Abstract
Adult Aplysia gonad contains high levels of a galactophilic lectin (MW around 65 kDa; composed of 2 subunits of apparent single species). It binds galactose and various a/ß-galactosides (but not N-acetylgalactosamine), in addition to an outstanding high affinity for galacturonic acid. This lectin is relatively resistant to heating up to 70°C and to alkaline pH, but sensitive to proteolysis and low pH. It resembles galectins in binding to poly LacNAc (preferentially branched) complexes at low temperatures (0°-4°C) more avidly than at room temperature or at 37°C, but differs from them in being Ca2+-dependent. It agglutinates papain/sialidase-treated erythrocytes more strongly than untreated cells and stimulates mitosis in peripheral human lymphocytes (inducing IL-2 formation). This lectin also enhances neurite outgrowth and increases their viability, while suppressing cell tumorigenicity. It is useful for histochemical/ cytochemical studies of galacturonic acid in plant tissues and fungi and for the study of cell surface composition of various prokaryotic (including halophilic Archaea) and eukaryotic cells and for their typing. It is useful as a reagent for I-antigen detection in adult human erythrocytes (anti-I), exhibiting strongest agglutination of 0(h) Bombay-type erythrocytes and also exhibits sensitivity to the T antigen. It binds galactosylated molecules in human body fluids (shown by hemagglutination - inhibition tests), including saliva, seminal fluid and milk (detecting individual divergence) and in fowl egg albumens (exhibiting highest affinity for that of pigeon). Therefore, it might be valuable as a probe and fishhook for fishing compounds exhibiting anti-bacterial/neoplastic cell adhesion activities.
Article FootNote
This review summarizes research work which involved several coworkers and collaborators over an 18-year-period. Among them: Prof. A. Susswein and Ms. S. Markovici, who kindly supplied us the Aplysia gonads and eggs, Ms. L. Mizrahi, Dr. D. Zipris, Dr. D. Avichezer, Dr. D. Sudakevitz, Dr. C. Levene, Ms. H. Mymon, Prof. A. Oren, Ms. B. LeITer and Ms, E. Lesman-Movshovich, all of them from Israel, as well as Prof. N. Benhamou et al., from Quebec, Canada. Thanks to all of them and to Ms. S. Victor and Ms. A. Goldreich, for the skillful preparation of this manuscript, and Ms. E. Gindi and Ms. T. Anker, for the graphic and photographic presentation of this manuscript. The research was supported by Bar-Han cancer research funds. This work was also supported by Grant 676 from the Chang-Gung Medical Research Project, Kwei-san, Taiwan, and Grant NSC 89-2320-B-182-003 from the National Science Council, Taipei, Taiwan.
Article FootNote
The abbreviations used are: AGL, Aplysia gonad lectin; Con A, Concanavalin A; E. coli, Escherichia coli; Gal, o-galactopyranose; GaINAc, N-acetyl-D-galactosamine; GaIUA, galacturonic acid; Gle, glucose; GleNAc, N-acetyl-D-glucosamine; GleUA, glucuronic acid; Met-alp Gal, methyl derivative of alp-Gal; LacNAc, N-acetyllactosamine; MPL, Maclura porni/era lectin; PHA, phytohemagglutinin (from Phaseolus vulgaris seeds); PNA, peanut agglutinin.
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Gilboa-Garber, N., Wu, A.M. (2001). Binding Properties and Applications of Aplysia Gonad Lectin. In: Wu, A.M. (eds) The Molecular Immunology of Complex Carbohydrates —2. Advances in Experimental Medicine and Biology, vol 491. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1267-7_8
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