Immunolocalization of 67 kDa elastin-binding protein in perinatal rat lungs

1992 ◽  
Vol 268 (2) ◽  
pp. 277-281 ◽  
Author(s):  
Kojiro Wasano ◽  
Yasuhiro Hirakawa ◽  
Keiichiro Nakamura

1995 ◽  
Vol 220 (2) ◽  
pp. 312-324 ◽  
Author(s):  
Aleksander Hinek ◽  
Fred W. Keeley ◽  
John Callahans


2012 ◽  
Vol 288 (2) ◽  
pp. 1317-1328 ◽  
Author(s):  
Charlotte Blanchevoye ◽  
Nicolas Floquet ◽  
Amandine Scandolera ◽  
Stéphanie Baud ◽  
Pascal Maurice ◽  
...  


2005 ◽  
Vol 167 (6) ◽  
pp. 1689-1698 ◽  
Author(s):  
Anna Caciotti ◽  
Maria Alice Donati ◽  
Tiziana Bardelli ◽  
Alessandra d'Azzo ◽  
Graziella Massai ◽  
...  


1982 ◽  
Vol 204 (1) ◽  
pp. 97-102 ◽  
Author(s):  
G L Sanford ◽  
L D Davis ◽  
J T Powell

The subcellular localization of the beta-galactoside-binding protein, or lectin, from rat lung was investigated by the specific binding of anti-lectin immunoglobulin G to subcellular fractions. We used both adult and immature (12-day-old) rats; the immature rat lungs have an 8-10-fold greater concentration than adult rat lungs [Powell & Whitney (1980) Biochem. J. 188, 1-8]. In both groups of animals we observed greater specific binding of anti-lectin immunoglobulin G to intracellular membrane (mitochondrial and microsomal fractions) than to plasma membranes. Pre-incubation of membrane fractions with lactose resulted in a marked diminution of anti-lectin immunoglobulin G binding. In the adult rat lung most (approx. 80%) of the lectin activity was membrane-associated. In the immature rat lung only approx. 30% of the lectin activity was membrane associated and most of the beta-galactoside-binding protein appeared to be a soluble cytoplasmic component. The rat lung beta-galactoside-binding protein appeared to have a broad but predominantly intracellular location, being associated with membranes through one of its galactoside-binding sites.



2004 ◽  
Vol 11 (3) ◽  
pp. 159-166 ◽  
Author(s):  
Hiroshi Wachi ◽  
Hideki Sugitani ◽  
Hayato Murata ◽  
Junji Nakazawa ◽  
Robert P. Mecham ◽  
...  


Nature ◽  
2002 ◽  
Vol 415 (6868) ◽  
pp. 168-171 ◽  
Author(s):  
Hiromi Yanagisawa ◽  
Elaine C. Davis ◽  
Barry C. Starcher ◽  
Takashi Ouchi ◽  
Masashi Yanagisawa ◽  
...  


1994 ◽  
Vol 126 (2) ◽  
pp. 563-574 ◽  
Author(s):  
A Hinek ◽  
M Rabinovitch

The 67-kD elastin-binding protein (EBP) mediates cell adhesion to elastin and elastin fiber assembly, and it is similar, if not identical, to the 67-kD enzymatically inactive, alternatively spliced beta-galactosidase. The latter contains an elastin binding domain (S-GAL) homologous both to the aorta EBP and to NH2-terminal sequences of serine proteinases (Hinek, A., M. Rabinovitch, F. W. Keeley, and J. Callahan. 1993. J. Clin. Invest. 91:1198-1205). We now confirm the functional importance of this homology by showing that elastolytic activity of a representative serine elastase, porcine pancreatic elastase, was prevented by an antibody (anti-S-GAL) and by competing with purified EBP or S-GAL peptide. Immunohistochemistry of adult aorta indicates that the EBP exists as a permanent component of mature elastic fibers. This observation, together with the in vitro studies, suggests that the EBP could protect insoluble elastin from extracellular proteolysis and contribute to the extraordinary stability of this protein. Double immunolabeling of fetal lamb aorta with anti-S-GAL and antitropoelastin antibodies demonstrated, under light and electron microscopy, intracellular colocalization of the proteins in smooth muscle cells (SMC). Incubation of SMC with galactosugars to dissociate tropoelastin from EBP caused intracellular aggregation of tropoelastin. A tropoelastin/EBP complex was extracted from SMC lysates by coimmunoprecipitation and cross-linking, and its functional significance was addressed by showing that its dissociation by galactosugars caused degradation of tropoelastin by endogenous serine proteinase(s). This suggests that the EBP may also serve as a "companion" to intracellular tropoelastin, protecting this highly hydrophobic protein from self-aggregation and proteolytic degradation.



2006 ◽  
Vol 126 (12) ◽  
pp. 2707-2714 ◽  
Author(s):  
Qian Zheng ◽  
Jiwon Choi ◽  
Leonie Rouleau ◽  
Richard L. Leask ◽  
James A. Richardson ◽  
...  


Biochemistry ◽  
2013 ◽  
Vol 52 (44) ◽  
pp. 7731-7741 ◽  
Author(s):  
Ming Miao ◽  
Sean E. Reichheld ◽  
Lisa D. Muiznieks ◽  
Yayi Huang ◽  
Fred W. Keeley


2014 ◽  
Vol 156 (3) ◽  
pp. 155-162 ◽  
Author(s):  
Makoto Nakakido ◽  
Chihiro Aikawa ◽  
Ichiro Nakagawa ◽  
Kouhei Tsumoto


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