Self-Assembly of Elastin-Based Peptides into the ECM: the Importance of Integrins and the Elastin Binding Protein in Elastic Fiber Assembly

2011 ◽  
Vol 12 (2) ◽  
pp. 432-440 ◽  
Author(s):  
Dhaval Patel ◽  
Rohan Menon ◽  
Lakeshia J. Taite

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


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.



2013 ◽  
Vol 110 (8) ◽  
pp. 2852-2857 ◽  
Author(s):  
K. Noda ◽  
B. Dabovic ◽  
K. Takagi ◽  
T. Inoue ◽  
M. Horiguchi ◽  
...  


2007 ◽  
Vol 26 (14) ◽  
pp. 3283-3295 ◽  
Author(s):  
Maretoshi Hirai ◽  
Masahito Horiguchi ◽  
Tetsuya Ohbayashi ◽  
Toru Kita ◽  
Kenneth R Chien ◽  
...  


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Akira Minami ◽  
Yuka Fujita ◽  
Jun Goto ◽  
Ayano Iuchi ◽  
Kosei Fujita ◽  
...  

AbstractReduction of elastin in the skin causes various skin diseases as well as wrinkles and sagging with aging. Sialidase is a hydrolase that cleaves a sialic acid residue from sialoglycoconjugate. Cleavage of sialic acid from microfibrils by the sialidase isozyme Neu1 facilitates elastic fiber assembly. In the present study, we showed that a lower layer of the dermis and muscle showed relatively intense sialidase activity. The sialidase activity in the skin decreased with aging. Choline and geranate (CAGE), one of the ionic liquids, can deliver the sialidase subcutaneously while maintaining the enzymatic activity. The elastin level in the dermis was increased by applying sialidase from Arthrobacter ureafaciens (AUSA) with CAGE on the skin for 5 days in rats and senescence-accelerated mice prone 1 and 8. Sialidase activity in the dermis was considered to be mainly due to Neu2 based on the expression level of sialidase isozyme mRNA. Transdermal administration of Neu2 with CAGE also increased the level of elastin in the dermis. Therefore, not only Neu1 but also Neu2 would be involved in elastic fiber assembly. Transdermal administration of sialidase is expected to be useful for improvement of wrinkles and skin disorders due to the loss of elastic fibers.



2014 ◽  
Vol 289 (50) ◽  
pp. 34815-34826 ◽  
Author(s):  
Giselle C. Yeo ◽  
Clair Baldock ◽  
Steven G. Wise ◽  
Anthony S. Weiss


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


Sign in / Sign up

Export Citation Format

Share Document