Vascularisation and progenitor cells of primary and secondary ossification centres in the human growth plate

2013 ◽  
Author(s):  
Sonja M Walzer ◽  
Erdal Cetin ◽  
Ruth Grubl-Barabas ◽  
Irene Sulzbacher ◽  
Beate Ruger ◽  
...  
2014 ◽  
Vol 14 (1) ◽  
Author(s):  
Sonja M Walzer ◽  
Erdal Cetin ◽  
Ruth Grübl-Barabas ◽  
Irene Sulzbacher ◽  
Beate Rueger ◽  
...  

Author(s):  
Joshua M. Abzug ◽  
Hongying Tian ◽  
Masatake Matsuoka ◽  
Danielle A. Hogarth ◽  
Casey M. Codd ◽  
...  

2013 ◽  
Vol 38 (4) ◽  
pp. 881-889 ◽  
Author(s):  
Karin Pichler ◽  
Tanja Kraus ◽  
Elisabeth Martinelli ◽  
Patrick Sadoghi ◽  
Giuseppe Musumeci ◽  
...  

2014 ◽  
Vol 53 (1) ◽  
pp. T1-T9 ◽  
Author(s):  
Julian C Lui ◽  
Ola Nilsson ◽  
Jeffrey Baron

For most bones, elongation is driven primarily by chondrogenesis at the growth plates. This process results from chondrocyte proliferation, hypertrophy, and extracellular matrix secretion, and it is carefully orchestrated by complex networks of local paracrine factors and modulated by endocrine factors. We review here recent advances in the understanding of growth plate physiology. These advances include new approaches to study expression patterns of large numbers of genes in the growth plate, using microdissection followed by microarray. This approach has been combined with genome-wide association studies to provide insights into the regulation of the human growth plate. We also review recent studies elucidating the roles of bone morphogenetic proteins, fibroblast growth factors, C-type natriuretic peptide, and suppressor of cytokine signaling in the local regulation of growth plate chondrogenesis and longitudinal bone growth.


1991 ◽  
Vol 99 (3) ◽  
pp. 641-649 ◽  
Author(s):  
A. Marriott ◽  
S. Ayad ◽  
M.E. Grant

Chondrocytes were isolated from bovine growth-plate cartilage and cultured within type I collagen gels. A major collagen with chains of Mr 59,000, decreasing to 47,000 on pepsinization, was synthesized and identified as type X collagen. This collagen was cleaved at two sites by mammalian collagenase, resulting in a major triple-helical fragment with chains of Mr 32,000. The species of Mr 59,000, 47,000 and 32,000 were not detected by SDS-polyacrylamide gel electrophoresis before reduction, indicating the presence of disulphide bonds within the triple helix. In contrast, similar biosynthetic studies with human growth-plate cartilage in organ culture, indicated that human type X collagen does not contain disulphide bonds. A polyclonal antiserum was raised to bovine type X collagen and used in immunolocalization studies to provide direct evidence for the association of type X collagen with the hypertrophic chondrocytes in both bovine and human growth plates during development.


2010 ◽  
Vol 52 (3) ◽  
pp. 235-241 ◽  
Author(s):  
Toshiyuki Inoue ◽  
Kiichi Suzuki ◽  
Hideaki Maehara ◽  
Katsuji Shimizu
Keyword(s):  

2012 ◽  
Vol 21 (23) ◽  
pp. 5193-5201 ◽  
Author(s):  
Julian C. Lui ◽  
Ola Nilsson ◽  
Yingleong Chan ◽  
Cameron D. Palmer ◽  
Anenisia C. Andrade ◽  
...  

2004 ◽  
Vol 74 (2) ◽  
pp. 181-186 ◽  
Author(s):  
E. Cetin ◽  
W. Girsch ◽  
G. Brand ◽  
D. Thurnher ◽  
E. M. Cetin ◽  
...  
Keyword(s):  

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