Christensen L, Johansen N, Jensen B A, Clemmensen I
Department of Pathological Anatomy, Rigshospitalet, Copenhagen, Denmark.
Histochemistry. 1987;87(3):195-9. doi: 10.1007/BF00492409.
A monospecific antibody to a plasminogen kringle 4-binding tetramer protein of human blood, tetranectin, was applied to various human endocrine tissues employing the peroxidase-antiperoxidase staining technique. Endocrine cells with a known protein or glycoprotein hormonal production such as chromophils (pituitary), follicular and parafollicular cells (thyroid), chief cells (parathyroid), hepatocytes (liver), islet cells (pancreas) and ganglion cells of the adrenal medulla displayed a convincing, positive staining reaction for tetranectin, which varied from cell to cell within the different tissues. The liver showed a distinct and universal reaction within almost all hepatocytes, thus raising suspicion of producing the bulk of tetranectin to the blood. Tetranectin has recently been characterized as a lectin-like protein with amino acid sequence homology to the core protein of a rat chondrosarcoma proteoglycan. Proteoglycans have been demonstrated in secretory granules of rat pituitary and pancreatic islet cells, where they probably serve as modulators in hormonal production. The granular, cytoplasmic immunohistochemical localization of tetranectin demonstrated in this study combined with the fact that tetranectin is known to attach to plasminogen and promote plasminogen activation catalysed by tissue plasminogen activator suggests that this protein might have a dual function, serving both as a regulator in the secretion of certain hormones and as a participant in the regulation of the limited proteolysis, which is considered important for the activation of prohormones.
采用过氧化物酶-抗过氧化物酶染色技术，将一种针对人血液中纤溶酶原kringle 4结合四聚体蛋白（腱生蛋白）的单特异性抗体应用于各种人类内分泌组织。已知能产生蛋白质或糖蛋白激素的内分泌细胞，如嗜色细胞（垂体）、滤泡细胞和滤泡旁细胞（甲状腺）、主细胞（甲状旁腺）、肝细胞（肝脏）、胰岛细胞（胰腺）以及肾上腺髓质的神经节细胞，对腱生蛋白呈现出令人信服的阳性染色反应，不同组织中的细胞反应各不相同。肝脏几乎所有肝细胞都显示出明显且普遍的反应，因此怀疑肝脏是血液中大部分腱生蛋白的产生部位。腱生蛋白最近被鉴定为一种凝集素样蛋白，其氨基酸序列与大鼠软骨肉瘤蛋白聚糖的核心蛋白具有同源性。蛋白聚糖已在大鼠垂体和胰岛细胞的分泌颗粒中得到证实，它们可能在激素产生过程中起调节作用。本研究中显示的腱生蛋白的颗粒状细胞质免疫组化定位，结合腱生蛋白已知能附着于纤溶酶原并促进组织纤溶酶原激活剂催化的纤溶酶原激活这一事实，表明该蛋白可能具有双重功能，既作为某些激素分泌的调节剂，又作为有限蛋白水解调节的参与者，而有限蛋白水解被认为对激素原的激活很重要。
