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脑钠肽存在于人类羊水当中,由羊膜细胞分泌。

Brain natriuretic peptide is present in the human amniotic fluid and is secreted from amnion cells.

作者信息

Itoh H, Sagawa N, Hasegawa M, Okagaki A, Inamori K, Ihara Y, Mori T, Ogawa Y, Suga S, Mukoyama M

机构信息

Department of Gynecology and Obstetrics, Kyoto University Faculty of Medicine, Japan.

出版信息

J Clin Endocrinol Metab. 1993 Apr;76(4):907-11. doi: 10.1210/jcem.76.4.8473404.

Abstract

The presence and biochemical characteristics of human brain natriuretic peptide (hBNP) in the amniotic fluid at various gestational ages were investigated. The hBNP-like immunoreactivity (hBNP-LI) levels in amniotic fluid, determined by RIA, were 118.7 +/- 57.6 pmol/L (mean +/- SEM; n = 5) and 107.7 +/- 8.7 pmol/L (n = 9) in the first and second trimesters of pregnancy, respectively; it was significantly decreased to 28.4 +/- 5.1 pmol/L (n = 9) in the third trimester. However, human atrial natriuretic peptide-like immunoreactivity (hANP-LI) was not detected (< 0.3 pmol/L) in any of these samples. Northern blot analysis demonstrated hBNP mRNA in human amnion tissue. Moreover, cultured amnion cells secreted a significant amount of hBNP-LI (100-200 fmol/10(6) cells/day), but not hANP-LI, into the culture medium. The synthesis of hBNP in cultured amnion cells was further confirmed using the polymerase chain reaction. High performance gel permeation chromatography of hBNP-LI extracted from human amniotic fluid and the culture medium of amnion cells revealed that the predominant molecular form of hBNP-LI in both samples was the hBNP precursor, with an approximate mol wt of 12 kilodaltons. These findings indicate that hBNP is present in the human amniotic fluid, and that amnion cells synthesize hBNP and secrete it into the amniotic cavity.

摘要

研究了不同孕周羊水中人脑钠肽(hBNP)的存在情况及其生化特性。采用放射免疫分析法(RIA)测定,妊娠早、中期羊水hBNP样免疫活性(hBNP-LI)水平分别为118.7±57.6 pmol/L(均值±标准误;n = 5)和107.7±8.7 pmol/L(n = 9);妊娠晚期显著降至28.4±5.1 pmol/L(n = 9)。然而,在所有这些样本中均未检测到人心房钠肽样免疫活性(hANP-LI)(< 0.3 pmol/L)。Northern印迹分析显示人羊膜组织中有hBNP mRNA。此外,培养的羊膜细胞向培养基中分泌大量hBNP-LI(100 - 200 fmol/10⁶细胞/天),但不分泌hANP-LI。采用聚合酶链反应进一步证实了培养的羊膜细胞中hBNP的合成。对从人羊水和羊膜细胞培养基中提取的hBNP-LI进行高效凝胶渗透色谱分析,结果显示两个样本中hBNP-LI的主要分子形式均为hBNP前体,分子量约为12千道尔顿。这些发现表明hBNP存在于人羊水中,且羊膜细胞合成hBNP并将其分泌到羊膜腔内。

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