Efficient transfection of neuroendocrine cell lines by scrape loading

1993 ◽  
Vol 15 (4) ◽  
pp. 181-184
Author(s):  
Birgitte S. Wulff ◽  
Teit E. Johansen ◽  
Thue W. Schwartz
Keyword(s):  
Cell Lines ◽  
Neuroendocrine Cell ◽  
Scrape Loading

Tumor necrosis factor induces neuroendocrine differentiation in small cell lung cancer cell lines

1998 ◽  
Vol 275 (2) ◽  
pp. L311-L321 ◽  
Author(s):  
Kathleen J. Haley ◽  
Kirit Patidar ◽  
Fan Zhang ◽  
Rodica L. Emanuel ◽  
Mary E. Sunday
Keyword(s):  
Cell Differentiation ◽  
Cell Lines ◽  
Nuclear Factor Κb ◽  
Neuroendocrine Cell ◽  
Acid Decarboxylase ◽  
Nuclear Factor ◽  
Small Cell Lung ◽  
Amino Acid Decarboxylase ◽  
Tnf Α ◽  
Necrosis Factor

We studied tumor necrosis factor (TNF)-α as a candidate cytokine to promote neuroendocrine cell differentiation in a nitrosamine-hyperoxia hamster lung injury model. Differential screening identified expression of the genes modulated by TNF-α preceding neuroendocrine cell differentiation. Undifferentiated small cell lung carcinoma (SCLC) cell lines NCI-H82 and NCI-H526 were treated with TNF-α for up to 2 wk. Both cell lines demonstrated rapid induction of gastrin-releasing peptide (GRP) mRNA; H82 cells also expressed aromatic-l-amino acid decarboxylase mRNA within 5 min after TNF-α was added. Nuclear translocation of nuclear factor-κB immunostaining occurred with TNF-α treatment, suggesting nuclear factor-κB involvement in the induction of GRP and/or aromatic-l-amino acid decarboxylase gene expression. We also demonstrated dense core neurosecretory granules and immunostaining for proGRP and neural cell adhesion molecule in H82 cells after 7–14 days of TNF-α treatment. We conclude that TNF-α can induce phenotypic features of neuroendocrine cell differentiation in SCLC cell lines. Similar effects of TNF-α in vivo may contribute to the neuroendocrine cell differentiation/hyperplasia associated with many chronic inflammatory pulmonary diseases.

Establishment and Characterization of Two New Rectal Neuroendocrine Cell Carcinoma Cell Lines

Digestion ◽  
2000 ◽  
Vol 62 (4) ◽  
pp. 262-270 ◽  
Author(s):  
Yoshiyuki Takahashi ◽  
Masahiko Onda ◽  
Noritake Tanaka ◽  
Tomoko Seya
Keyword(s):  
Cell Carcinoma ◽  
Cell Lines ◽  
Carcinoma Cell ◽  
Neuroendocrine Cell ◽  
Carcinoma Cell Lines

Inhibition of proliferation of small intestinal and bronchopulmonary neuroendocrine cell lines by using peptide analogs targeting receptors

Cancer ◽  
2008 ◽  
Vol 112 (6) ◽  
pp. 1404-1414 ◽  
Author(s):  
Mark Kidd ◽  
Andrew V. Schally ◽  
Roswitha Pfragner ◽  
Maximillian V. Malfertheiner ◽  
Irvin M. Modlin
Keyword(s):  
Cell Lines ◽  
Neuroendocrine Cell ◽  
Inhibition Of Proliferation ◽  
Peptide Analogs ◽  
Small Intestinal

scholarly journals mTOR inhibitors activate PERK signaling and favor viability of gastrointestinal neuroendocrine cell lines

Oncotarget ◽  
2017 ◽  
Vol 8 (13) ◽  
pp. 20974-20987 ◽  
Author(s):  
Patricia Freis ◽  
Julien Bollard ◽  
Justine Lebeau ◽  
Patrick Massoma ◽  
Joëlle Fauvre ◽  
...  
Keyword(s):  
Cell Lines ◽  
Mtor Inhibitors ◽  
Neuroendocrine Cell

Immortalized Neuronal and Neuroendocrine Cell Lines by Targeted Oncogenesis in Transgenic Mice Using the PNMT Promoter

1993 ◽  
Vol 3 (3) ◽  
pp. 176-183
Author(s):  
Joseph P. Hammang ◽  
E.Edward Baetge ◽  
Albee Messing
Keyword(s):  
Transgenic Mice ◽  
Cell Lines ◽  
Neuroendocrine Cell

scholarly journals Secretion of bioactive human insulin following plasmid-mediated gene transfer to non-neuroendocrine cell lines, primary cultures and rat skeletal muscle in vivo

