Human and sheep growth-plate cartilage type X collagen synthesis and the influence of tissue storage.
Direct comparison of type X collagen synthesized by human, sheep and chick growth-plate cartilage has shown that the human type X collagen is similar to the chick in both its molecular mass, containing component alpha-chains of 59 kDa with helical regions of 45 kDa, and apparent absence of disulphide-stabilized aggregates, whereas the sheep type X collagen has slightly larger alpha-chains (63 kDa) accounted for by a longer helical region (49 kDa) that contains cystine residues essential for the formation of the high-molecular-mass aggregates found with this species. Type X collagen from all three species showed heterogeneity in primary collagen structure as revealed by Staphylococcus aureus V8 proteinase-generated peptide maps. Collagen synthesis by growth-plate cartilage in culture, particularly synthesis of type IX and X collagen, was shown to be very sensitive to prior storage and suggests caution in the interpretation of changes detected when examining collagen synthesis by growth plates in culture.
Gibson
G J
GJ
Department of Chemical Pathology, Adelaide Children's Hospital, South Australia.
Francki
K T
KT
Hopwood
J J
JJ
Foster
B K
BK
D000375:Aging; D000818:Animals; D002648:Child; D002675:Child, Preschool; D003094:Collagen / Q000096:biosynthesis* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D005333:Fetus; D006132:Growth Plate / Q000254:growth & development / Q000378:metabolism* / Q000473:pathology; D006801:Humans; D007223:Infant; D007700:Kinetics; D008970:Molecular Weight; D011180:Postmortem Changes; D014176:Protein Biosynthesis; D011506:Proteins / Q000302:isolation & purification; D012756:Sheep; D013696:Temperature
D011506:Proteins; D003094:Collagen