Antiangiogenic Activity of Restin, NC10 Domain of Human Collagen XV: Comparison to Endostatin

1999 ◽  
Vol 255 (3) ◽  
pp. 735-739 ◽  
Author(s):  
Ramani Ramchandran ◽  
Mohanraj Dhanabal ◽  
Ruediger Volk ◽  
Matthew J.F. Waterman ◽  
Mark Segal ◽  
...  
Keyword(s):  
Antiangiogenic Activity ◽  
Human Collagen ◽  
Collagen Xv

scholarly journals Crystal structure of the human collagen XV trimerization domain: A potent trimerizing unit common to multiplexin collagens

2011 ◽  
Vol 30 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Jacqueline A. Wirz ◽  
Sergei P. Boudko ◽  
Thomas F. Lerch ◽  
Michael S. Chapman ◽  
Hans Peter Bächinger
Keyword(s):  
Crystal Structure ◽  
Human Collagen ◽  
Collagen Xv

scholarly journals Human collagen XV is a prominent histopathological component of sinusoidal capillarization in hepatocellular carcinogenesis

2015 ◽  
Vol 21 (2) ◽  
pp. 302-309 ◽  
Author(s):  
Kouji Kimura ◽  
Masaru Nakayama ◽  
Ichiro Naito ◽  
Takaaki Komiyama ◽  
Kouichi Ichimura ◽  
...  
Keyword(s):  
Hepatocellular Carcinogenesis ◽  
Human Collagen ◽  
Collagen Xv

scholarly journals Improved stability of multivalent antibodies containing the human collagen XV trimerization domain

mAbs ◽  
2012 ◽  
Vol 4 (2) ◽  
pp. 226-232 ◽  
Author(s):  
Ángel M. Cuesta ◽  
David Sánchez-Martín ◽  
Ana Blanco-Toribio ◽  
Maider Villate ◽  
Kelly Enciso-Álvarez ◽  
...  
Keyword(s):  
Improved Stability ◽  
Human Collagen ◽  
Collagen Xv

scholarly journals Recombinant Human Collagen XV Regulates Cell Adhesion and Migration

2009 ◽  
Vol 285 (8) ◽  
pp. 5258-5265 ◽  
Author(s):  
Merja Hurskainen ◽  
Florence Ruggiero ◽  
Pasi Hägg ◽  
Taina Pihlajaniemi ◽  
Pirkko Huhtala
Keyword(s):  
Cell Adhesion ◽  
Cell Adhesion And Migration ◽  
Human Collagen ◽  
And Migration ◽  
Collagen Xv

Collagen XV as a bone matrix organizer

2013 ◽  
Author(s):  
David Vicente ◽  
Mikko Finnila ◽  
Valerio Izzi ◽  
Jarkko Koivunen ◽  
Taina Pihlajaniemi
Keyword(s):  
Bone Matrix ◽  
Collagen Xv

Engineering and Characterization of the Chimeric Antibody that Targets the C-terminal Telopeptide of the α2 Chain of Human Collagen I: A Next Step in the Quest to Reduce Localized Fibrosis

2013 ◽  
pp. 130222063815006
Author(s):  
Jolanta Fertala ◽  
Andrzej Steplewski ◽  
James Kostas ◽  
Pedro Beredjiklian ◽  
Gerard Williams ◽  
...  
Keyword(s):  
Collagen I ◽  
Chimeric Antibody ◽  
Human Collagen

Time Series Analysis of Transmesothelial Invasion by Endometrial Stromal and Epithelial Cells Using Three-dimensional Confocal Microscopy

2001 ◽  
Vol 7 (S2) ◽  
pp. 580-581
Author(s):  
CA Witz ◽  
S Cho ◽  
VE Centonze ◽  
IA Montoya-Rodriguez ◽  
RS Schenken
Keyword(s):  
Epithelial Cells ◽  
Stromal Cells ◽  
Time Course ◽  
Three Dimensional ◽  
Collagen Iv ◽  
Mesothelial Cells ◽  
Endometrial Stromal Cells ◽  
Human Collagen ◽  
Endometrial Epithelial Cells

Using human peritoneal explants, we have previously demonstrated that endometrial stromal cells (ESCs) and endometrial epithelial cells (EECs) attach to intact mesothelium. Attachment occurs within one hour and mesothelial invasion occurs within 18 hours (Figure 1). We have also demonstrated that, in vivo, the mesothelium overlies a continuous layer of collagen IV (Col IV).More recently we have used CLSM, to study the mechanism and time course of ESC and EEC attachment and invasion through mesothelial monolayers. in these studies, CellTracker® dyes were used to label cells. Mesothelial cells were labeled with chloromethylbenzoylaminotetramethylrhodamine (CellTracker Orange). Mesothelial cells were then plated on human collagen IV coated, laser etched coverslips. Mesothelial cells were cultured to subconfluence. ESCs and EECs, labeled with chloromethylfluorscein diacetate (CellTracker Green) were plated on the mesothelial monolayers. Cultures were examined at 1, 6, 12 and 24 hours with simultaneous differential interference contrast and CLSM.

scholarly journals Plant Recombinant Human Collagen Type I Hydrogels for Corneal Regeneration

2021 ◽  
Author(s):  
Michel Haagdorens ◽  
Elle Edin ◽  
Per Fagerholm ◽  
Marc Groleau ◽  
Zvi Shtein ◽  
...  
Keyword(s):  
Collagen Type ◽  
Collagen Type I ◽  
Collagen Fibrils ◽  
Type I ◽  
Safe Alternative ◽  
Human Donor ◽  
Human Collagen ◽  
Donor Corneas

Abstract Purpose To determine feasibility of plant-derived recombinant human collagen type I (RHCI) for use in corneal regenerative implants Methods RHCI was crosslinked with 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide (EDC) and N-hydroxysuccinimide (NHS) to form hydrogels. Application of shear force to liquid crystalline RHCI aligned the collagen fibrils. Both aligned and random hydrogels were evaluated for mechanical and optical properties, as well as in vitro biocompatibility. Further evaluation was performed in vivo by subcutaneous implantation in rats and corneal implantation in Göttingen minipigs. Results Spontaneous crosslinking of randomly aligned RHCI (rRHCI) formed robust, transparent hydrogels that were sufficient for implantation. Aligning the RHCI (aRHCI) resulted in thicker collagen fibrils forming an opaque hydrogel with insufficient transverse mechanical strength for surgical manipulation. rRHCI showed minimal inflammation when implanted subcutaneously in rats. The corneal implants in minipigs showed that rRHCI hydrogels promoted regeneration of corneal epithelium, stroma, and nerves; some myofibroblasts were seen in the regenerated neo-corneas. Conclusion Plant-derived RHCI was used to fabricate a hydrogel that is transparent, mechanically stable, and biocompatible when grafted as corneal implants in minipigs. Plant-derived collagen is determined to be a safe alternative to allografts, animal collagens, or yeast-derived recombinant human collagen for tissue engineering applications. The main advantage is that unlike donor corneas or yeast-produced collagen, the RHCI supply is potentially unlimited due to the high yields of this production method. Lay Summary A severe shortage of human-donor corneas for transplantation has led scientists to develop synthetic alternatives. Here, recombinant human collagen type I made of tobacco plants through genetic engineering was tested for use in making corneal implants. We made strong, transparent hydrogels that were tested by implanting subcutaneously in rats and in the corneas of minipigs. We showed that the plant collagen was biocompatible and was able to stably regenerate the corneas of minipigs comparable to yeast-produced recombinant collagen that we previously tested in clinical trials. The advantage of the plant collagen is that the supply is potentially limitless.

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