Ovalbumin Secretory Signal Peptide-containing Collagen Gel as a Cell Scaffold

2017 ◽  
Vol 46 (3) ◽  
pp. 395-397 ◽  
Author(s):  
Chie Kojima ◽  
Yuri Narita ◽  
Tomonori Waku ◽  
Naoya Morimoto ◽  
Daiki Togawa ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Collagen Gel ◽  
Cell Scaffold ◽  
A Cell ◽  
Secretory Signal Peptide

Modulation of Cell Adhesion and Differentiation on Collagen Gels by the Addition of the Ovalbumin Secretory Signal Peptide

2019 ◽  
Vol 5 (11) ◽  
pp. 5698-5704 ◽  
Author(s):  
Chie Kojima ◽  
Yuri Narita ◽  
Yusuke Nakajima ◽  
Naoya Morimoto ◽  
Takashi Yoshikawa ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Signal Peptide ◽  
Collagen Gels ◽  
Secretory Signal Peptide

scholarly journals Cell-free synthesis of the hirudin variant 1 of the blood-sucking leech Hirudo medicinalis

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Doreen A. Wüstenhagen ◽  
Phil Lukas ◽  
Christian Müller ◽  
Simone A. Aubele ◽  
Jan-Peter Hildebrandt ◽  
...  
Keyword(s):  
Signal Peptide ◽  
Peptide Sequence ◽  
Bacterial Cells ◽  
Recombinant Hirudin ◽  
Signal Peptide Sequence ◽  
Cell Lysates ◽  
Blood Sucking ◽  
A Cell ◽  
Synthesis Approach ◽  
Cell Free Protein Synthesis

AbstractSynthesis and purification of peptide drugs for medical applications is a challenging task. The leech-derived factor hirudin is in clinical use as an alternative to heparin in anticoagulatory therapies. So far, recombinant hirudin is mainly produced in bacterial or yeast expression systems. We describe the successful development and application of an alternative protocol for the synthesis of active hirudin based on a cell-free protein synthesis approach. Three different cell lysates were compared, and the effects of two different signal peptide sequences on the synthesis of mature hirudin were determined. The combination of K562 cell lysates and the endogenous wild-type signal peptide sequence was most effective. Cell-free synthesized hirudin showed a considerably higher anti-thrombin activity compared to recombinant hirudin produced in bacterial cells.

Transfer-Print of CNTs and its Application to Cell Scaffold

2017 ◽  
Vol 11 (6) ◽  
pp. 941-946 ◽  
Author(s):  
Arata Kaneko ◽  
◽  
Yuuki Miyazaki ◽  
Tatsuya Goto
Keyword(s):  
Cultured Cells ◽  
Hydrophobic Interactions ◽  
Casting Process ◽  
Water Contact ◽  
Si Substrates ◽  
Dimethyl Siloxane ◽  
Cell Scaffold ◽  
Assembled Monolayers ◽  
A Cell ◽  
Surface Modified

A bio-chip using cultured cells is developed for an application to drug screening. Carbon nanotubes (CNTs) are a candidate for this electrode material. A transfer-prints is expected to be a CNT-patterning technique applicable to soft material. This present paper is intended to show some basic properties about the transfer-print of CNTs, and also to demonstrate the possibility of the CNTs as a cell scaffold. The present study prepared several types of surface-modified Si substrate with different wettability to investigate the effects of wettability on the transferring ratio of CNTs. Some Si substrates are terminated by OH or H groups, while other substrates are coated with hydrophobic or hydrophilic self-assembled monolayers. The stamps for transfer-print, which have circular dots (50-μm diameter) or a straight ridge (50-μm width) array, are fabricated using poly-dimethyl-siloxane (PDMS). The surfaces of PDMS stamps are inked by single-walled CNTs by a pre-transferring or casting process. The transfer-prints to surface-modified Si surfaces allow the CNTs to be formed in lines of several tens of micrometers, while the coverage of transfer-printed CNTs is also dominated by surface wettability. The coverage of transfer-printed CNTs increases with the water contact angle of the Si surface. It is reasonable that the transfer-print of CNTs is performed by hydrophobic interactions. Meanwhile, two kinds of polymer (polystyrene (PS) and polyethylene terephthalate (PET)) sheets are also utilized as a substrate. The transfer-prints with heating around the softening point of the polymer allow CNTs to be accurately patterned into an array of 50-μm dots. The coverage of CNTs is 94% on the PET substrate. The PS sheet with patterned CNTs is applied to a cell scaffold. PC12 cells are cultured on the PS sheets so that the cells are selectively adhered to the transfer-printed CNTs. The adhered cells are extended with some pseudopods. It is demonstrated that the transfer-printed CNTs are expected to be electrodes of the cell scaffold.

scholarly journals Nanofibrillar cellulose wound dressing supports the growth and characteristics of human mesenchymal stem/stromal cells without cell adhesion coatings

