Cloning, expression and characterization of a novel human CAP10-like gene hCLP46 from CD34+ stem/progenitor cells

Teng, Yun; Liu, Qiaohong; Ma, Jun; Liu, Feng; Han, Ze‐Guang; Wang, Youxin; Wang, Wei

doi:10.1016/j.gene.2005.08.027

Cited by 28 publications

(36 citation statements)

References 21 publications

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“…Ofut1 has been proposed to function as a chaperone in Drosophila (independent of its O-fucosyltransferase activity) (33)(34)(35), although a similar function for Pofut1 in mammals is not clear (36). Poglut/Rumi is also localized to the ER (13,15,37), suggesting that like Pofut1, it could also play a role in quality control. Elimination of Poglut/ Rumi in flies or mice does not result in decreased cell-surface expression of Notch, which would be expected if it were required for quality control of Notch folding (13,14).…”

Section: Discussionmentioning

confidence: 99%

Site-specific O-Glucosylation of the Epidermal Growth Factor-like (EGF) Repeats of Notch

Takeuchi

Kantharia

Sethi

et al. 2012

Journal of Biological Chemistry

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Background: O-Glucosylation of EGF repeats occurs at high but variable stoichiometries on Notch. Results: In vitro assays revealed that the variability in glycosylation depends on the amino acid sequence and three-dimensional structure of individual EGF repeats. Conclusion: Proper folding and amino acid sequence of individual EGF repeats determine O-glucosylation efficiency. Significance: This work provides a regulatory mechanism for site-specific O-glucosylation on individual EGF repeats.

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Section: Discussionmentioning

confidence: 99%

Site-specific O-Glucosylation of the Epidermal Growth Factor-like (EGF) Repeats of Notch

Takeuchi

Kantharia

Sethi

et al. 2012

Journal of Biological Chemistry

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“…The confocal microscopy analyses revealed the colocalization of the WT POGLUT1 with the endoplasmic reticulum (ER) for both the N-and C-TAP constructs ( Figure 4C; Figure S7) as previously reported in COS7 cells. 16 No significant difference was observed in the subcellular localization of the WT protein and the protein with the p.Arg279Trp substitution in either of the constructs ( Figure 4C; Figure S7). However, compared to the WT proteins, the truncated N-TAP-POGLUT1 appeared to form more aggregates, which coincided with an impaired colocalization with the ER ( Figure 4C).…”

Section: Dowling-degos Disease (Ddd [Mim 179850 Mim 615327])mentioning

confidence: 94%

“…Immunoblot analysis showed that the WT construct led to translation of a protein of about 50 kDa in size, which is in accordance with previous reports. 16 While the missense mutation did not alter the molecular weight, the nonsense mutation resulted in a truncated protein of about 30 kDa in size ( Figure 4B). There were no significant differences in the molecular weights between the N-TAP and C-TAP tagged proteins ( Figure S6).…”

Section: Dowling-degos Disease (Ddd [Mim 179850 Mim 615327])mentioning

confidence: 94%

Mutations in POGLUT1, Encoding Protein O-Glucosyltransferase 1, Cause Autosomal-Dominant Dowling-Degos Disease

Basmanav

Oprişoreanu

Pasternack

et al. 2014

The American Journal of Human Genetics

141

153

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Dowling-Degos disease (DDD) is an autosomal-dominant genodermatosis characterized by progressive and disfiguring reticulate hyperpigmentation. We previously identified loss-of-function mutations in KRT5 but were only able to detect pathogenic mutations in fewer than half of our subjects. To identify additional causes of DDD, we performed exome sequencing in five unrelated affected individuals without mutations in KRT5. Data analysis identified three heterozygous mutations from these individuals, all within the same gene. These mutations, namely c.11G>A (p.Trp4*), c.652C>T (p.Arg218*), and c.798-2A>C, are within POGLUT1, which encodes protein O-glucosyltransferase 1. Further screening of unexplained cases for POGLUT1 identified six additional mutations, as well as two of the above described mutations. Immunohistochemistry of skin biopsies of affected individuals with POGLUT1 mutations showed significantly weaker POGLUT1 staining in comparison to healthy controls with strong localization of POGLUT1 in the upper parts of the epidermis. Immunoblot analysis revealed that translation of either wild-type (WT) POGLUT1 or of the protein carrying the p.Arg279Trp substitution led to the expected size of about 50 kDa, whereas the c.652C>T (p.Arg218*) mutation led to translation of a truncated protein of about 30 kDa. Immunofluorescence analysis identified a colocalization of the WT protein with the endoplasmic reticulum and a notable aggregating pattern for the truncated protein. Recently, mutations in POFUT1, which encodes protein O-fucosyltransferase 1, were also reported to be responsible for DDD. Interestingly, both POGLUT1 and POFUT1 are essential regulators of Notch activity. Our results furthermore emphasize the important role of the Notch pathway in pigmentation and keratinocyte morphology.

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“…Transfection of COS-7 cells with plasmid, expressing hCLP-46, led to the acceleration of proliferation of COS -7 cells (8). Over-expression of C30RF9 in MDS cells may suggest an increased proliferation rate of these cells, which means a proliferation advantage over normal hemopoietic cells.…”

Section: Discussionmentioning

confidence: 97%

“…The XO 10 protein contains capsule-associated protein-IO domain (CAP-lO), a domain with homology to endoplasmic reticulum (ER) proteins and a hydrophobic signal peptide (8). The ER proteins help in the retention of proteins to the endoplasmic reticulum (ER).…”

mentioning

confidence: 99%

Abnormal Expression of C3ORF9 Gene in Patients with Myelodysplastic Syndromes

Karadonta

Alexandrakis

Kourelis

et al. 2009

Int J Immunopathol Pharmacol

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Myelodysplastic Syndrome (MDS) cells present genetic instability and dysregulation of the gene C30RF9, which was isolated from an MDS cDNA library and codes for a putative protein. We studied the expression of C30RF9 in MDS syndromes to contribute to the understanding of the pathophysiology of MDS. One hundred and thirty-one patients and 35 healthy controls were involved in our study. Bone marrow aspirates and isolated CD34+ cells were used. Gene expression was estimated by quantitative PCR. C3ORF9 was found to be down-regulated in patients with CMML compared to the controls (p<0.01). There was no difference between RARS and the controls (p=0.1), while increased expression was found in RA, RAEB and RAEB-T (p< 0.01 for all). No mutations or polymorphism were detected in our population. CD34+ cells expressed higher levels of C30RF9 (p<0.01) in patients. The gene expression was correlated to the percentage of + cells in RAEB and RAEB-T (r= 0.64). The altered C30RF9 expression was possibly due to different gene regulation in these patients and/or to the increased CD34+ cells.

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Cloning, expression and characterization of a novel human CAP10-like gene hCLP46 from CD34+ stem/progenitor cells

Cited by 28 publications

References 21 publications

Site-specific O-Glucosylation of the Epidermal Growth Factor-like (EGF) Repeats of Notch

Site-specific O-Glucosylation of the Epidermal Growth Factor-like (EGF) Repeats of Notch

Mutations in POGLUT1, Encoding Protein O-Glucosyltransferase 1, Cause Autosomal-Dominant Dowling-Degos Disease

Abnormal Expression of C3ORF9 Gene in Patients with Myelodysplastic Syndromes

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