Pancreas-specific protein disulfide isomerase has a cell type-specific expression in various mouse tissues and is absent in human pancreatic adenocarcinoma cells: implications for its functions

Fu, Xinmiao; Dai, Xiangchen; Ding, Jian; Zhu, Bao Ting

doi:10.1007/s10735-009-9230-5

Cited by 16 publications

(24 citation statements)

References 37 publications

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“…Following this observation, we also showed that the accumulation of E 2 in the pancreas is largely attributable to PDIp [pancreas-specific PDI (protein disulfide isomerase)], which has a high capacity for binding E 2 in vitro and in vivo and can also slow down E 2 metabolism in vitro. PDIp was previously reported to be a protein-folding catalyst [25][26][27], predominantly localized in the endoplasmic reticulum [28] and selectively expressed at high levels in pancreatic acinar cells [25,[28][29][30][31]. The results of the present study indicate that besides serving as a proteinfolding catalyst, PDIp may also have other biological functions through modulating pancreatic tissue levels and the metabolism of endogenous oestrogens.…”

Section: Introductionsupporting

confidence: 62%

“…Secondly, although PDI is abundantly expressed in many tissues [28,34], PDIp is highly and selectively expressed in the pancreas, at an estimated concentration of up to 0.5 % of the total cellular proteins [25,28]. Thirdly, the molecular sizes of PDI and PDIp appear to be comparable with the sizes seen at the SEC elution volumes for fractions A7 and A8 (Figure 2A and Supplementary Figure S2).…”

Section: Identification Of Pdip As the Most Abundant E 2 -Binding Promentioning

confidence: 86%

“…Our previous study showed that human pancreatic cancer cells (e.g. BxPC-3, Mia Paca-2 and Capan-2) do not express endogenous PDIp [28], but they express oestrogen receptors [38]. Hence we chose to use the approach of selectively overexpressing PDIp in BxPC-3 cells, coupled with concomitant transfection of an ERE-driven luciferase reporter gene.…”

Section: Modulation Of Pdip On E 2 In Vitromentioning

confidence: 99%

“…The ERE (oestrogen response element)-driven luciferase vector (pGL3-Basic + ERE + E1b + luciferase) was a gift from Dr Carolyn Smith (Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX, U.S.A.). pcDNA3.1-PDIp was constructed as described previously [28]. The monkey kidney COS-7 cell line was purchased from the A.T.C.C.…”

Section: Introductionmentioning

confidence: 99%

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

Wang

Fukui

et al. 2012

Biochemical Journal

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E(2) (17β-oestradiol), a female sex hormone, has important biological functions in a woman's body. The pancreas, often considered a non-classical E(2)-targeting organ, is known to be functionally regulated by E(2), 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 E(2) storage protein in a rat model to modulate the pancreatic tissue level, metabolism and action of E(2). The purified endogenous PDIp from both rat and human pancreatic tissues can bind E(2) with a K(d) value of approximately 150 nM. The endogenous PDIp-bound E(2) accounts for over 80% of the total protein-bound E(2) present in rat and human pancreatic tissues, and this binding protects E(2) from metabolic disposition and prolongs its duration of action. Importantly, we showed in ovariectomized female rats that the E(2) level in the pancreas reaches its highest level (9-fold increase over its basal level) at 24-48 h after a single injection of E(2), and even at 96 h its level is still approximately 5-fold higher. In contrast, the E(2) level 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.

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Section: Introductionsupporting

confidence: 62%

Section: Identification Of Pdip As the Most Abundant E 2 -Binding Promentioning

confidence: 86%

Section: Modulation Of Pdip On E 2 In Vitromentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Wang

Fukui

et al. 2012

Biochemical Journal

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“…Pdip expression level was highest in the corpus and appeared to be localized to gastric chief cells (16).…”

Section: Digestion and Absorptionmentioning

confidence: 97%

Selective gene expression by rat gastric corpus epithelium

Goebel

Stengel

Lambrecht

et al. 2011

Physiological Genomics

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The gastrointestinal (GI) tract is divided into several segments that have distinct functional properties, largely absorptive. The gastric corpus is the only segment thought of as largely secretory. Microarray hybridization of the gastric corpus mucosal epithelial cells was used to compare gene expression with other segments of the columnar GI tract followed by statistical data subtraction to identify genes selectively expressed by the rat gastric corpus mucosa. This provides a means of identifying less obvious specific functions of the corpus in addition to its secretionrelated genes. For example, important properties found by this GI tract comparative transcriptome reflect the energy demand of acid secretion, a role in lipid metabolism, the large variety of resident neuroendocrine cells, responses to damaging agents and transcription factors defining differentiation of its epithelium. In terms of overlap of gastric corpus genes with the rest of the GI tract, the distal small bowel appears to express many of the gastric corpus genes in contrast to proximal small and large bowel. This differential map of gene expression by the gastric corpus epithelium will allow a more detailed description of major properties of the gastric corpus and may lead to the discovery of gastric corpus cell differentiation genes and those mis-regulated in gastric carcinomas.transcriptome; stomach THE FUNCTION OF AN ORGAN DEPENDS on the genes and protein products expressed and their regulation. Much has been learnt by classical physiological or biochemical approaches, but the complexity of biology suggests that many functions may be overlooked by conventional approaches. If a complete and specific gene expression profile were available, a more realistic understanding of a specific organ's capabilities would ensue.The gastric corpus epithelium is the most complicated region of the gastrointestinal (GI) tract in terms of secretion, endocrine function, and differentiation due to its large variety of cell types. In this article, we present the specific transcriptome of the rat gastric corpus mucosa as obtained by whole rat genome microarray hybridization compared with three other mucosal segments of the columnar GI tract (proximal and distal small bowel, and colon). This is followed by statistical data subtraction to identify genes selectively expressed by the rat gastric corpus mucosa, but not by the other segments. Genes identified with this method most likely reflect functional importance in the stomach when considered in the context of relative rather than absolute expression levels. For example, many receptors are expressed at relatively low levels but their increased expression relative to other regions of the GI tract indicates significant function in the gastric secretory epithelium. The success of this method has been previously shown during transcriptomal analysis of purified suspensions of individual cell types, such as parietal and enterochromaffin-like (ECL) cells compared with the primary mucosal digest of the gastric corpus m...

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Benchmark of site- and structure-specific quantitative tissue N-glycoproteomics for discovery of potential N-glycoprotein markers: a case study of pancreatic cancer

Xiao

Tian

2021

Glycoconj J

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Pancreas-specific protein disulfide isomerase has a cell type-specific expression in various mouse tissues and is absent in human pancreatic adenocarcinoma cells: implications for its functions

Cited by 16 publications

References 37 publications

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

Selective gene expression by rat gastric corpus epithelium

Benchmark of site- and structure-specific quantitative tissue N-glycoproteomics for discovery of potential N-glycoprotein markers: a case study of pancreatic cancer

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