TY - JOUR
T1 - Fibrogenesis and biosynthesis of elastin in cartilage
AU - Quintarelli, Giuliano
AU - Starcher, Barry C.
AU - Vocaturo, Amina
AU - Gianfilippo, Franca Di
AU - Gotte, Lorenzo
AU - Mecham, Robert P.
PY - 1979/1/1
Y1 - 1979/1/1
N2 - This study presents direct evidence that dissociated chondroblasts from rabbit ear cartilage grown in vitro are capable of synthesizing insoluble elastin. Ultrastructural examination indicated that at an early stage of tissue development, elastogenesis is initiated producing a form of primary fibrils which later condense into an electron dense amorphous material which, unlike other elastin-containing tissues, is heavily stained by metal cations and lacks peripheral microfibrils. Native elastic fibrils and the mature elastic fiber bundles are both susceptible to elastase digestion. Transmission electronmicroscopy demonstrated the presence of many intracellular filaments all showing a substructural organization and localized in close proximity to the nucleus. Their possible contractile nature is discussed. Amino acid analysis of cartilage elastin and of the elastin synthesized in vitro revealed a close chemical similarity between the two molecules. Ultrastructural analysis of the in vitro elastin demonstrated a substructural organization quite similar to that of the elastin observed in an in vivo system.
AB - This study presents direct evidence that dissociated chondroblasts from rabbit ear cartilage grown in vitro are capable of synthesizing insoluble elastin. Ultrastructural examination indicated that at an early stage of tissue development, elastogenesis is initiated producing a form of primary fibrils which later condense into an electron dense amorphous material which, unlike other elastin-containing tissues, is heavily stained by metal cations and lacks peripheral microfibrils. Native elastic fibrils and the mature elastic fiber bundles are both susceptible to elastase digestion. Transmission electronmicroscopy demonstrated the presence of many intracellular filaments all showing a substructural organization and localized in close proximity to the nucleus. Their possible contractile nature is discussed. Amino acid analysis of cartilage elastin and of the elastin synthesized in vitro revealed a close chemical similarity between the two molecules. Ultrastructural analysis of the in vitro elastin demonstrated a substructural organization quite similar to that of the elastin observed in an in vivo system.
UR - http://www.scopus.com/inward/record.url?scp=0018673887&partnerID=8YFLogxK
U2 - 10.3109/03008207909152348
DO - 10.3109/03008207909152348
M3 - Article
C2 - 158482
AN - SCOPUS:0018673887
VL - 7
SP - 1
EP - 19
JO - Connective Tissue Research
JF - Connective Tissue Research
SN - 0300-8207
IS - 1
ER -