Shimoyama R, Savage C R, Boden G
J Clin Endocrinol Metab. 1985 May;60(5):928-33. doi: 10.1210/jcem-60-5-928.
The effects of two antiinsulin receptor antisera (AIRA) on alpha-amino-2-[14C]isobutyric acid [( 14C]AIB) uptake by and [125I]insulin binding to cultured rat hepatocytes were examined. Diluted 1:100, both antisera inhibited insulin binding by 75-80%, mainly by decreasing available high affinity insulin-binding sites. Diluted 1:500, they decreased insulin binding and high affinity binding sites by 35-40%. Neither antiserum had an effect on basal [14C]AIB uptake, but decreased insulin-stimulated AIB uptake by 83% (dilution, 1:100; 24-h incubation) and 25% (dilution, 1:500; 24-h incubation), respectively. Insulin stimulation of AIB uptake correlated positively (r = 0.96; P less than 0.01) with insulin binding to high affinity receptors on hepatocytes incubated with normal serum or AIRA. We conclude that: 1) insulin stimulation of amino acid uptake by hepatocytes was mediated through insulin receptors, especially high affinity binding sites, and was inhibited by AIRA in parallel with receptor blockade; and 2) AIRA had no insulin-like effect on basal amino acid uptake by hepatocytes.
研究了两种抗胰岛素受体抗血清（AIRA）对培养的大鼠肝细胞摄取α-氨基-2-[¹⁴C]异丁酸[¹⁴C]AIB以及[¹²⁵I]胰岛素结合的影响。两种抗血清稀释1:100时，均抑制胰岛素结合75 - 80%，主要是通过减少可用的高亲和力胰岛素结合位点。稀释1:500时，它们使胰岛素结合和高亲和力结合位点减少35 - 40%。两种抗血清对基础[¹⁴C]AIB摄取均无影响，但分别使胰岛素刺激的AIB摄取减少83%（稀释度1:100；孵育24小时）和25%（稀释度1:500；孵育24小时）。在与正常血清或AIRA孵育的肝细胞上，胰岛素对AIB摄取的刺激与胰岛素与高亲和力受体的结合呈正相关（r = 0.96；P < 0.01）。我们得出结论：1）胰岛素对肝细胞摄取氨基酸的刺激是通过胰岛素受体介导的，尤其是高亲和力结合位点，并且被AIRA抑制，同时受体被阻断；2）AIRA对肝细胞基础氨基酸摄取没有胰岛素样作用。
