Immunohistochemical localization of a tenascin-like extracellular matrix protein in sea urchin embryos

1990 ◽  
Vol 199 (3) ◽  
pp. 169-173 ◽  
Author(s):  
John A. Anstrom ◽  
Eleanor J. Mackie ◽  
Richard P. Tucker
Keyword(s):  
Extracellular Matrix ◽  
Sea Urchin ◽  
Matrix Protein ◽  
Immunohistochemical Localization ◽  
Extracellular Matrix Protein ◽  
Sea Urchin Embryos

scholarly journals Developmental Regulation of FKBP65

2000 ◽  
Vol 11 (11) ◽  
pp. 3925-3935 ◽  
Author(s):  
Charles E. Patterson ◽  
Theresa Schaub ◽  
Elaine J. Coleman ◽  
Elaine C. Davis
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Subcellular Fractionation ◽  
Immunohistochemical Localization ◽  
Extracellular Matrix Protein ◽  
Elastic Fibers ◽  
Airway Smooth Muscle Cells ◽  
Specific Expression ◽  
Adult Tissues ◽  
Mouse Tissues

FKBP65 (65-kDa FK506-binding protein) is a member of the highly conserved family of intracellular receptors called immunophilins. All have the property of peptidyl-prolyl cis-trans isomerization, and most have been implicated in folding and trafficking events. In an earlier study, we identified that FKBP65 associates with the extracellular matrix protein tropoelastin during its transport through the cell. In the present study, we have carried out a detailed investigation of the subcellular localization of FKBP65 and its relationship to tropoelastin. Using subcellular fractionation, Triton X-114 phase separation, protease protection assays, and immunofluorescence microscopy (IF), we have identified that FKBP65 is contained within the lumen of the endoplasmic reticulum (ER). Subsequent IF studies colocalized FKBP65 with tropoelastin and showed that the two proteins dissociate before reaching the Golgi apparatus. Immunohistochemical localization of FKBP65 in developing lung showed strong staining of vascular and airway smooth muscle cells. Similar areas stained positive for the presence of elastic fibers in the extracellular matrix. The expression of FKBP65 was investigated during development as tropoelastin is not expressed in adult tissues. Tissue-specific expression of FKBP65 was observed in 12-d old mouse tissues; however, the pattern of expression of FKBP65 was not restricted to those tissues expressing tropoelastin. This suggests that additional ligands for FKBP65 likely exist within the ER. Remarkably, in the adult tissues examined, FKBP65 expression was absent or barely detectable. Taken together, these results support an ER-localized FKBP65-tropoelastin interaction that occurs specifically during growth and development of tissues.

A new extracellular matrix protein of the sea urchin embryo with properties of a substrate adhesion molecule

1992 ◽  
Vol 201 (3) ◽  
pp. 173-178 ◽  
Author(s):  
Valeria Matranga ◽  
Daniela Ferrol ◽  
Francesca Zito ◽  
Melchiorre Cervello ◽  
Eizo Nakano
Keyword(s):  
Extracellular Matrix ◽  
Sea Urchin ◽  
Adhesion Molecule ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Substrate Adhesion ◽  
Sea Urchin Embryo

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