Molecular characterization of Calymmin, a novel notochord sheath-associated extracellular matrix protein in the zebrafish embryo

2002 ◽  
Vol 224 (2) ◽  
pp. 200-209 ◽  
Author(s):  
Joan Cerdà ◽  
Christine Gründ ◽  
Werner W. Franke ◽  
Michael Brand
Keyword(s):  
Extracellular Matrix ◽  
Molecular Characterization ◽  
Matrix Protein ◽  
Zebrafish Embryo ◽  
Extracellular Matrix Protein

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

scholarly journals 3317 Localization and characterization of a novel extracellular matrix protein β-IG-H3

1995 ◽  
Vol 35 ◽  
pp. S136
Author(s):  
I. Rawe ◽  
Q. Zhan ◽  
Y. Komai-Hori ◽  
R. Burrows ◽  
C.L. Kublin ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein

scholarly journals Identification and characterization of a novel extracellular matrix protein nephronectin that is associated with integrin α8β1 in the embryonic kidney

2001 ◽  
Vol 154 (2) ◽  
pp. 447-458 ◽  
Author(s):  
Ralph Brandenberger ◽  
Andrea Schmidt ◽  
James Linton ◽  
Denan Wang ◽  
Carey Backus ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Cdna Libraries ◽  
Newborn Mouse ◽  
Metanephric Mesenchyme ◽  
Rgd Sequence ◽  
Kidney Organogenesis

The epithelial–mesenchymal interactions required for kidney organogenesis are disrupted in mice lacking the integrin α8β1. None of this integrin's known ligands, however, appears to account for this phenotype. To identify a more relevant ligand, a soluble integrin α8β1 heterodimer fused to alkaline phosphatase (AP) has been used to probe blots and cDNA libraries. In newborn mouse kidney extracts, α8β1-AP detects a novel ligand of 70–90 kD. This protein, named nephronectin, is an extracellular matrix protein with five EGF-like repeats, a mucin region containing a RGD sequence, and a COOH-terminal MAM domain. Integrin α8β1 and several additional RGD-binding integrins bind nephronectin. Nephronectin mRNA is expressed in the ureteric bud epithelium, whereas α8β1 is expressed in the metanephric mesenchyme. Nephronectin is localized in the extracellular matrix in the same distribution as the ligand detected by α8β1-AP and forms a complex with α8β1 in vivo. Thus, these results strongly suggest that nephronectin is a relevant ligand mediating α8β1 function in the kidney. Nephronectin is expressed at numerous sites outside the kidney, so it may also have wider roles in development. The approaches used here should be generally useful for characterizing the interactions of novel extracellular matrix proteins identified through genomic sequencing projects.

scholarly journals Extracellular matrix protein microarray-based biosensor with single cell resolution: Integrin profiling and characterization of cell-biomaterial interactions

2019 ◽  
Vol 299 ◽  
pp. 126954 ◽  
Author(s):  
Ainhoa Gonzalez-Pujana ◽  
Edorta Santos-Vizcaino ◽  
Maite García-Hernando ◽  
Beatriz Hernaez-Estrada ◽  
Marian M. de Pancorbo ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Single Cell ◽  
Matrix Protein ◽  
Protein Microarray ◽  
Extracellular Matrix Protein

Generation and characterization of a mouse/human chimeric antibody directed against extracellular matrix protein tenascin

1994 ◽  
Vol 52 (2) ◽  
pp. 127-137 ◽  
Author(s):  
Xuanmin He ◽  
Gary E. Archer ◽  
Carol J. Wikstrand ◽  
Sherie L. Morrison ◽  
Michael R. Zalutsky ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Chimeric Antibody
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