Identification of small collagenous proteins with properties of procollagen alpha 1 (I) pN-propeptide in fetal porcine calvarial bone.
Several small collagenous apatite binding (SCAB) proteins have been extracted from the mineralized matrix of fetal porcine calvarial bone. One protein (SCAB 3), released on demineralization of bone with 0.5 M EDTA, appears to represent the alpha 1 pN-propeptide that is normally released during proteolytic processing of type I procollagen. The 28 Kd protein, which stains blue with "Stains-all", is reduced to a 19 Kd fragment by bacterial collagenase digestion, but is not susceptible to cyanogen bromide. The amino acid composition, blocked amino-terminus and immunological properties are all consistent with properties of alpha 1 (I) pN-propeptide. Fractionation on hydroxylapatite in the presence of urea has revealed a nonbinding (SCAB 3a) and a binding (SCAB 3b) form. Extraction of the demineralized matrix of bone with 4 M GuHCl revealed a third form (G2-28) which was similar to SCAB 3a on hydroxylapatite chromatography but showed differences on FPLC "Mono Q" resin. The occurrence of these different forms of pN-propeptide in bone may be of significance in collagen fibril-associated hydroxylapatite formation and in the regulation of osteoblastic function during bone resorption.
Goldberg
H A
HA
Medical Research Council Group in Periodontal Physiology, University of Toronto, Ontario, Canada.
Maeno
M
M
Domenicucci
C
C
Qi
Z N
ZN
Sodek
J
J
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001842:Bone and Bones / Q000032:analysis* / Q000196:embryology; D003094:Collagen / Q000032:analysis*; D005326:Fetal Proteins / Q000032:analysis; D011347:Procollagen / Q000032:analysis*; D013552:Swine
D000596:Amino Acids; D005326:Fetal Proteins; D011347:Procollagen; D003094:Collagen