scholarly journals Peroxynitrite modifies the structure and function of the extracellular matrix proteoglycan perlecan by reaction with both the protein core and the heparan sulfate chains

2010 ◽  
Vol 49 (2) ◽  
pp. 282-293 ◽  
Author(s):  
Eleanor C. Kennett ◽  
Martin D. Rees ◽  
Ernst Malle ◽  
Astrid Hammer ◽  
John M. Whitelock ◽  
...  
2020 ◽  
Author(s):  
Reena Singh ◽  
Richard Tan ◽  
Clara Tran ◽  
Thomas Loudovaris ◽  
Helen E. Thomas ◽  
...  

Oncotarget ◽  
2017 ◽  
Vol 8 (11) ◽  
pp. 17981-17994 ◽  
Author(s):  
Balaji Krishnamachary ◽  
Ioannis Stasinopoulos ◽  
Samata Kakkad ◽  
Marie-France Penet ◽  
Desmond Jacob ◽  
...  

2012 ◽  
Vol 180 (5) ◽  
pp. 1863-1878 ◽  
Author(s):  
Gerald C. Koenig ◽  
R. Grant Rowe ◽  
Sharlene M. Day ◽  
Farideh Sabeh ◽  
Jeffrey J. Atkinson ◽  
...  

2014 ◽  
Vol 2014 ◽  
pp. 1-15 ◽  
Author(s):  
Manoel Luís Costa

The function of muscle is to contract, which means to exert force on a substrate. The adaptations required for skeletal muscle differentiation, from a prototypic cell, involve specialization of housekeeping cytoskeletal contracting and supporting systems into crystalline arrays of proteins. Here I discuss the changes that all three cytoskeletal systems (microfilaments, intermediate filaments, and microtubules) undergo through myogenesis. I also discuss their interaction, through the membrane, to extracellular matrix and to other cells, where force will be exerted during contraction. The three cytoskeletal systems are necessary for the muscle cell and must exert complementary roles in the cell. Muscle is a responsive system, where structure and function are integrated: the structural adaptations it undergoes depend on force production. In this way, the muscle cytoskeleton is a portrait of its physiology. I review the cytoskeletal proteins and structures involved in muscle function and focus particularly on their role in myogenesis, the process by which this incredible muscle machine is made. Although the focus is on skeletal muscle, some of the discussion is applicable to cardiac and smooth muscle.


1991 ◽  
Vol 69 (3) ◽  
pp. 618-627 ◽  
Author(s):  
William R. Bates ◽  
Joan E. Mallett

Molgula pacifica embryos exhibit anural development in which embryogenesis proceeds directly to the development of a juvenile, without the development of a tailed larva. The purpose of this study was to investigate the key events that are responsible for the development of M. pacifica juveniles. The results of the present investigation indicate that the timing and spatial rearrangements of the egg cytoplasm that occur after fertilization (termed ooplasmic segregation) are similar in M. pacifica eggs as compared with those that occur in typical urodele species. These observations suggest that the mechanism that is responsible for the urodele pattern of ooplasmic segregation was conserved during the evolution of anural species. The cleavage patterns displayed by M. pacifica embryos up to the eight-cell stage were similar to those exhibited by urodele embryos. However, gastrulation in M. pacifica embryos differed from the typical urodele mode of gastrulation. The mode of gastrulation exhibited by M. pacifica embryos is likely a consequence of their eggs containing a greater quantity of yolk than the less yolky eggs of species more commonly studied. In the second part of this investigation, ampullar development, structure, and function were studied. Two conclusions were made from these studies. First, the extracellular matrix materials comprising the tunic are secreted by the epidermal ampullar cells. Second, a shift in the timing of ampullar rudiment development in M. pacifica embryos suggests the possibility of a heterochronic mechanism of evolutionary change within the epidermal cell lineage.


2017 ◽  
Author(s):  
Yu Chen ◽  
Barbara A. Bensing ◽  
Ravin Seepersaud ◽  
Wei Mi ◽  
Maofu Liao ◽  
...  

ABSTRACTMany pathogenic bacteria, including Streptococcus gordonii, possess a pathway for the export of a single serine-rich-repeat protein that mediates the adhesion of bacteria to host cells and the extracellular matrix. These adhesins are O-glycosylated by several cytosolic glycosyltransferases and require three accessory Sec proteins (Asp1-3) for export, but how the adhesins are processed for secretion is not well defined. Here, we show that O-glycosylation of S. gordonii adhesin GspB occurs in a sequential manner by three enzymes (GtfA/B, Nss, Gly) that attach N-acetylglucosamine and glucose to Ser/Thr residues. The modified substrate is subsequently transferred from the last glycosyltransferase to the Asp1/2/3 complex. Crystal structures show that both Asp1 and Asp3 are related to carbohydrate binding proteins. Asp1 also has an affinity for phospholipids, which is attenuated by Asp2. These results suggest a mechanism for the modification of adhesin in the cytosol and its subsequent targeting to the export machinery.


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