INVITRO ACETYLATION OF RAT PULMONARY SURFACTANT-ASSOCIATED GLYCOPROTEIN(S) A PRIMARY TRANSLATION PRODUCTS
INVITRO ACETYLATION OF RAT PULMONARY SURFACTANT-ASSOCIATED GLYCOPROTEIN(S) A PRIMARY TRANSLATION PRODUCTS
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DOI：
10.1016/0167-4838(86)90073-7
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发表时间：
1986-02-14
期刊：
影响因子：
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通讯作者：
WHITSETT, JA
中科院分区：
文献类型：
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作者：
WEAVER, TE;HULL, WM;WHITSETT, JA
肺表面活性剂相关糖蛋白 A（哺乳动物表面活性剂中的主要载脂蛋白）的主要翻译产物表现出广泛的电荷异质性。对大鼠肺中的 Poly(A)+ mRNA 进行体外翻译后，糖蛋白 A 的主要翻译产物被鉴定为 26 kDa (pI 4.6-5.0) 5 种蛋白质上的电荷序列，主要形式是酸性较强的成员 (pI < 4.8)。大鼠肺 Poly(A)+ mRNA 体外翻译过程中乙酰化的抑制导致更基本的亚型占主导地位 (pI≥4.8)。在用衣霉素处理后或用内切糖苷酶 H 去糖基化后，从大鼠 II 型上皮细胞中免疫沉淀糖蛋白 A 的细胞内形式。鉴定出主要由电荷序列的酸性成员组成的五种细胞内前体，这与蛋白质的细胞内乙酰化一致。相比之下，犬糖蛋白A翻译产物仅由三种26 kDa的蛋白质组成(pI 4.8-5.0)，其中大部分放射性标记集中在更碱性的成分中。乙酰化可能解释了大鼠中表面活性剂相关糖蛋白 A 的初级翻译产物和加工形式中的部分但不是全部电荷异质性。
The primary translation products of pulmonary surfactant-associated glycoprotein(s) A, the major apolipoprotein in mammalian surfactants, exhibit extensive charge heterogeneity. After in vitro translation of poly(A)+ mRNA from rat lung, the primary translation products of glycoprotein(s) A were identified as a charge train on five proteins of 26 kDa (pI 4.6-5.0), the predominant forms being the more acidic members (pI < 4.8). Inhibition of acetylation during in vitro translation of rat lung poly(A)+ mRNA resulted in a predominance of the more basic isoforms (pI .gtoreq. 4.8). Intracellular forms of glycoprotein(s) A were immunoprecipitated from rat Type II epithelial cells after treatment with tunicamycin or after deglycosylation with endoglycosidase H. Five intracellular precursors consisting primarily of acidic members of the charge train were identified, this being consistent with the intracellular acetylation of the protein. In contrast, canine glycoprotein(s) A translation products consisted of only three proteins of 26 kDa (pI 4.8-5.0), in which most of the radiolabel was concentrated in the more basic components. Acetylation may account for some, but not all, of the charge heterogeneity in the primary translation products and processed forms of surfactant-associated glycoprotein(s) A in the rat.