A Monoclonal Antibody Against γ-Glutamyltransferase From Human Primary Hepatoma: Its Use in Enzyme-Linked Immunosorbent Assay of Sera of Cancer Patients2

Taniguchi, Naoyuki; House, Stephanie; Kuzumaki, Noboru; Yokosawa, Noriko; Yamagiwa, Saburo; Iizuka, Susumu; Makita, Akira; Sekiya, Chihiro

doi:10.1093/jnci/75.5.841

Cited by 28 publications

(11 citation statements)

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“…Although several anti-GGT monoclonal antibodies have been described that reacted with tissues of normal human kidney [4,22], or hepatocellular carcinoma [26], our mAb 138Hll is the only of these mAbs that proved to be specifically reactive with GGT from human renal cell carcinomas [8].…”

Section: Discussionmentioning

confidence: 78%

Differential diagnosis of histogenetically distinct human epithelial renal tumours with a monoclonal antibody against γ-glutamyltransferase

Fischer

Störkel

Haase

et al. 1991

Cancer Immunol Immunother

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The localization of membrane-bound gamma-glutamyltransferase with monoclonal antibody (mAb) 138H11 proved to be of value for differential diagnosis of renal cancer, since it correlated with the histogenetic profile of human epithelial renal tumors. Immunoreactive gamma-glutamyltransferase was located in the proximal tubule in all normal human kidneys (15/15) examined thus far by both ultrastructural and immunohistochemical techniques. From 68 epithelial renal cancers tested 31/31 clear-cell carcinomas and 15/16 chromophilic carcinomas expressed the target epitope of mAb 138H11. In contrast, 0/11 oncytomas, 0/9 chromophobic carcinomas, and 0/1 Duct-Bellini carcinoma were immunoreactive. These results support a model of histogenesis and classification of epithelial renal tumours, according to which clear-cell and chromophilic renal carcinomas originate from transformed proximal tubule cells, whereas oncocytomas, chromophilic and Duct-Bellini carcinomas originate from cells of the collecting duct.

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Section: Discussionmentioning

confidence: 78%

Differential diagnosis of histogenetically distinct human epithelial renal tumours with a monoclonal antibody against γ-glutamyltransferase

Fischer

Störkel

Haase

et al. 1991

Cancer Immunol Immunother

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“…5A), and the resulting chimeric protein was expressed in COS cells. As revealed by immunofluorescence microscopic analysis using anti-GGT antibody (30), the insertion of the domain had a dramatic effect on the localization of the protein: the chimeric protein was localized in the intracellular organelles, predominantly the Golgi apparatus, in contrast to the cell surface expression of the nonchimeric GGT (Fig. 5B).…”

Section: Resultsmentioning

confidence: 99%

The Critical Role of the Stem Region as a Functional Domain Responsible for the Oligomerization and Golgi Localization of N-Acetylglucosaminyltransferase V

Sasai¹,

Ikeda²,

Tsuda³

et al. 2001

Journal of Biological Chemistry

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We demonstrated that a region in the stem of N-acetylglucosaminyltransferase V (GnT-V), a Golgi resident protein, is not required for enzyme activity but serves as functional domain, responsible for intracellular localization. Deletion of the domain led to complete retention of the kinetic properties but resulted in the cell surface localization of the enzyme as well as its efficient secretion into the medium. The lack of this domain concomitantly abolished the disulfide-mediated oligomerization of GnT-V, which appears to confer the Golgi retention. When the domain was inserted into the stem region of a cell surface-localized type II membrane protein, the resulting chimeric protein was substantially oligomerized and predominantly localized in the intracellular organelle. Furthermore, it was found that the presence of this domain is exclusively responsible for homo-oligomer formation. This homophilic interaction appears to involve a hydrophobic cluster of residues in the ␣-helix of the domain, as indicated by secondary structure predictions. These findings suggest that the domain specifically participates in the Golgi retention of GnT-V, probably via inducing homo-oligomer formation, and would also provide a possible mechanism for the oligomerization, which is critical for localization in the Golgi.␤1,6-N-Acetylglucosaminyltransferase V (EC 2.4.1.155, GnT-V), 1 a type II membrane protein that is localized in the Golgi apparatus, is involved in the biosynthesis of Asn-linked oligosaccharides. The enzyme catalyzes the transfer of a GlcNAc residue from UDP-GlcNAc to an ␣1,6-linked mannose moiety of Asn-linked oligosaccharides via a ␤1,6-linkage (1, 2).

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“…Expression of GGT is elevated in hepatic diseases and chronic alcoholism (33,36,37), which are frequently accompanied with osteopenia and osteoporosis (38,39). Recently, it has been reported that OPG prevents an ethanol-mediated bone loss by inhibiting osteoclast formation (40).…”

Section: Discussionmentioning

confidence: 99%

γ-Glutamyltranspeptidase Stimulates Receptor Activator of Nuclear Factor-κB Ligand Expression Independent of Its Enzymatic Activity and Serves as a Pathological Bone-resorbing Factor

Niida¹,

Kawahara

Ishizuka³

et al. 2004

Journal of Biological Chemistry

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A novel bone-resorbing factor was cloned using an expression cloning technique, which involved a Xenopus oocyte expression system and an assay for osteoclast formation. A candidate clone was isolated from a BW5147 mouse T-lymphoma cell cDNA library. Sequencing analysis identified the factor as ␥-glutamyltranspeptidase (GGT), which is an enzyme involved in glutathione metabolism. The addition of purified GGT protein to mouse bone marrow culture effectively induced formation of osteoclasts. An antibody against GGT inhibited osteoclast formation but not the enzymatic activity. We also demonstrated that an inactive form of GGT, the enzymatic activity of which had been blocked by chemical modification with a specific inhibitor, acivicin, supported osteoclast formation. These results indicate that GGT acts on osteoclast formation independent of its own enzymatic activity. Furthermore, both native GGT and inactive GGT stimulated the expression of the receptor activator of nuclear factor-B ligand (RANKL) mRNA and protein from bone marrow stromal cells. This report is the first demonstration of a novel biological activity of GGT protein in a manner independent of its enzymatic activity.

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A Monoclonal Antibody Against γ-Glutamyltransferase From Human Primary Hepatoma: Its Use in Enzyme-Linked Immunosorbent Assay of Sera of Cancer Patients2

Cited by 28 publications

References 0 publications

Differential diagnosis of histogenetically distinct human epithelial renal tumours with a monoclonal antibody against γ-glutamyltransferase

Differential diagnosis of histogenetically distinct human epithelial renal tumours with a monoclonal antibody against γ-glutamyltransferase

The Critical Role of the Stem Region as a Functional Domain Responsible for the Oligomerization and Golgi Localization of N-Acetylglucosaminyltransferase V

γ-Glutamyltranspeptidase Stimulates Receptor Activator of Nuclear Factor-κB Ligand Expression Independent of Its Enzymatic Activity and Serves as a Pathological Bone-resorbing Factor

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