scholarly journals The distribution and initial characterization of oligosaccharide units on the COOH-terminal propeptide extensions of the pro-alpha 1 and pro-alpha 2 chains of type I procollagen.

1979 ◽  
Vol 254 (21) ◽  
pp. 10798-10802
Author(s):  
C.C. Clark
Author(s):  
Jae-Ho Hwang ◽  
Yoshihiro Yokoyama ◽  
Shoshi Mizuta ◽  
Reiji Yoshinaka

Author(s):  
Paul Tolstoshev ◽  
Charles D. Boyd ◽  
Millie P. Schafer ◽  
Bruce C. Trapnell ◽  
Helen C. Coon ◽  
...  

1994 ◽  
Vol 269 (15) ◽  
pp. 11381-11390
Author(s):  
Y. Hojima ◽  
M.M. Mörgelin ◽  
J. Engel ◽  
M.M. Boutillon ◽  
M. van der Rest ◽  
...  

1986 ◽  
Vol 163 (2) ◽  
pp. 400-413 ◽  
Author(s):  
D F Bainton ◽  
M A Maloney ◽  
H M Patt ◽  
R Stern

Rabbit stromal fibroblasts subcultured from red and yellow bone marrow and implanted beneath the renal capsule form ossicles the hemic cellularity of which mirrors the cellularity of the marrow used for culture. Although the cultured red and yellow marrow cells are similar in fine-structural appearance, they differ strikingly in enzymatic content of alpha-naphthylbutyrate esterase, which is abundant only in the cells derived from yellow marrow. Other observers (20, 21) have proposed that stromal fibroblasts are preadipocytes, and this data suggests that those derived from yellow marrow have the phenotype of more differentiated adipocytes. On the other hand, fibroblasts derived from red and yellow bone marrow show no differences in their profiles of procollagen synthesis. Both types of fibroblasts secrete type III procollagen as the major species, with a I/III ratio of 1:3; in contrast, rabbit dermal fibroblasts have a prominent peak of type I procollagen. The similarity of stromal cells derived from red and yellow bone marrow in procollagen synthesis suggests that the collagen part of the extracellular matrix is not the only basis for their intrinsic difference in capacity for hematopoiesis.


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