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Glycobiology Advance Access originally published online on March 24, 2004
Glycobiology 2004 14(8):671-679; doi:10.1093/glycob/cwh071
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Glycobiology vol. 14 no. 8 © Oxford University Press 2004; all rights reserved.

Carbohydrate structure and differential binding of prostate specific antigen to Maackia amurensis lectin between prostate cancer and benign prostate hypertrophy

Chikara Ohyama1,2, Masahiro Hosono3, Kazuo Nitta3, Masayoshi Oh-eda4, Kazuyuki Yoshikawa5, Tomonori Habuchi2, Yoichi Arai6 and Minoru Fukuda1,7

2 Department of Urology, Akita University School of Medicine, Akita, Japan; 3 Department of Biochemistry, Cancer Research Institute, Tohoku Pharmaceutical University, Sendai, Japan; 4 Chugai Pharmaceuticals, Bio-Product Technology Laboratory, Gotenba, Japan; 5 Department of Urology, Sendai National Hospital, Sendai, Japan; 6 Department of Urology, Tohoku University School of Medicine, Sendai, Japan; and 7 Glycobiology Program, Cancer Research Center, The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037

Received on January 20, 2004; revised on February 27, 2004; accepted on February 29, 2004

Serum prostate-specific antigen (PSA) assay is widely used for detection of prostate cancer. Because PSA is also synthesized from normal prostate, false positive diagnosis cannot be avoided by the conventional serum PSA test. To apply the cancer-associated carbohydrate alteration to the improvement of PSA assay, we first elucidated the structures of PSA purified from human seminal fluid. The predominant core structure of N-glycans of seminal fluid PSA was a complex type biantennary oligosaccharide and was consistent with the structure reported previously. However, we found the sialic acid {alpha}2-3 galactose linkage as an additional terminal carbohydrate structure on seminal fluid PSA. We then analyzed the carbohydrate moiety of serum PSA from the patients with prostate cancer and benign prostate hypertrophy using lectin affinity chromatography. Lectin binding was assessed by lectin affinity column chromatography followed by determining the amount of total and free PSA. Concanavalin A, Lens culinaris, Aleuria aurantia, Sambucus nigra, and Maackia amurensis lectins were tested for their binding to the carbohydrates on PSA. Among the lectins examined, the M. amurensis agglutinin–bound fraction of free serum PSA is increased in prostate cancer patients compared to benign prostate hypertrophy patients. The binding of PSA to M. amurensis agglutinin, which recognizes {alpha}2,3-linked sialic acid, was also confirmed by surface plasmon resonance analysis. These results suggest that the differential binding of free serum PSA to M. amurensis agglutinin lectin between prostate cancer and benign prostate hypertrophy could be a potential measure for diagnosis of prostate cancer.

1 To whom correspondence should be addressed; e-mail: coyama{at}uro.med.tohoku.ac.jp; minoru{at}burnham.org


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