Cellular prion protein promotes invasion and metastasis of gastric cancer

Pan, Yanglin; Zhao, Lina; Liang, Jie; Liu, Jie; Shi, Yongquan; Liu, Na; Zhang, Guoyun; Jin, Haifeng; Gao, Juan; Xie, Hui; Wang, Jun; Liu, Zhiguo; Fan, Daiming

doi:10.1096/fj.06-6138fje

Cited by 110 publications

(136 citation statements)

References 45 publications

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“…A positive correlation between PrP C expression and tumor progression was found in a series of gastric tumor samples, 19,20 where overexpression of PrP C increased tumor cell proliferation through the PI3K/AKT/ Cyclin D1 signaling pathways. 23 Similarly in glioblastomas, STI1 binding to PrP C was shown to induce cell proliferation.…”

Section: Prpmentioning

confidence: 92%

“…18 PrP C overexpression in gastric tumor cell lines has also been associated with increased expression of Bcl-2, and decreased expression of p53 and Bax, indicating a possible increase in resistance to programmed cell death. [18][19][20] In the absence of PrP C expression, resistance to TRAIL-induced apoptosis was inhibited in breast adriamycinresistant carcinoma cells. 21 In addition, breast tumor lacking estrogen receptor and PrP C expression show a high sensitivity to adjuvant chemotherapy.…”

Section: Uiccmentioning

confidence: 99%

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Prion protein ablation increases cellular aggregation and embolization contributing to mechanisms of metastasis

Muras¹,

Hajj²,

Ribeiro

et al. 2009

Intl Journal of Cancer

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Section: Prpmentioning

confidence: 92%

Section: Uiccmentioning

confidence: 99%

Prion protein ablation increases cellular aggregation and embolization contributing to mechanisms of metastasis

Muras¹,

Hajj²,

Ribeiro

et al. 2009

Intl Journal of Cancer

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“…Prion replication occurs in lymphoid tissues after peripheral infection, a process that is at least partly dependent on lymphoid PrP C expression (4). There is a need to refine understanding of PrP C function and the mechanisms regulating PrP C expression, as PrP C levels can be correlated with prion disease susceptibility (5,6) as well as with other pathological features, such as neoplastic transformation (7). Furthermore, therapeutic strategies in prion disease may involve targeting or silencing of PrP, with the accompanying potential for inadvertent modulation of immune function.…”

mentioning

confidence: 99%

A role of cellular prion protein in programming T‐cell cytokine responses in disease

et al. 2009

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The cellular prion protein (PrPC) is widely expressed in neural and non‐neural tissues, but its function is unknown. Elucidation of the part played by PrPC in adaptive immunity has been a particular conundrum: increased expression of cell surface PrPChas been documented during T‐cell activation, yet the functional significance of this activation remains unclear, with conflicting data on the effects of Prnp gene knockout on various parameters of T‐cell immunity. We show here that Prnp mRNA is highly inducible within 8‐24 h of T‐cell activation, with surface protein levels rising from 24 h. When measured in parallel with CD69 and CD25, PrPC is a late activation antigen. Consistent with its up‐regulation being a late activation event, PrP deletion did not alter T‐cell‐antigen presenting cell conjugate formation. Most important, activated PrP0/0T cells demonstrated much reduced induction of several T helper (Th) 1, Th2, and Th17 cytokines, whereas others, such as TNF‐α and IL‐9, were unaffected. These changes were investigated in the context of an autoimmune model and a bacterial challenge model. In experimental autoimmune encephalomyelitis, PrP‐knockout mice showed enhanced disease in the face of reduced IL‐17 responses. In a streptococcal sepsis model, this constrained cytokine program was associated with poorer local control of infection, although with reduced bacteremia. The findings indicate that PrPC is a potentially important molecule influencing T‐cell activation and effector function.—Ingram, R.J., Isaacs, J.D., Kaur, G., Lowther, D.E., Reynolds, C.J., Boyton,R. J., Collinge, J., Jackson, G.S., Altmann, D.M. A role of cellular prion protein in programming T‐cell cytokine responses in disease. FASEB J. 23, 1672–1684 (2009)

