Reelin, the Extracellular Matrix Protein Deficient in Reeler Mutant Mice, Is Processed by a Metalloproteinase

1999 ◽  
Vol 156 (1) ◽  
pp. 214-217 ◽  
Author(s):  
Catherine Lambert de Rouvroit ◽  
Vinciane de Bergeyck ◽  
Caroline Cortvrindt ◽  
Isabelle Bar ◽  
Yves Eeckhout ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Mutant Mice ◽  
Extracellular Matrix Protein ◽  
Reeler Mutant

scholarly journals Mystery solved

2001 ◽  
Vol 154 (2) ◽  
pp. 257-260 ◽  
Author(s):  
Jeffrey H. Miner
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Kidney Development ◽  
Mutant Mice ◽  
Wolffian Duct ◽  
Extracellular Matrix Protein ◽  
Ureteric Bud ◽  
Lines Of Evidence

Mutant mice lacking the integrin α8 subunit exhibit variable defects in kidney development with most mutants missing both kidneys. Several lines of evidence indicate that the known extracellular matrix ligands for integrin α8β1 are either dispensable for or not involved in α8β1 signaling during kidney development. This suggests the presence of an unknown ligand. A novel α8β1 ligand, nephronectin, has now been identified. Nephronectin is a new extracellular matrix protein associated with the Wolffian duct and the ureteric bud, epithelial structures with well-defined roles in kidney development.

1280: Increased Susceptibility to Genitovaginal Prolapse Associated with a Polymorphism in the Promoter of the Extracellular Matrix Protein LAMC1

2007 ◽  
Vol 177 (4S) ◽  
pp. 421-422
Author(s):  
Ganka Nikolova ◽  
Christian O. Twiss ◽  
Hane Lee ◽  
Nelson Stanley ◽  
Janet Sinsheimer ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Increased Susceptibility

scholarly journals Homogenous overexpression of the extracellular matrix protein Netrin-1 in a hollow fiber bioreactor

2021 ◽  
Author(s):  
Aniel Moya-Torres ◽  
Monika Gupta ◽  
Fabian Heide ◽  
Natalie Krahn ◽  
Scott Legare ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Hollow Fiber ◽  
Mammalian Cells ◽  
Matrix Protein ◽  
Continuous Production ◽  
Extracellular Matrix Protein ◽  
Close Monitoring ◽  
High Quality ◽  
Biolayer Interferometry ◽  
Hollow Fiber Bioreactor

Abstract The production of recombinant proteins for functional and biophysical studies, especially in the field of structural determination, still represents a challenge as high quality and quantities are needed to adequately perform experiments. This is in part solved by optimizing protein constructs and expression conditions to maximize the yields in regular flask expression systems. Still, work flow and effort can be substantial with no guarantee to obtain improvements. This study presents a combination of workflows that can be used to dramatically increase protein production and improve processing results, specifically for the extracellular matrix protein Netrin-1. This proteoglycan is an axon guidance cue which interacts with various receptors to initiate downstream signaling cascades affecting cell differentiation, proliferation, metabolism, and survival. We were able to produce large glycoprotein quantities in mammalian cells, which were engineered for protein overexpression and secretion into the media using the controlled environment provided by a hollow fiber bioreactor. Close monitoring of the internal bioreactor conditions allowed for stable production over an extended period of time. In addition to this, Netrin-1 concentrations were monitored in expression media through biolayer interferometry which allowed us to increase Netrin-1 media concentrations tenfold over our current flask systems while preserving excellent protein quality and in solution behavior. Our particular combination of genetic engineering, cell culture system, protein purification, and biophysical characterization permitted us to establish an efficient and continuous production of high-quality protein suitable for structural biology studies that can be translated to various biological systems. Key points • Hollow fiber bioreactor produces substantial yields of homogenous Netrin-1 • Biolayer interferometry allows target protein quantitation in expression media • High production yields in the bioreactor do not impair Netrin-1 proteoglycan quality Graphical abstract

Direct interaction of the extracellular matrix protein DANCE with apolipoprotein(a) mediated by the kringle IV-type 2 domain

2002 ◽  
Vol 267 (4) ◽  
pp. 440-446 ◽  
Author(s):  
A. Kapetanopoulos ◽  
F. Fresser ◽  
G. Millonig ◽  
Y. Shaul ◽  
G. Baier ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Direct Interaction ◽  
Extracellular Matrix Protein ◽  
Apolipoprotein A

scholarly journals Characterization of the human extracellular matrix protein 1 gene on chromosome 1q21

1997 ◽  
Vol 16 (5) ◽  
pp. 289-292 ◽  
Author(s):  
Maureen R. Johnson ◽  
Douglas J. Wilkin ◽  
Hans L. Vos ◽  
Rosa Isela Ortiz De Luna ◽  
Anindya M. Dehejia ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Extracellular Matrix Protein 1 ◽  
Chromosome 1Q21

Argon Laser Welding Induces Degradation And Crosslinking Of Extracellular Matrix Protein: A Preliminary Report

1989 ◽  
Author(s):  
Lyndon Su ◽  
Louann W. Murray ◽  
Rodney A. White ◽  
George Kopchok ◽  
Carol Guthrie ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Laser Welding ◽  
Preliminary Report ◽  
Matrix Protein ◽  
Protein A ◽  
Argon Laser ◽  
Extracellular Matrix Protein

scholarly journals Molecular Structure and Tissue Distribution of Matrilin-3, a Filament-forming Extracellular Matrix Protein Expressed during Skeletal Development

2000 ◽  
Vol 275 (6) ◽  
pp. 3999-4006 ◽  
Author(s):  
Andreas R. Klatt ◽  
D. Patric Nitsche ◽  
Birgit Kobbe ◽  
Matthias Mörgelin ◽  
Mats Paulsson ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Extracellular Matrix ◽  
Tissue Distribution ◽  
Matrix Protein ◽  
Skeletal Development ◽  
Extracellular Matrix Protein
Sign in / Sign up

Export Citation Format

Share Document