Końska Grazyna, Wójtowicz Urszula, Pituch-Noworolska Anna
Katedra i Zakład Botaniki Farmaceutycznej Collegium Medicum, Uniwersytetu Jagiellońskiego w Krakowie.
Przegl Lek. 2008;65(4):189-94.
Lectins are proteins or glyco-proteins binding selectively and without the involvement of enzymes specific for carbohydrate ligands. Lectins are present in organisms on different levels of evolutionary development and play very important roles in life processes of these organisms. Lectins' functioning mechanism is based on the reaction of glycolysation. In vertebrates, functions of lectins are connected with cell recognition, proliferation control, adhesion, cell differentiation, mechanisms of organ creation, and defense mechanisms. Due to their ability to bind reversibly with specific carbohydrate structures, Lectins have commonly been used as a perfect molecular tool in various disciplines of biology and medicine. With the use of modern methods of lectin affinity chromatography (LAC) and various histochemistry methods, lectins provide practical application during observation of changes occurring in the cell membrane in different stages of physiological and pathological development of human or animal organisms. What is particularly important is lectins' contribution to studies on the isolation and structure of glycoconjugates in clinical pathology (including processes of tumor transformation). Serology was the first discipline of medicine relying on the specific activity of lectins. It had been based on the discoveries (by Rekonen in 1948 and Nowell in 1960) that proved that some lectins are able to bind with human and animal blood group antigens. Another discovery (by Nowell in 1960s) of mitogenic effect of PHA on human lymphocytes made lectins helpful and commonly used in the diagnosis of genetic conditions in several diseases. Proving that lectins bind differently with glycoconjugates of normal and tumor cells and are able to detect subtle neoplastic changes was a clue that lectins can be precious and useful in cancer treatment and diagnostics. For many years lectins inducing apoptosis, with immuno-modulatory or antiproliferative activity and toxic lectins belonging to II-RIP class (Ribosome Inactivating Proteins like viscumin, ricin) have been intensively examined in therapy of various diseases, esp. in cancer. Currently the use of lectins in drug targeting is being examined (lectins as drug-carriers, the preparation of bioadhesive "Second Generation" drug-delivery systems). Paper presents below is an attempt at collecting the latest information on diagnostic and therapeutic application possibilities of lectins.
凝集素是一类蛋白质或糖蛋白,它们能选择性地结合碳水化合物配体,且无需特定酶的参与。凝集素存在于不同进化发展水平的生物体中,并在这些生物体的生命过程中发挥着非常重要的作用。凝集素的作用机制基于糖基化反应。在脊椎动物中,凝集素的功能与细胞识别、增殖控制、黏附、细胞分化、器官形成机制以及防御机制相关。由于凝集素能够与特定的碳水化合物结构可逆结合,它们在生物学和医学的各个学科中通常被用作一种完美的分子工具。通过使用现代凝集素亲和色谱法(LAC)和各种组织化学方法,凝集素在观察人类或动物生物体生理和病理发展不同阶段细胞膜发生的变化时具有实际应用价值。特别重要的是,凝集素在临床病理学(包括肿瘤转化过程)中对糖缀合物的分离和结构研究做出了贡献。血清学是医学中最早依赖凝集素特异性活性的学科。它基于(1948年由雷科宁和1960年由诺威尔)的发现,即证明某些凝集素能够与人及动物血型抗原结合。20世纪60年代诺威尔的另一项发现,即PHA对人淋巴细胞的促有丝分裂作用,使得凝集素在几种疾病的遗传状况诊断中变得有用且常用。证明凝集素与正常细胞和肿瘤细胞的糖缀合物结合方式不同,并能够检测到细微的肿瘤变化,这提示凝集素在癌症治疗和诊断中可能是宝贵且有用的。多年来,具有诱导凋亡、免疫调节或抗增殖活性的凝集素以及属于II - RIP类的有毒凝集素(如相思豆毒素、蓖麻毒素等核糖体失活蛋白)在各种疾病,尤其是癌症的治疗中得到了深入研究。目前正在研究凝集素在药物靶向中的应用(凝集素作为药物载体,制备生物黏附性“第二代”药物递送系统)。下面这篇论文旨在收集关于凝集素诊断和治疗应用可能性的最新信息。