Sugars protect desmosome and corneosome glycoproteins from proteolysis

Walsh, A.; Chapman, Stephen J.

doi:10.1007/bf00372058

Cited by 46 publications

(39 citation statements)

References 21 publications

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“…Although desmogleins and desmocollins are reported to be glycoproteins containing mainly N-glycans, detailed information about oligosaccharide structures has been so far limited (33)(34)(35). The current study also raises an interesting query: why desmosomes require high mannose glycans particularly when it is possible that any type of oligosaccharides could protect desmosomal proteins from protease degradation and may prevent premature desquamation as suggested by Walsh and Chapman (36).…”

Section: Table I Observed Signals Of Aowr-labeled Oligosaccharides Rementioning

confidence: 76%

High Throughput Quantitative Glycomics and Glycoform-focused Proteomics of Murine Dermis and Epidermis

Uematsu

Furukawa

Nakagawa

et al. 2005

Molecular & Cellular Proteomics

111

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Despite recent advances in our understanding of the significance of the protein glycosylation, the throughput of protein glycosylation analysis is still too low to be applied to the exhaustive glycoproteomic analysis. Aiming to elucidate the N-glycosylation of murine epidermis and dermis glycoproteins, here we used a novel approach for focused proteomics. A gross N-glycan profiling (glycomics) of epidermis and dermis was first elucidated both qualitatively and quantitatively upon N-glycan derivatization with novel, stable isotope-coded derivatization reagents followed by MALDI-TOF(/TOF) analysis. This analysis revealed distinct features of the N-glycosylation profile of epidermis and dermis for the first time. A high abundance of high mannose type oligosaccharides was found to be characteristic of murine epidermis glycoproteins. Based on this observation, we performed high mannose type glycoform-focused proteomics by direct tryptic digestion of protein mixtures and affinity enrichment. We The rapid progress in the sequence analysis of genomes of a variety of living organisms is accelerating the investigation of various related proteins involved in biological processes and disorders. Carbohydrate modifications can profoundly affect protein function. Their importance in disease is evident from a growing number of embryonic lethal phenotypes seen in knock-out mice with defects in glycoconjugate assembly or processing (1), and hence a large scale protein glycosylation analysis has become important.The accurate identification of protein glycosylation is challenging because of the complex structures, labile nature, and microheterogeneity of glycoproteins. The presence of nonglycopeptides in a sample also limits the sensitivity for analysis of glycopeptides on mass spectrometry due to ion suppression. Although several new techniques enabling the large scale identification of glycoproteins have recently been developed (2-4), they cannot provide information about oligosaccharide moieties because the analysis is performed on peptides of which such moieties are enzymatically removed prior to the analysis. It is also well known that glycosylation is cell type-specific, so a single glycoprotein can have a different spectrum of glycan structures when expressed in different cells. Recent progress in mass spectrometry (e.g. electron capture-induced dissociation using Fourier transform mass spectrometry (5, 6) and MALDI-LIFT-TOF/TOF (7)) has demonstrated the ability to provide information both on peptide sequence and glycan structure for the analysis of glycopeptides. However, the throughput of these techniques is not high enough to apply to large scale protein glycosylation analyses. Therefore, unveiling the significance of protein glycosylation in an efficient manner requires further thought. One solution is to develop a focused approach based on function and information content.In this study, we describe a glycomic approach to rationalize the focusing process using murine dermis and epidermis as models. A gross N-glycan profi...

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Section: Table I Observed Signals Of Aowr-labeled Oligosaccharides Rementioning

confidence: 76%

High Throughput Quantitative Glycomics and Glycoform-focused Proteomics of Murine Dermis and Epidermis

Uematsu

Furukawa

Nakagawa

et al. 2005

Molecular & Cellular Proteomics

111

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“…They could hydrolyze the sugar moieties of the extracellular parts of corneodesmosome proteins, facilitating their proteolytic degradation (62,63). However, the exact nature of the glycosidases present in the stratum corneum is not known.…”

Section: Clip-170 Association With Lamellar Bodies Of Human Epidermismentioning

confidence: 99%

Lamellar Bodies of Human Epidermis

Raymond

Peredo

Stella

et al. 2008

Molecular & Cellular Proteomics

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“…Because these nanoridges resisted the proteolysis applied and the glycoconjugates protect desmosomal material against proteolysis (Walsh and Chapman 1991), we conclude that the nanoridges originated from desmosomal-keratinaceous material. The nanoridges found were recovered in the freshly freeze-etched and aldehyde-fixed samples in this study.…”

Section: Discussionmentioning

confidence: 80%

Average nanorough skin surface of the pilot whale ( Globicephala melas , Delphinidae): considerations on the self-cleaning abilities based on nanoroughness

et al. 2002

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Abstract. In aquatic environments, the biofouling process is assumed to initiate from the conditioning layer of absorbed organic carbon residues on wetted surfaces. Microfouling organisms attach to this conditioning layer, building up a biofilm on which further biofouling proceeds. In dolphins, biofouling reduces hydrodynamic efficiency and may negatively affect health if not managed. In the present study we examined the skin surface of the pilot whale (Globicephala melas). Employing cryo-scanning electron microscopic techniques combined with various sample preparations, the skin displayed an average nanorough surface characterized by a pattern of nanoridge-enclosed pores; the average pore size (approximately 0.20 µm 2 ) was below the size of most marine biofouling organisms. Further, the implications of this type of surface to the self-cleaning abilities of the skin of pilot whales are discussed, based on reduced available space for biofouler attachment, the lack of any particular microniches as shelters for biofoulers, and the challenges of turbulent water flow and liquid-air interfaces during surfacing and jumping of the dolphin.

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Sugars protect desmosome and corneosome glycoproteins from proteolysis

Cited by 46 publications

References 21 publications

High Throughput Quantitative Glycomics and Glycoform-focused Proteomics of Murine Dermis and Epidermis

High Throughput Quantitative Glycomics and Glycoform-focused Proteomics of Murine Dermis and Epidermis

Lamellar Bodies of Human Epidermis

Average nanorough skin surface of the pilot whale ( Globicephala melas , Delphinidae): considerations on the self-cleaning abilities based on nanoroughness

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