increases expression of the chemokine ligand-receptor CXCL10-CXCR3 and downstream-associated PLC signalling, which might contribute to the increased metastatic potential of SCCs with reduced or absent ColVII expression. Together, these findings may explain the aggressive behaviour of SCCs in RDEB patients and may also be relevant to non-RDEB skin cancer, as well as other tumours from organs where ColVII is expressed.

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Section: Loss Of Colvii In Scc Increases Expression Of the Chemokine mentioning

confidence: 58%

Increased invasive behaviour in cutaneous squamous cell carcinoma with loss of basement-membrane type VII collagen

Martins

Vyas

Chen

et al. 2009

Journal of Cell Science

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“…USA 87 (1990) mens as described by Stampfer et al (17) (20). Stock cultures were grown in the presence of a feeder layer of mitomycin Ctreated 3T3 cells (21,22), in a 1:3 (vol/vol) mixture of Ham's F12 medium and DMEM containing 1.8 x 10' M adenine, 10%6 fetal calf serum, hydrocortisone (0.5 ,ug/ml), insulin (5 ,ug/ml), 10-10 M cholera toxin, and epidermal growth factor (10 ng/ml; prepared by C. George-Nascimento and generously donated by Chiron, Emeryville, CA). Experimental cultures were plated without feeder layers in a serum-free medium supplemented with bovine pituitary extract, epidermal growth factor (10 ng/ml), insulin (5 ,ug/ml), and hydrocortisone (0.5 ,g/ml) (complete KGM; Clonetics, San Diego; ref.…”

Section: Methodsmentioning

confidence: 99%

DNA amplification is rare in normal human cells.

Wright¹,

Smith

Watt

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

167

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“…Cell surface properties of keratinocytes are linked to their biological status, as shown by the modulation of glycoconjugate expression during keratinocyte differentiation, evidenced by the binding of exogenous lectins to the cell surface [31,[46][47][48]. Furthermore, cell surface glycoproteins are involved in adhesion processes [9].…”

Section: Introductionmentioning

confidence: 99%

Human keratinocyte membrane lectins: characterization and modulation of their expression by cytokines

Cerdan

Grillon

Monsigny

et al. 1991

Biology of the Cell

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In an attempt to identify cell surface molecules involved in recognition phenomena between cells such as keratinocytes and melanocytes and putatively target biological responses modifiers to keratinocytes, we undertook the detection of cell surface sugar specific receptors: membrane lectins. Keratinocyte membrane lectins were found to bind synthetic glycoproteins (neoglycoproteins) carrying either alpha-L-fucosyl or alpha-L-rhamnosyl residues. Fluorescence microscopy observations indicate that cultured keratinocytes are able to bind these two neoglycoproteins while frozen sections of human skin labelled with neoglycoprotein-coated covaspheres show that the selectivity of the binding to keratinocytes is restricted to alpha-L-rhamnosyl-BSA. Keratinocytes were adapted to grow on collagen; harvesting conditions allowing the analysis of keratinocytes by flow cytometry are described. This technique allows the quantification of the binding at 4 degrees C, and the estimation of the endocytosis of F-, neoglycoproteins: F-, alpha-L-Rha-BSA and F-, alpha-L-Fuc-BSA were efficiently internalized. Thereafter, alpha-L-rhamnose-substituted liposomes containing 5-(6)carboxyfluorescein were prepared in order to follow the delivery of the fluorescent dye into cells. This was measured both by flow cytometry and by spectrofluorimetry. The expression of surface lectins was checked upon action of cytokines (IL1 alpha, IL1 beta, IL2 and TNF) which are known as biological response modifiers of keratinocytes.

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The peanut lectin-binding glycoproteins of human epidermal keratinocytes

Cited by 25 publications

References 24 publications

Increased invasive behaviour in cutaneous squamous cell carcinoma with loss of basement-membrane type VII collagen

Increased invasive behaviour in cutaneous squamous cell carcinoma with loss of basement-membrane type VII collagen

DNA amplification is rare in normal human cells.

Human keratinocyte membrane lectins: characterization and modulation of their expression by cytokines

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