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“…Çeşitli tip kanserlerde PrP C 'nin aşırı ekspresyonu hızlı hücre proliferasyonu, sınırsız replikatif potansiyel, apoptosizin inhibisyonu, doku invazyonu ve metastaz gibi bazı kanser belirleyicileri ile ilişkilidir [49]. Örneğin, aşırı PrP C ekspresyonu gastrik kanser hücre hatlarında Akt yolağının aktivasyonuna, hücrelerin adesif, invaziv ve metastatik özellik kazanmasına ve Akt aktivasyonuyla MAP-kinaz ERK1/2 fosforilasyonu üzerinden tümör invazyonu ve metastazı için önemli bir adım olan ekstrasellüler matriks yıkımından sorumlu matriksmetaloproteinaz 11'in artışına neden olur [78,83,84]. 3.…”

Section: Prp C Ve Apoptozisunclassified

Prion Proteinlerinin Biyolojisi / Biology of Prion Proteins

Balcan¹

2017

Celal Bayar Üniversitesi Fen Bilimleri Dergisi

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ÖzetAlzheimer, Parkinson, Huntington ve prion hastalıkları gibi nörodejeneratif bozukluklarda ortak özellik, yanlış katlanma gösteren spesifik proteinlerin kümelenmesi ve geniş amiloid fibril ya da plakların oluşu-mudur. Son bulgular küçük soluble oligomerlerin nöronal yetersizlikten öncelikli olarak sorumlu olduğunu göstermiştir. Glikozilfosfatidilinozitol (GPI) çapalı hücresel bir glikoprotein olan prion proteini insan ve hayvanlarda prion hastalıkları olarak bilinen transmissible spongiform ensefalopatilerin (TSE) patogenezinde önemli bir rol oynamaktadır. Prion hastalıklarında bu proteinin normal hücresel formu (PrP C ) hastalık etkeni izoforma (PrP Sc ) dönüşebilir. Prion proteinlerinin bu yapısal dönüşüm sırasında kullandığı moleküler stratejiler henüz tam olarak anlaşılamamış olmasına karşın bu proteinin nörodejeneratif hastalıkların etyolojisinde ve patolojisinde merkezi bir rol oynadığı ve prion proteinlerini kodlayan genlerin (Prnp) mutasyonları ve polimorfizmlerinin hastalığa duyarlık açısından önemli etkilerinin olduğu bilinmektedir. Öte yandan, çok sayıdaki çalışmaya karşın prion proteininin patolojik ve fizyolojik koşullardaki rolleri tam olarak belirlenememiştir. Bu derlemede, prion proteinlerinin yapısal özellikleri, hücre içi trafiği, olası fizyolojik rolleri ve apoptozis ile ilişkisi özetlenmiştir. Anahtar Kelimeler-Apoptozis, Prion proteini, Protein yanlış katlanması, Sinyal transdüksiyonu. Biology of PrionProteins AbstractThe common trait of neurodegenerative disorders such as Alzheimer's, Parkinson's, Huntington's, and prion diseases is accumulation of specific misfolded proteins and forming of large amyloid fibrils or plaques. Recent findings indicate that small soluble oligomers are primary causes of the neuronal dysfunction. Prion protein, a glycosylphosphatidylinositol (GPI)-anchored cellular glycoprotein, have a fundamental role in human and animal prion diseases known as transmissible spongiform encephalopathies (TSEs). In prion diseases, cellular form (PrP C ) of protein may convert into pathogen isoform (PrP Sc ). In the course of this conversion, molecular strategies used by prion proteins remain unclear however, it is known that cellular and pathological isoforms play a key role in etiology and patholology of the neurodegenerative diseases and that mutations and polymorphisms of prion protein coding genes (Prnp) have an important effect on the susceptibility to disease. On the other hand, despite many efforts, the roles of prion protein in pathological and physiological conditions remain be elusive. This review summarizes the structural features, intracellular traffic, and possible physiological roles of PrP C and its relevance with apoptosis.

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Cellular prion protein promotes invasion and metastasis of gastric cancer

Cited by 110 publications

References 45 publications

Prion protein ablation increases cellular aggregation and embolization contributing to mechanisms of metastasis

Prion protein ablation increases cellular aggregation and embolization contributing to mechanisms of metastasis

A role of cellular prion protein in programming T‐cell cytokine responses in disease

Prion Proteinlerinin Biyolojisi / Biology of Prion Proteins

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