Protein glycosylation in development and disease

Dennis, James W.; Granovsky, Maria; Warren, Charles E.

doi:10.1002/(sici)1521-1878(199905)21:5<412::aid-bies8>3.0.co;2-5

Cited by 395 publications

(267 citation statements)

References 75 publications

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“…Average of mean fluorescence intensities and standard deviations (SD) are calculated based on many independent experiments.-2 Average of mean fluorescence intensities 6 SD for lectins and antibodies based on 3 replications is shown. nd, not determined.- 3 Mouse IgG and IgM were used as negative controls for antibody staining.…”

Section: Sle X Is the Major Carbohydrate Determinant That Differs Betmentioning

confidence: 99%

“…1,2 Tissue invasion and metastasis of tumor cells are highly dependent on cell-cell interactions, many of which involve alterations in cell surface glycosylation patterns. 3,4 Although adhesion pathways utilized by tumor cells show considerable diversity, members of the selectin family of molecules and numerous neolactoseries antigens highly expressed on the tumor cell surface are involved in tumor metastasis by mediating binding of blood-borne tumor cells via E-and/or P-selectin to vascular endothelium. [5][6][7][8][9][10] Much of what we know about selectin interactions comes from studies of leukocytes.…”

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confidence: 99%

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Deficiency in surface expression of E‐selectin ligand promotes lung colonization in a mouse model of breast cancer

Monzavi‐Karbassi

Whitehead

Jousheghany

et al. 2005

Intl Journal of Cancer

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Expression of sialyl Lewis x (sLe x ) and sLe a on tumor cells is thought to facilitate metastasis by promoting cell adhesion to selectins on vascular endothelial cells. Experiments supporting this concept usually bypass the early steps of the metastatic process by employing tumor cells that are injected directly into the blood. We investigated the relative role of sLe x oligosaccharide in the dissemination of breast carcinoma, employing a spontaneous murine metastasis model. An sLe x deficient subpopulation of the 4T1 mammary carcinoma cell line was produced by negative selection using the sLe x -reactive KM93 MAb. This subpopulation was negative for E-selectin binding but retained P-selectin binding. Both sLe x -negative and -positive cells grew at the same rate; however, sLe x -negative cells spread more efficiently on plates and had greater motility in wound-scratch assays. Mice inoculated in the mammary fat pad with sLe x -negative and -positive variants produced lung metastases. However, the number of lung metastases was significantly increased in the group inoculated with the sLe x -negative variant (p 5 0.0031), indicating that negative selection for the sLe x epitope resulted in enrichment for a subpopulation of cells with a high metastatic phenotype. Cell variants demonstrated significant differences in cellular morphology and pattern of tumor growth in primary and secondary tumor sites. These results strongly suggest that loss of sLe x may facilitate the metastatic process by contributing to escape from the primary tumor mass. ' 2005 Wiley-Liss, Inc.Key words: sialyl Lewis x antigen; metastasis; 4T1 cells; breast cancer Tumor metastasis is a multistep process requiring detachment of malignant cells from the primary tumor, penetration of blood or lymph vessels, attachment to endothelium of distant organs and formation of new tumor foci. 1,2 Tissue invasion and metastasis of tumor cells are highly dependent on cell-cell interactions, many of which involve alterations in cell surface glycosylation patterns. 3,4 Although adhesion pathways utilized by tumor cells show considerable diversity, members of the selectin family of molecules and numerous neolactoseries antigens highly expressed on the tumor cell surface are involved in tumor metastasis by mediating binding of blood-borne tumor cells via E-and/or P-selectin to vascular endothelium. [5][6][7][8][9][10] Much of what we know about selectin interactions comes from studies of leukocytes. 11,12 Functionally, the binding of selectins to leukocytes requires sialylated and fucosylated carbohydrate structures; their prototypes are SAa2-3Galb1-4(Fuca1-3)GlcNAc and SAa2-3Galb1-3(Fuca1-4)GlcNAc, referred to as sLe x and sLe a , respectively. [13][14][15] Both sLe x and sLe a are involved in selectin-mediated adhesion of cancer cells to vascular endothelium, and these determinants are thought to be closely associated with hematogenous metastasis of cancers. [16][17][18][19] These determinants not only are markers for cancer but also are functionally implicated ...

