Genetically engineered binding proteins as biosensors for fermentation and cell culture

2003 ◽  
Vol 84 (6) ◽  
pp. 723-731 ◽  
Author(s):  
Xudong Ge ◽  
Leah Tolosa ◽  
Jen Simpson ◽  
Govind Rao
Keyword(s):  
Cell Culture ◽  
Binding Proteins ◽  
Genetically Engineered

Fluorescently labeled collagen binding proteins allow specific visualization of collagen in tissues and live cell culture

2006 ◽  
Vol 350 (2) ◽  
pp. 177-185 ◽  
Author(s):  
Katy Nash Krahn ◽  
Carlijn V.C. Bouten ◽  
Sjoerd van Tuijl ◽  
Marc A.M.J. van Zandvoort ◽  
Maarten Merkx
Keyword(s):  
Cell Culture ◽  
Binding Proteins ◽  
Live Cell ◽  
Collagen Binding

scholarly journals Concerted cell and in vivo screen for pancreatic ductal adenocarcinoma (PDA) chemotherapeutics

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Somayeh Layeghi-Ghalehsoukhteh ◽  
Shreoshi Pal Choudhuri ◽  
Ozhan Ocal ◽  
Yalda Zolghadri ◽  
Victor Pashkov ◽  
...  
Keyword(s):  
Cell Culture ◽  
Suppressor Gene ◽  
Genetically Engineered ◽  
Ductal Adenocarcinoma ◽  
Rgs Proteins ◽  
Contributing Factors ◽  
Gfp Expression ◽  
Kras Mutations ◽  
In Vivo Screen

AbstractPDA is a major cause of US cancer-related deaths. Oncogenic Kras presents in 90% of human PDAs. Kras mutations occur early in pre-neoplastic lesions but are insufficient to cause PDA. Other contributing factors early in disease progression include chronic pancreatitis, alterations in epigenetic regulators, and tumor suppressor gene mutation. GPCRs activate heterotrimeric G-proteins that stimulate intracellular calcium and oncogenic Kras signaling, thereby promoting pancreatitis and progression to PDA. By contrast, Rgs proteins inhibit Gi/q-coupled GPCRs to negatively regulate PDA progression. Rgs16::GFP is expressed in response to caerulein-induced acinar cell dedifferentiation, early neoplasia, and throughout PDA progression. In genetically engineered mouse models of PDA, Rgs16::GFP is useful for pre-clinical rapid in vivo validation of novel chemotherapeutics targeting early lesions in patients following successful resection or at high risk for progressing to PDA. Cultured primary PDA cells express Rgs16::GFP in response to cytotoxic drugs. A histone deacetylase inhibitor, TSA, stimulated Rgs16::GFP expression in PDA primary cells, potentiated gemcitabine and JQ1 cytotoxicity in cell culture, and Gem + TSA + JQ1 inhibited tumor initiation and progression in vivo. Here we establish the use of Rgs16::GFP expression for testing drug combinations in cell culture and validation of best candidates in our rapid in vivo screen.

Insulin-like growth factors and binding proteins in the fetal rat: Alterations during maternal starvation and effects in fetal brain cell culture

1993 ◽  
Vol 18 (6) ◽  
pp. 695-703 ◽  
Author(s):  
G. E. Shambaugh ◽  
J. A. Radosevich ◽  
R. P. Glick ◽  
D. S. Gu ◽  
B. E. Metzger ◽  
...  
Keyword(s):  
Cell Culture ◽  
Growth Factors ◽  
Binding Proteins ◽  
Fetal Brain ◽  
Brain Cell ◽  
Fetal Rat ◽  
Brain Cell Culture ◽  
Insulin Like Growth Factors

Mechanical and In-Vitro Cell Compatibility Properties of Silk-Elastinlike Protein-Based Biomaterial

2010 ◽  
Author(s):  
Weibing Teng ◽  
Yiding Huang ◽  
Joseph Cappello ◽  
Xiaoyi Wu
Keyword(s):  
Mechanical Property ◽  
Cell Culture ◽  
Mechanical Strength ◽  
Genetically Engineered ◽  
Load Bearing ◽  
Cell Compatibility ◽  
Chemical Treatments ◽  
Good Biocompatibility ◽  
Physical And Chemical

A series of genetically engineered recombinant silk-elastinlike proteins (SELPs) have been produced by combining polypeptide sequences derived from native silk of superior mechanical strength and elastin that is extremely durable and resilient. They have displayed a set of outstanding properties such as good biocompatibility and controllable biodegradation rates. In the study, we characterized the mechanical property of genetically engineered, recombinant silk-elastinlike protein copolymer, SELP-47K, under physical and chemical treatments. The biocompatibility of the SELP-47K was also evaluated by cell culture. The ultimate goal of this study is to explore the potential of SELPs for applications in the engineering of load-bearing tissues such as arteries.

Insulin-like growth factor-binding proteins and bone metabolism

2008 ◽  
Vol 294 (1) ◽  
pp. E10-E14 ◽  
Author(s):  
Cheryl A. Conover
Keyword(s):  
Cell Culture ◽  
Growth Factor ◽  
Bone Metabolism ◽  
Posttranslational Modifications ◽  
Clinical Studies ◽  
Binding Proteins ◽  
Insulin Like Growth Factor ◽  
Rodent Models ◽  
Factor Binding ◽  
Independent Effects

Insulin-like growth factor-binding proteins (IGFBPs) are important regulators of bone metabolism. However, their precise roles are not fully understood, since IGFBPs can have both enhancing and inhibiting effects on IGF action, depending on context and posttranslational modifications, as well as IGF-independent effects. This review focuses on recent findings from cell culture, rodent models, and clinical studies concerning local IGFBP-2, IGFBP-4, and IGFBP-5 action in bone.

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