2002 ◽  
Vol 172 (3) ◽  
pp. 653-672 ◽  
Author(s):  
JA Shaw ◽  
MI Delday ◽  
AW Hart ◽  
HM Docherty ◽  
CA Maltin ◽  
...  
Keyword(s):  
Gene Transfer ◽  
Cell Lines ◽  
Human Insulin ◽  
Primary Cultures ◽  
Neuroendocrine Cell ◽  
Wild Type ◽  
Plasmid Injection ◽  
Mutant Construct

The objective of these studies was to evaluate human insulin gene expression following intramuscular plasmid injection in non-diabetic rats as a potential approach to gene therapy for diabetes mellitus avoiding the need for immunosuppression. A wild-type human preproinsulin construct and a mutant construct in which PC2/PC3 sites were engineered to form furin consensus sites were evaluated in in vitro transfections of hepatocyte (HepG2) and myoblast (C2C12/L6) cell lines, primary rat myoblasts, and dermal fibroblasts. In vivo gene transfer by percutaneous plasmid injection of soleus muscle +/- prior notexin-induced myolysis was assessed in rats. In vitro transfection of non-neuroendocrine cell lines and primary cultures with wild-type human preproinsulin resulted in secretion of predominantly unprocessed proinsulin. Employing the mutant construct, there was significant processing to mature insulin (HepG2, 95%; C2C12, 75%; L6, 65%; primary myoblasts, 48%; neonatal fibroblasts, 56%; adult fibroblasts, 87%). In rats aged 5 weeks, circulating human (pro)insulin was detected from 1 to 37 days following plasmid injection and the potential of augmenting transfection efficiency by prior notexin injection was demonstrated (wild-type processing, 87%; mutant, 90%). Relative hypoglycaemia was confirmed by HbA1C (saline, 5.5%; wild type, 5.1%; mutant, 5.1% (P<0.05)). Human (pro)insulin levels and processing (wild-type, 8%; mutant, 53%) were lower in rats aged 9 months but relative hypoglycaemia was confirmed by serum glucose at 10 days (saline, 6.4 mmol/l; wild-type, 6.0 mmol/l; mutant, 5.4 mmol/l). In conclusion, prolonged constitutive systemic secretion of bioactive human (pro)insulin has been attained in non-neuroendocrine cells in vitro and in growing and mature rats following intramuscular plasmid injection.

Processing of proSAAS in neuroendocrine cell lines

2001 ◽  
Vol 361 (1) ◽  
pp. 67-76 ◽  
Author(s):  
Nino MZHAVIA ◽  
Yimei QIAN ◽  
Yun FENG ◽  
Fa-Yun CHE ◽  
Lakshmi A. DEVI ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cell Lines ◽  
Phorbol Ester ◽  
Term Treatment ◽  
Neuroendocrine Cell ◽  
Prohormone Convertase ◽  
Wild Type ◽  
Long Term Treatment ◽  
Mouse Pituitary

ProSAAS, a recently discovered granin-like protein, potently inhibits prohormone convertase (PC)1, and might also perform additional functions. In the present study, the processing of proSAAS was compared in two neuroendocrine cell lines overexpressing this protein: the AtT-20 mouse pituitary corticotrophic line and the PC12 rat adrenal phaeochromocytoma line. The processing of proSAAS was examined by pulse–chase analysis using [3H]leucine, by MS, and by chromatography and radioimmunoassay. Various smaller forms of proSAAS were detected, including peptides designated as little SAAS, PEN and big LEN. Because the PC-12 cells used in the present study do not express either PC1 or PC2, the finding that these cells efficiently cleave proSAAS indicates that these cleavages do not require either enzyme. Two of the peptides identified in AtT-20 media represent novel C-terminally truncated forms of PEN. In both cell lines, the secretion of the small proSAAS-derived peptides is stimulated by secretagogues. However, long-term treatment of wild-type AtT-20 cells with two different secretagogues (8-bromo-cAMP and a phorbol ester) does not affect levels of proSAAS mRNA; this treatment significantly increases PC1 mRNA by approx. 60–80%. The lack of co-regulation of proSAAS and PC1 mRNA implies that enzyme activity can be induced without an accompanying increase in the inhibitor. In addition, the finding that the peptides are secreted via the regulated pathway is consistent with the proposal that they may function as neuropeptides.

Sign in / Sign up

Export Citation Format

Share Document