PDIp is a major intracellular oestrogen-storage protein that modulates tissue levels of oestrogen in the pancreas.

PDIp is a major intracellular oestrogen-storage protein that modulates tissue levels of oestrogen in the pancreas.
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PDIp 是一种主要的细胞内雌激素储存蛋白,可调节胰腺中雌激素的组织水平。

DOI:
10.1042/bj20120868
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发表时间:
2012
期刊:
The Biochemical journal
影响因子:
--
通讯作者:
Zhu,BaoTing
Zhu,BaoTing
中科院分区:
--
文献类型:
--
作者:
Fu,Xinmiao;Wang,Pan;Fukui,Masayuki;Long,Cheng;Yin,Linxiang;Choi,HyeJoung;Zhu,BaoTing

文献摘要

相似文献

E2(17β-oestradiol), a female sex hormone, has important biological functions in a woman's body. The pancreas, often considered a non-classical E2-targeting organ, is known to be functionally regulated by E2, but little is known about how oestrogen actions are regulated in this organ. In the present study we report that PDIp (pancreas-specific protein disulfide isomerase), a protein-folding catalyst, can act as a major intracellular E2storage protein in a rat model to modulate the pancreatic tissue level, metabolism and action of E2. The purified endogenous PDIp from both rat and human pancreatic tissues can bind E2with aKdvalue of approximately 150 nM. The endogenous PDIp-bound E2accounts for over 80% of the total protein-bound E2present in rat and human pancreatic tissues, and this binding protects E2from metabolic disposition and prolongs its duration of action. Importantly, we showed in ovariectomized female rats that the E2level in the pancreas reaches its highest level (9-fold increase over its basal level) at 24–48 h after a single injection of E2, and even at 96 h its level is still approximately 5-fold higher. In contrast, the E2level in the uterus quickly returns to its basal level at 48 h after reaching its maximal level (approximately 2-fold increase) at 24 h. Taken together, these results show for the first time that PDIp is a predominant intracellular oestrogen storage protein in the pancreas, which offers novel mechanistic insights into the accumulation and action of oestrogen inside pancreatic cells.