scholarly journals Rapid formation of capillary endothelial cells in rat skeletal muscle after exposure to insulin

Diabetologia ◽  
1996 ◽  
Vol 39 (2) ◽  
pp. 206-211 ◽  
Author(s):  
A. Holm�ng ◽  
E. Jennische ◽  
P. Bj�rntorp
Development ◽  
1992 ◽  
Vol 116 (3) ◽  
pp. 585-600 ◽  
Author(s):  
J.L. Duband ◽  
A.M. Belkin ◽  
J. Syfrig ◽  
J.P. Thiery ◽  
V.E. Koteliansky

In this study, we have examined the spatiotemporal distribution of the alpha 1 integrin subunit, a putative laminin and collagen receptor, in avian embryos, using immunofluorescence microscopy and immunoblotting techniques. We used an antibody raised against a gizzard 175 × 10(3) M(r) membrane protein which was described previously and which we found to be immunologically identical to the chicken alpha 1 integrin subunit. In adult avian tissues, alpha 1 integrin exhibited a very restricted pattern of expression; it was detected only in smooth muscle and in capillary endothelial cells. In the developing embryo, alpha 1 integrin subunit expression was discovered in addition to smooth muscle and capillary endothelial cells, transiently, in both central and peripheral nervous systems and in striated muscles, in association with laminin and collagen IV. alpha 1 integrin was practically absent from most epithelial tissues, including the liver, pancreas and kidney tubules, and was weakly expressed by tissues that were not associated with laminin and collagen IV. In the nervous system, alpha 1 integrin subunit expression occurred predominantly at the time of early neuronal differentiation. During skeletal muscle development, alpha 1 integrin was expressed on myogenic precursors, during myoblast migration, and in differentiating myotubes. alpha 1 integrin disappeared from skeletal muscle cells as they became contractile. In visceral and vascular smooth muscles, alpha 1 integrin appeared specifically during early smooth muscle cell differentiation and, later, was permanently expressed after cell maturation. These results indicate that (i) the expression pattern of alpha 1 integrin is consistent with a function as a laminin/collagen IV receptor; (ii) during avian development, expression of the alpha 1 integrin subunit is spatially and temporally regulated; (iii) during myogenesis and neurogenesis, expression of alpha 1 integrin is transient and correlates with cell migration and differentiation.


1993 ◽  
Vol 292 (3) ◽  
pp. 639-641 ◽  
Author(s):  
L A Räsänen ◽  
U Karvonen ◽  
A R Pösö

In situ hybridization was used to localize xanthine dehydrogenase (XDH) mRNA in horse skeletal muscle. Capillary endothelial cells were found to express XDH, but muscle cells did not give any signal. The digoxigenin-labelled probe was produced by PCR with primers based on the cDNA sequence of mouse XDH and horse lung cDNAs. A 4.3 kb mRNA was detected in a Northern blot.


Aging Cell ◽  
2013 ◽  
Vol 13 (2) ◽  
pp. 254-262 ◽  
Author(s):  
Huijuan Wang ◽  
Anne Listrat ◽  
Bruno Meunier ◽  
Marine Gueugneau ◽  
Cécile Coudy‐Gandilhon ◽  
...  

2022 ◽  
Vol 12 (1) ◽  
Author(s):  
Marina Cefis ◽  
Remi Chaney ◽  
Aurore Quirié ◽  
Clélia Santini ◽  
Christine Marie ◽  
...  

AbstractBDNF (brain-derived neurotrophic factor) is present in skeletal muscle, controlling muscular metabolism, strength and regeneration processes. However, there is no consensus on BDNF cellular source. Furthermore, while endothelial tissue expresses BDNF in large amount, whether endothelial cells inside muscle expressed BDNF has never been explored. The aim of the present study was to provide a comprehensive analysis of BDNF localization in rat skeletal muscle. Cellular localization of BDNF and activated Tropomyosin-related kinase B (TrkB) receptors was studied by immunohistochemical analysis on soleus (SOL) and gastrocnemius (GAS). BDNF and activated TrkB levels were also measured in muscle homogenates using Western blot analysis and/or Elisa tests. The results revealed BDNF immunostaining in all cell types examined with a prominent staining in endothelial cells and a stronger staining in type II than type I muscular fibers. Endothelial cells but not other cells displayed easily detectable activated TrkB receptor expression. Levels of BDNF and activated TrkB receptors were higher in SOL than GAS. In conclusion, endothelial cells are an important and still unexplored source of BDNF present in skeletal muscle. Endothelial BDNF expression likely explains why oxidative muscle exhibits higher BDNF levels than glycolytic muscle despite higher the BDNF expression by type II fibers.


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