Insogna K L, Stewart A F, Morris C A, Hough L M, Milstone L M, Centrella M
Department of Internal Medicine, Yale University School of Medicine, New Haven, Connecticut 06510.
J Clin Invest. 1989 Mar;83(3):1057-60. doi: 10.1172/JCI113947.
A human parathyroid-like protein (PLP) has recently been isolated and cloned from human tumors associated with the paraneoplastic syndrome, humoral hypercalcemia of malignancy. PLP shares NH2-terminal amino acid sequence similarity with PTH but has a unique primary structure thereafter. Studies reported to date have indicated that both native and synthetic amino-terminal PLP polypeptides display actions in vivo and in vitro that are similar to those of PTH. We report here that purified native PLP and synthetic 36Tyr(1-36)amide human PLP induce epidermal growth factor-dependent transformation of NRK 49F cells in soft agar. Further, the synthetic peptide induces a significant increase in the biosynthesis of fibronectin by human dermal fibroblasts. (1-34)PTH does not display either of these biological activities. These data indicate that there are qualitative differences between PTH and the recently identified PLP. The latter hormone appears to possess transforming growth factor-like properties that may be relevant to its physiological actions.
最近，一种人甲状旁腺样蛋白（PLP）已从与副肿瘤综合征（恶性肿瘤体液性高钙血症）相关的人类肿瘤中分离并克隆出来。PLP与甲状旁腺激素（PTH）在氨基末端氨基酸序列上具有相似性，但此后具有独特的一级结构。迄今为止报道的研究表明，天然和合成的氨基末端PLP多肽在体内和体外均表现出与PTH相似的作用。我们在此报告，纯化的天然PLP和合成的36Tyr(1 - 36)酰胺人PLP在软琼脂中诱导NRK 49F细胞发生表皮生长因子依赖性转化。此外，合成肽可显著增加人皮肤成纤维细胞中纤连蛋白的生物合成。(1 - 34)PTH不具有这两种生物学活性。这些数据表明PTH与最近鉴定出的PLP之间存在质的差异。后一种激素似乎具有类似转化生长因子的特性，这可能与其生理作用相关。