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Section: Sle X Is the Major Carbohydrate Determinant That Differs Betmentioning

confidence: 99%

mentioning

confidence: 99%

Deficiency in surface expression of E‐selectin ligand promotes lung colonization in a mouse model of breast cancer

Monzavi‐Karbassi

Whitehead

Jousheghany

et al. 2005

Intl Journal of Cancer

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“…Putative N-linked glycosilation, as well as N-myristilation sites, are highly conserved between XDHCR7-L and other vertebrate DHCR7 proteins. This suggests a conserved posttranslational Golgi maturation, supporting membrane anchoring of these proteins (Masaki et al, 1996;Bhatnagar et al, 1998;Dennis et al, 1999;Farazi et al, 2001). The potential sterol-sensing domain (SSD) comprising amino acids 174 -352 of XDHCR7-L is highly conserved in all the vertebrate DHCR7 proteins compared, as only minor substitutions are present.…”

Section: Xenopus Dhcr7 Consists Of At Least Three Alternatively Splicmentioning

confidence: 75%

“…1A) are present at positions 8 -11 (NASR); 253-256 (NLSY), and 410 -413 (NYTG), as well as an N-myristilation site (bluehighlighted residues in Fig. 1A) at position 127-132 (GVQEGA), which would allow posttranslational Golgi maturation and support membrane anchoring of the protein (Masaki et al, 1996;Bhatnagar et al, 1998;Dennis et al, 1999;Farazi et al, 2001). XDHCR7-L also contains a potential sterol-sensing domain (SSD; bold residues in Fig.…”

Section: Xenopus Dhcr7 Consists Of Three Alternatively Spliced Isoformentioning

confidence: 99%

Cholesterol homeostasis in development: The role of Xenopus 7‐dehydrocholesterol reductase (Xdhcr7) in neural development

Tadjuidje¹,

Hollemann²

2006

Developmental Dynamics

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7-dehydrocholesterol reductase (7-Dhcr) catalyses the final step in the pathway of cholesterol biosynthesis. Human patients with inborn errors of 7-Dhcr (Smith-Lemli-Opitz-Syndrome) have elevated serum levels of 7-dehydrocholesterol but low levels of cholesterol, which in phenotypical terms can result in growth retardation, craniofacial abnormalities including cleft palate, and reduced metal abilities. This study reports the isolation and molecular characterisation of 7-dehydrocholesterol reductase (Xdhcr7) from Xenopus laevis. During early embryonic development, the expression of Xdhcr7 is first of all spatially restricted to the Spemann's organizer and later to the notochord. In both tissues, Xdhcr7 is coexpressed with Sonic hedgehog (Shh), which itself is cholesterol-modified during autoproteolytic cleavage. Data from Xdhcr7 overexpression and knockdown experiments reveals that a tight control of cholesterol synthesis is particularly important for proper development of the central and peripheral nervous system.

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“…Previous work has shown that AhR could undergo several types of post-translational modifications. Post-translational modifications of protein, such as phosphorylation, acetylation, methylation, glycosylation and ubiquitylation, play pivotal roles in regulation of protein function (Beevers, 1982;Dennis et al, 1999). These post-modification played important roles in AhR activation (Backlund and Ingelman-Sundberg, 2004;Powis et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Development and characterization of monoclonal antibodies against human aryl hydrocarbon receptor

Tian

Pei

Xie

et al. 2016

Journal of Environmental Sciences

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Aryl hydrocarbon receptor (AhR), a ligand-dependent nuclear receptor, is involved in a diverse spectrum of biological and toxicological effects. Due to the lack of three dimensional (3D) crystal or nuclear magnetic resonance structure, the mechanisms of these complex effects of AhR remain to be unclear. Also, commercial monoclonal antibodies (mAbs) against human AhR protein (hAhR), as alternative immunological tools, are very limited. Thus, in order to provide more tools for further studies on hAhR, we prepared two mAbs (1D6 and 4A6) against hAhR. The two newly generated mAbs specifically bound to amino acids 484-508 (located in transcription activation domain) and amino acids 201-215 (located in Per-ARNT-Sim domain) of hAhR, respectively. These epitopes were new as compared with those of commercial mAbs.The mAbs were also characterized by enzyme-linked immunosorbent assay, western blot, immunoprecipitation and indirect immunofluorescence assay in different cell lines. The results showed that the two mAbs could recognize the linearized AhRs in six different human cell lines and a rat hepatoma cell line, as well as the hAhR with native conformations. We concluded that the newly generated mAbs could be employed in AhR-based bioassays for analysis of environmental contaminants, and held great potential for further revealing the spatial structure of AhR and its biological functions in future studies.

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Protein glycosylation in development and disease

Cited by 395 publications

References 75 publications

Deficiency in surface expression of E‐selectin ligand promotes lung colonization in a mouse model of breast cancer

Deficiency in surface expression of E‐selectin ligand promotes lung colonization in a mouse model of breast cancer

Cholesterol homeostasis in development: The role of Xenopus 7‐dehydrocholesterol reductase (Xdhcr7) in neural development

Development and characterization of monoclonal antibodies against human aryl hydrocarbon receptor

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