Castronovo V
Metastasis Research Laboratory, University of Liège, Sart-Tilman-Liège, Belgium.
Invasion Metastasis. 1993;13(1):1-30.
Interactions between cancer cells and laminin, a major component of basement membranes, play a critical role at several steps of the complex process of tumor invasion and metastasis. These interactions are mediated through a large variety of cell surface proteins designated as laminin receptors and/or laminin-binding proteins. The growing number of identified laminin binding proteins and domains of this glycoprotein that are biologically active illustrate the complexity of cellular interactions with laminin. The 67-kD laminin receptor (67 LR) was the first protein identified in 1983 as a high-affinity laminin receptor, and its expression is dramatically increased in a large variety of cancer cells. The 67 LR is the subject of several controversies and confusion generated mainly by two events. First, the identification of several new laminin-binding proteins has raised the difficult task of attributing specific functions to specific receptors in contrast to initial beliefs that all cellular laminin-driven biological activities were mediated through the 67 LR. The second source of controversy is the large molecular-weight discrepancy between the 37-kD polypeptide encoded by the 67 LR cDNA clone and the mature 67 LR. In this manuscript, a critical and extensive review of the data accumulated on the 67 LR is presented regarding both its molecular structure and its role during tumor invasion and metastasis. A hypothetical model of the 67 LR is also proposed. Since the first identification of the 67 LR, at least 14 other cell surface molecules have been reported to be potential laminin receptors or laminin-binding proteins. These include members of the beta-galactoside-binding lectin family, seven members of the integrin family, the galactosyltransferase and some not yet fully characterized cell surface molecules. These laminin receptors and laminin-binding proteins are also described and their functions are also discussed with a particular emphasis on their participation in the constitution of the invasive phenotype.
癌细胞与层粘连蛋白（基底膜的主要成分）之间的相互作用在肿瘤侵袭和转移这一复杂过程的多个步骤中起着关键作用。这些相互作用是通过多种被称为层粘连蛋白受体和/或层粘连蛋白结合蛋白的细胞表面蛋白介导的。已鉴定出的层粘连蛋白结合蛋白以及这种糖蛋白具有生物活性的结构域数量不断增加，这说明了细胞与层粘连蛋白相互作用的复杂性。67-kD层粘连蛋白受体（67 LR）是1983年首次被鉴定为高亲和力层粘连蛋白受体的蛋白质，其在多种癌细胞中的表达显著增加。67 LR存在一些争议和混淆，主要由两件事引起。首先，几种新的层粘连蛋白结合蛋白的鉴定带来了难题，即要将特定功能归因于特定受体，这与最初认为所有由层粘连蛋白驱动的细胞生物学活性都通过67 LR介导的观点不同。第二个争议来源是67 LR cDNA克隆编码的37-kD多肽与成熟的67 LR之间存在较大的分子量差异。在本手稿中，对67 LR积累的数据进行了批判性和广泛的综述，涉及其分子结构以及在肿瘤侵袭和转移过程中的作用。还提出了67 LR的假设模型。自首次鉴定出67 LR以来，至少还有14种其他细胞表面分子被报道为潜在的层粘连蛋白受体或层粘连蛋白结合蛋白。这些包括β-半乳糖苷结合凝集素家族的成员、整合素家族的七个成员、半乳糖基转移酶以及一些尚未完全表征的细胞表面分子。本文还描述了这些层粘连蛋白受体和层粘连蛋白结合蛋白，并讨论了它们的功能，特别强调了它们在侵袭性表型构成中的作用。