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Jasmi Kiiskinen ◽  
Arto Merivaara ◽  
Tiina Hakkarainen ◽  
Minna Kääriäinen ◽  
Susanna Miettinen ◽  
...  
Keyword(s):  
Wound Healing ◽  
Cell Adhesion ◽  
Cell Viability ◽  
Cell Survival ◽  
Cell Transplantation ◽  
Stromal Cells ◽  
Wound Dressing ◽  
Nanofibrillar Cellulose ◽  
Cell Scaffold ◽  
A Cell

Abstract Background In the field of regenerative medicine, delivery of human adipose-derived mesenchymal stem/stromal cells (hASCs) has shown great promise to promote wound healing. However, a hostile environment of the injured tissue has shown considerably to limit the survival rate of the transplanted cells, and thus, to improve the cell survival and retention towards successful cell transplantation, an optimal cell scaffold is required. The objective of this study was to evaluate the potential use of wood-derived nanofibrillar cellulose (NFC) wound dressing as a cell scaffold material for hASCs in order to develop a cell transplantation method free from animal-derived components for wound treatment. Methods Patient-derived hASCs were cultured on NFC wound dressing without cell adhesion coatings. Cell characteristics, including cell viability, morphology, cytoskeletal structure, proliferation potency, and mesenchymal cell and differentiation marker expression, were analyzed using cell viability assays, electron microscopy, immunocytochemistry, and quantitative or reverse transcriptase PCR. Student’s t test and one-way ANOVA followed by a Tukey honestly significant difference post hoc test were used to determine statistical significance. Results hASCs were able to adhere to NFC dressing and maintained high cell survival without cell adhesion coatings with a cell density-dependent manner for the studied period of 2 weeks. In addition, NFC dressing did not induce any remarkable cytotoxicity towards hASCs or alter the morphology, proliferation potency, filamentous actin structure, the expression of mesenchymal vimentin and extracellular matrix (ECM) proteins collagen I and fibronectin, or the undifferentiated state of hASCs. Conclusions As a result, NFC wound dressing offers a functional cell culture platform for hASCs to be used further for in vivo wound healing studies in the future.

Biological Evaluation of Chitosan Salts Cross-Linked to Genipin as a Cell Scaffold for Disk Tissue Engineering

2005 ◽  
Vol 11 (1-2) ◽  
pp. 130-140 ◽  
Author(s):  
Fackson Mwale ◽  
Mihaela Iordanova ◽  
Caroline N. Demers ◽  
Thomas Steffen ◽  
Peter Roughley ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Biological Evaluation ◽  
Cell Scaffold ◽  
A Cell

A plant secretory signal peptide targets plastome-encoded recombinant proteins to the thylakoid membrane

2010 ◽  
Vol 76 (3-5) ◽  
pp. 427-441 ◽  
Author(s):  
Francesca De Marchis ◽  
Andrea Pompa ◽  
Roberta Mannucci ◽  
Tomas Morosinotto ◽  
Michele Bellucci
Keyword(s):  
Recombinant Proteins ◽  
Signal Peptide ◽  
Thylakoid Membrane ◽  
Secretory Signal Peptide

scholarly journals Secretion of Active-Form Streptoverticillium mobaraense Transglutaminase by Corynebacterium glutamicum: Processing of the Pro-Transglutaminase by a Cosecreted Subtilisin-Like Protease from Streptomyces albogriseolus

2003 ◽  
Vol 69 (1) ◽  
pp. 358-366 ◽  
Author(s):  
Yoshimi Kikuchi ◽  
Masayo Date ◽  
Kei-ichi Yokoyama ◽  
Yukiko Umezawa ◽  
Hiroshi Matsui
Keyword(s):  
Corynebacterium Glutamicum ◽  
Signal Peptide ◽  
Food Industry ◽  
Protein Production ◽  
Active Form ◽  
Surface Protein ◽  
Peptide Bond ◽  
Cell Surface Protein ◽  
Amino Acid Residues ◽  
A Cell

ABSTRACT The transglutaminase secreted by Streptoverticillium mobaraense is a useful enzyme in the food industry. A fragment of transglutaminase was secreted by Corynebacterium glutamicum when it was coupled on a plasmid to the promoter and signal peptide of a cell surface protein from C. glutamicum. We analyzed the signal peptide and the pro-domain of the transglutaminase gene and found that the signal peptide consists of 31 amino acid residues and the pro-domain consists of 45 residues. When the pro-domain of the transglutaminase was used, the pro-transglutaminase was secreted efficiently by C. glutamicum but had no enzymatic activity. However, when the plasmid carrying the S. mobaraense transglutaminase also encoded SAM-P45, a subtilisin-like serine protease derived from Streptomyces albogriseolus, the peptide bond to the C side of 41-Ser of the pro-transglutaminase was hydrolyzed, and the pro-transglutaminase was converted to an active form. Our findings suggest that C. glutamicum has potential as a host for industrial-scale protein production.

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