Radioimmunoscintigraphy of Pelvic Lymph Nodes with<sup>111</sup>Indium-Labeled Monoclonal Antibody CYT-356

Babaian, R. Joseph; Sayer, Jeanie; Podoloff, Donald A.; Steelhammer, L.; Bhadkamkar, Viju; Gulfo, Joseph V.

doi:10.1016/s0022-5347(17)32277-2

Cited by 126 publications

(56 citation statements)

References 11 publications

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“…Faint expression of PSMA protein has been detected in normal human renal tubular cells (Lopes et al, 1990;Babain et al, 1994). Moreover, one putative homologue, a rat brain NAADLase which discloses a strong cDNA homology with PSMA has also been found in rat …”

Section: Discussionmentioning

confidence: 99%

Molecular expression of PSMA mRNA and protein in primary renal tumors

Dumas¹,

Gala

Berteau³

et al. 1999

Int. J. Cancer

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Section: Discussionmentioning

confidence: 99%

Molecular expression of PSMA mRNA and protein in primary renal tumors

Dumas¹,

Gala

Berteau³

et al. 1999

Int. J. Cancer

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“…Moreover, PSMA is present at the surface of endothelial cells found in tumors of different histotype but absent from normal endothelial cells (10). Radioimmunoconjugates of anti-PSMA monoclonal antibodies (mAbs) are currently used as imaging agents for prostate cancer (11). Moreover, it has been observed that, following contact with antibodies, PSMA is rapidly and efficiently internalized by the target cell and localizes in a juxtanuclear region of the cell (12).…”

mentioning

confidence: 99%

Apical Transport and Folding of Prostate-specific Membrane Antigen Occurs Independent of Glycan Processing

Castelletti¹,

Fracasso

Alfalah³

et al. 2006

Journal of Biological Chemistry

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Prostate-specific membrane antigen (PSMA) is an integral cellsurface membrane glycoprotein that is overexpressed in prostate carcinomas rendering it an appropriate target for antibody-based therapeutic strategies. The biosynthesis of PSMA in transfected COS-1 cells reveals a slow conversion of mannose-rich to complex glycosylated PSMA compatible with slow transport kinetics from the endoplasmic reticulum to the Golgi. Importantly, mannose-rich PSMA persists as a trypsin-sensitive protein throughout its entire life cycle, and only Golgi-located PSMA glycoforms acquire trypsin resistance. This resistance, used here as a tool to examine correct folding, does not depend on the type of glycosylation, because different PSMA glycoforms generated in the presence of inhibitors of carbohydrate processing in the Golgi are also trypsin resistant. The conformational transition of PSMA to a correctly folded molecule is likely to occur in the Golgi and does not implicate ER molecular chaperones, such as BiP. We show here that PSMA is not only heavily N-but also O-glycosylated. The question arising is whether glycans, which do not play a role in folding of PSMA, are implicated in its transport to the cell surface. Neither the cell-surface expression of PSMA nor its efficient apical sorting in polarized Madin-Darby canine kidney cells are influenced by modulators of N-and O-glycosylation. The acquisition of folding determinants in the Golgi, therefore, is an essential prerequisite for protein trafficking and sorting of PSMA and suggests that altered or aberrant glycosylation often occurring during tumorigenesis has no regulatory effect on the cell-surface expression of PSMA.

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“…CT scanning will only detect nodes greater than 1.5 cm, whereas 111 In labelled Cyt-356 has been shown to visualise those as small as 5 mm. 7 In that study the immunolabelled mAb was found to provide 30±40% higher sensitivity than CT scanning or MRI alone. Krynyckyi et al, 8 carried out a multicentre trial including both pre-and postoperative patients with biopsy proven prostate cancer.…”

Section: Anti-psm (Folh1) Monoclonal Antibodies In the Management Of mentioning

confidence: 85%

Prostate-specific membrane antigen (FOLH1): recent advances in characterising this putative prostate cancer gene

Maraj

Markham

1999

Prostate Cancer Prostatic Dis

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Radioimmunoscintigraphy of Pelvic Lymph Nodes with¹¹¹Indium-Labeled Monoclonal Antibody CYT-356

Cited by 126 publications

References 11 publications

Molecular expression of PSMA mRNA and protein in primary renal tumors

Molecular expression of PSMA mRNA and protein in primary renal tumors

Apical Transport and Folding of Prostate-specific Membrane Antigen Occurs Independent of Glycan Processing

Prostate-specific membrane antigen (FOLH1): recent advances in characterising this putative prostate cancer gene

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Radioimmunoscintigraphy of Pelvic Lymph Nodes with111Indium-Labeled Monoclonal Antibody CYT-356

Cited by 126 publications

References 11 publications

Molecular expression of PSMA mRNA and protein in primary renal tumors

Molecular expression of PSMA mRNA and protein in primary renal tumors

Apical Transport and Folding of Prostate-specific Membrane Antigen Occurs Independent of Glycan Processing

Prostate-specific membrane antigen (FOLH1): recent advances in characterising this putative prostate cancer gene

Contact Info

Product

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Radioimmunoscintigraphy of Pelvic Lymph Nodes with¹¹¹Indium-Labeled Monoclonal Antibody CYT-356