Paracrine effects of a uterine agglutinin are mediated via the sialic acids present in the rat uterine endometrium
Paracrine effects of a uterine agglutinin are mediated via the sialic acids present in the rat uterine endometrium
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DOI：
10.1023/a:1026582715752
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发表时间：
2000-12-01
影响因子：
4.3
通讯作者：
Chowdhury, M
中科院分区：
文献类型：
--
作者：
Chatterji, U;Sen, AK;Chowdhury, M
从大鼠发情前期子宫内膜中分离出一种32 kDa的雌激素诱导的唾液酸特异性凝集素（P-SAS）。为了研究P-SAS在子宫环境中的功能重要性，我们将i -125标记的P-SAS与从发情周期的不同阶段分离出来的子宫不同细胞成分（上皮细胞、基质细胞和子宫肌层细胞）进行了特异性结合试验。结果表明，虽然该蛋白在雌激素期由上皮细胞分泌，但它特异性地与基质细胞结合，特别是与那些从发情周期的发情期分离出来的基质细胞结合。然而，这种特异性结合随着妊娠的进展而减少。在过量冷P-SAS存在的情况下，用不同量的I-125-P-SAS进行的Scatchard分析显示，结合发生在Ka = 1.69 x 10(8) M-1。由于P-SAS特异性结合基质细胞表面的唾液酸，因此采用气相液相色谱（GLC）对P-SAS结合的唾液酸分子进行了进一步表征。研究表明，P-SAS优先与n -糖基神经氨酸结合，n -糖基神经氨酸通过α 2,6键连接到基质细胞表面糖蛋白链的第2位糖。由于P-SAS进一步被认为是有丝分裂[2]，我们在体外研究了P-SAS对培养基质细胞的影响。生长调节实验表明，P-SAS诱导培养基质细胞摄取h -3-胸腺嘧啶。因此，根据上述观察，可以假设P-SAS对基质细胞和随后的子宫生长发育有旁分泌作用。
A 32 kDa estrogen-induced, sialic acid-specific agglutinin (P-SAS) was isolated from rat endometrium in its proestrus stage [1]. To investigate the functional importance of P-SAS in the uterine milieu, specific binding assays were carried out with I-125-labeled P-SAS and different cellular components of the uterus (epithelial, stromal and myometrial cells), that were isolated from different stages of the estrus cycle. The results indicate that although the protein is secreted from the epithelial cells in the estrogenic phase, it binds specifically to the stromal cells, especially to those isolated from the diestrus stage of the estrus cycle. The specific binding, however, is seen to decrease with the progression of pregnancy. Scatchard analysis performed with varying amounts of I-125-P-SAS in the presence of excess cold P-SAS revealed that the binding occurs with a Ka = 1.69 x 10(8) M-1. As P-SAS binds specifically to sialic acids on the stromal cell surface, further characterization of the sialic acid molecule to which P-SAS binds was carried out by gas liquid chromatography (GLC). The studies revealed that P-SAS preferentially binds to N-glycolylneuraminic acid, which is attached to the penultimate sugar of the stromal cell surface glycoprotein chain via alpha2,6 linkage. As P-SAS is further known to be mitogenic [2], the effect of P-SAS on cultured stromal cells was studied in vitro. The growth regulatory assays revealed that P-SAS induced H-3-thymidine uptake by stromal cells in culture. Thus, from the above observations, paracrine effects of P-SAS on the stromal cells and on the subsequent growth and development of the uterus can be assumed.