ArticleThe Journal of biological chemistry2010
Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 48 citations in OpenAlex.
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- Production and cryo-electron microscopy structure of an internally tagged SARS-CoV-2 spike ecto-domain construct.Journal of structural biology: X · 2025Article
- Human Angiotensin I-Converting Enzyme Produced by Different Cells: Classification of the SERS Spectra with Linear Discriminant Analysis.Biomedicines · 2022Article
- A Resourceful Race: Bacterial Scavenging of Host Sulfur Metabolism during Colonization.Infection and immunity · 2022Review
- The enzymology of human eicosanoid pathways: the lipoxygenase branches.Molecular biology reports · 2020Review
- Article
- Increased risk of acute pancreatitis occurrence in smokers with rs5751901 polymorphisms in GGT1 gene.International journal of medical sciences · 2020Article
- Clinical glycomics for the diagnosis of congenital disorders of glycosylation.Journal of inherited metabolic disease · 2018Review
- Restricted processing of CD16a/Fc γ receptor IIIaThe Journal of biological chemistry · 2018Article
- Tissue glycomics distinguish tumour sites in women with advanced serous adenocarcinoma.Molecular oncology · 2017Article
- N-glycan MALDI Imaging Mass Spectrometry on Formalin-Fixed Paraffin-Embedded Tissue Enables the Delineation of Ovarian Cancer Tissues.Molecular & cellular proteomics : MCP · 2016Article
- Blood Plasma-Derived Anti-Glycan Antibodies to Sialylated and Sulfated Glycans Identify Ovarian Cancer Patients.PloS one · 2016Article
- Non enzymatic upregulation of tissue factor expression by gamma-glutamyl transferase in human peripheral blood mononuclear cells.Thrombosis journal · 2016Article
- Tissue-Specific Glycosylation at the Glycopeptide Level.Molecular & cellular proteomics : MCP · 2015Article
- Immunolabeling of gamma-glutamyl transferase 5 in normal human tissues reveals that expression and localization differ from gamma-glutamyl transferase 1.Histochemistry and cell biology · 2015Article
- Tissue Specificity of Human Angiotensin I-Converting Enzyme.PloS one · 2015Article
- Detection of distinct glycosylation patterns on human γ-glutamyl transpeptidase 1 using antibody-lectin sandwich array (ALSA) technology.BMC biotechnology · 2014Article
- Protein and site specificity of fucosylation in liver-secreted glycoproteins.Journal of proteome research · 2014Article
- Gamma-glutamyl transpeptidase: redox regulation and drug resistance.Advances in cancer research · 2014Review
- Human GGT2 does not autocleave into a functional enzyme: A cautionary tale for interpretation of microarray data on redox signaling.Antioxidants & redox signaling · 2013Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo. GGT is expressed by a single cell type in the kidney. The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins. Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT. A total of 36 glycan compositions, with 40 unique structures, were identified by site-specific glycan analysis. Up to 15 different glycans were observed at a single site, with site-specific variation in glycan composition. N-Glycans released from liver membrane glycoproteins included many glycans also identified in the kidney. However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT. No variation in glycosylation was observed among multiple kidney and liver donors. Two glycosylation sites on renal GGT were modified exclusively by neutral glycans. In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints. This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
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