Carbohydrate expression and modification during keratinocyte differentiation in normal human and reconstructed epidermis

Méhul, Bruno; Corre, Christophe; Capon, Catherine; Bernard, Dominique; Schmidt, Rainer

doi:10.1034/j.1600-0625.2003.00049.x

Cited by 13 publications

(15 citation statements)

References 43 publications

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“…This suggests that PNA does not recognize galactose moieties located at the nonreducing terminus of N-linked oligosaccharides. This conclusion agrees with previous studies which suggested that the main oligosaccharide sequence recognized by PNA, Galb(1-3) GalNAc, is located at the nonreducing end of O-linked oligosaccharides (Chacko and Appukuttan, 2001;Mehul et al, 2003). In both cases, the surface mucous cells were not stained apart from the perinuclear region in some cells.…”

Section: Discussionsupporting

confidence: 92%

Histochemical Demonstration of Two Subtypes of O‐linked Oligosaccharides in the Rat Gastric Glands

Gomez-Santos

Alonso

Ferrer

et al. 2007

Microscopy Res & Technique

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The gastric glands synthesize glycoproteins whose oligosaccharides are linked to the peptide core mainly by the O-glycosidic bond, specifically removed by beta-elimination procedure. Our aim was to research the possibility of the existence of two subtypes of O-linked oligosaccharides with a different behavior to the removal procedure. The lectins from peanut (PNA) and Maackia amurensis (MAA-I) were histochemically used as markers of the O-linked oligosaccharides. Sections were also pretreated with beta-elimination and/or peptide N-Glycosidase F (PNGase-F) for the specific removal of O- and N-linked oligosaccharides, respectively. The lectin GNA, which mainly labels to N-linked oligosaccharides, was used to test the correct working of PNGase-F. To test the possibility that the beta-elimination treatment could remove the terminal sialic acid residues, the lectin LFA was used. The surface epithelium was negative to PNA, while it became strongly positive when beta-elimination was performed for 1 day. This staining was resistant to PNGase-F, suggesting that PNA was labeling to O-linked oligosaccharides. However, after beta-elimination for 5 days this staining is not observed. A similar pattern appeared with MAA-I. We propose the existence of two subtypes of O-linked oligosaccharides: labile and resistant. The labile O-linked oligosaccharides are removed with beta-elimination for 1 day, unmasking the PNA-positive oligosaccharides. These oligosaccharides are resistant O-linked oligosaccharides because staining is abolished with longer treatment of beta-elimination. The results with MAA-I also support this suggestion. In summary, the labile O-linked oligosaccharides are removed with short treatment, while the resistant O-linked oligosaccharides need a stronger procedure (for 5 days).

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Section: Discussionsupporting

confidence: 92%

Histochemical Demonstration of Two Subtypes of O‐linked Oligosaccharides in the Rat Gastric Glands

Gomez-Santos

Alonso

Ferrer

et al. 2007

Microscopy Res & Technique

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“…This lack of reaction to lectins may be due to the occurrence of glycosidases in this layer (Chang et al 1991). Alternatively, it may be the result of limited accessibility of the corresponding carbohydrate residues in the dense lipid-rich environment of corneocytes (Mehul et al 2003). The latter hypothesis is supported by the detection of glycoproteins in the horny layer by lectin-affinity chromatography and of Con Aand WGA-binding to delipidized corneocytes (Brysk andMiller 1984, Watt andJones 1992).…”

Section: Discussionmentioning

confidence: 99%

Qualitative and quantitative alterations of cell surface carbohydrate residues during epidermal morphogenesis

et al. 2005

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The purpose of this study was to investigate the carbohydrate residue composition of cell surface in the developing epidermis and to define the chronological sequence of its alterations in human fetuses from the 10th to the 20th weeks of gestation and at the 23rd week of gestation, using a panel of six biotinylated lectins: Concanavalin A, Ulex europaeus agglutinin-I, Ricinus communis agglutinin-I, Peanut agglutinin, Wheat germ agglutinin, and Dolichos biflorus agglutinin. Distinct qualitative and quantitative alterations in the expression of cell surface carbohydrate residues were found during epidermal morphogenesis prior to keratinization (10th to 20th weeks). At the 23rd week of gestation, the already keratinized fetal human epidermis revealed a pattern of cell surface glycosylation very similar to that of the adult human epidermis. Further studies are now warranted to answer the question regarding whether the glycosylation pattern in the developing human epidermis is disturbed in fetuses with genodermatoses and whether these disturbances might be important for prenatally diagnosing the latter.

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“…However, these antibodies stained HaCaT cells. Because glycosylation of C4.4A shows great variability and glycosylation of keratinocytes depends on the differentiation status (Mehul et al, 2003), it becomes likely that the restricted epidermal staining patterns by distinct anti-C4.4A antibodies are a consequence of C4.4A glycosylation that may hide the respective epitopes.…”

Section: Discussionmentioning

confidence: 99%

C4.4A as a candidate marker in the diagnosis of colorectal cancer

et al. 2007

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C4.4A is a member of the Ly-6 family with restricted expression in non-transformed tissues. C4.4A expression in human cancer has rarely been evaluated. Thus, it became important to explore C4.4A protein expression in human tumour tissue to obtain an estimate on the frequency of expression and the correlation with tumour progression, the study focusing on colorectal cancer. The analysis of C4.4A in human tumour lines by western blot and immunoprecipitation using polyclonal rabbit antibodies that recognize different C4.4A epitopes revealed C4.4A oligomer and heavily glycosylated C4.4A isoform expression that, in some instances, inhibited antibody binding and interaction with the C4.4A ligand galectin-3. In addition, tumour cell lines released C4.4A by vesicle shedding and proteolytic cleavage. C4.4A was expressed in over 80% of primary colorectal cancer and liver metastasis with negligible expression in adjacent colonic mucosa, inflamed colonic tissue and liver. This compares well with EpCAM and CO-029 expression in over 90% of colorectal cancer. C4.4A expression was only observed in about 50% of pancreatic cancer and renal cell carcinoma. By de novo expression in colonic cancer tissue, we consider C4.4A as a candidate diagnostic marker in colorectal cancer, which possibly can be detected in body fluids.

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Carbohydrate expression and modification during keratinocyte differentiation in normal human and reconstructed epidermis

Cited by 13 publications

References 43 publications

Histochemical Demonstration of Two Subtypes of O‐linked Oligosaccharides in the Rat Gastric Glands

Histochemical Demonstration of Two Subtypes of O‐linked Oligosaccharides in the Rat Gastric Glands

Qualitative and quantitative alterations of cell surface carbohydrate residues during epidermal morphogenesis

C4.4A as a candidate marker in the diagnosis of colorectal cancer

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