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At least 91 records · Page 5Linked to original sources
PubMed1975

Abnormal bone development and lameness associated with secondary copper deficiency in young cattle.

Lameness in a group of 5- to 12-month-old calves was found to be clinically, radiographically, and pathologically associated with abnormal bone development of the distal growth plates of the metacarpus and metatarsus. Copper concentrations in serum and liver were low. Serum calcium, phosphorus, and alkaline phosphatase values were normal. In pasture forage samples, sulfate, zinc, and molybdenum concentrations were high, whereas copper, calcium, and phosphorus concentrations were normal. Red blood cell (RBC) counts and hemoglobin values were within normal limits. Radiographic findings included a widened zone of cartilage and lipping of the medial and lateral areas of the physeal plate. Histologic findings included focal widenings of the growth plate consisting of tongues of uncalcified cartilage.

Animal Feed↗
PubMed1987

The Mr 24,000 phosphoprotein from developing bone is the NH2-terminal propeptide of the alpha 1 chain of type I collagen.

Using nondegradative isolation procedures, we have purified and characterized the Mr 24,000 phosphoprotein from developing bovine and human bone where it constitutes 5% of the noncollagenous protein in the mineral compartment. This hydroxyproline-containing protein could not be cleaved by cyanogen bromide. The purified, intact product spontaneously formed a complex consistent with a collagen-like trimer that remained a trimer even in sodium dodecyl sulfate-polyacrylamide gels. The ability to form the complex was lost upon treatment with bacterial collagenase, a treatment that resulted in an NH2-terminally blocked fragment of Mr 17,000. After deblocking, the NH2-terminus of the intact, Mr 24,000 bovine product was shown to have virtually the same amino acid sequence (residues 1-24 with asparagine rather than aspartic acid at position 20 as reported earlier by Horlein et al. (Horlein, D., Fietzek, P. P., Wachter, E., Lapiere, C. M., and Kuhn, K. (1979) Eur. J. Biochem. 90, 31-38) as the amino-terminal segment of dermatosparatic calf skin alpha 1 type I procollagen. Furthermore, pulse-chase studies showed a precursor-product relationship between procollagen and the Mr 24,000 protein. Anti-serum made against the bovine bone protein bound to bands on electrotransfers that were consistent with the positions of both alpha 1(I) procollagen and the procollagen chain missing its COOH-terminal extension peptide (pN-alpha 1(I), as well as the original Mr 24,000 product in extracts of bone, skin, tendon, cornea, and other type I collagen-containing tissues. Fetal calf serum contained an average of 106 micrograms/ml of the Mr 24,000 protein as determined by quantitative enzyme-linked immunosorbent assay. The only serine residue in the bovine bone protein was phosphorylated. It is unknown whether the corresponding collagen NH2-terminal pro-peptides in other tissues and serum are similarly phosphorylated.

Animals↗
PubMed1984

[Influence of nutrition on the bone development of children].

The effect of nutrition on infant bone age was studied. Bone age was examined in children with different degrees of malnutrition using wrist X-Rays and comparing them with Greulich and Pyle Atlas. There were no differences in the socioeconomic level of the different groups. In obese children bone age was advanced, while in under-nourished, it was retarded. The more severe the undernutrition the more delayed the bone age. A positive correlation between the percentage of variation of bone age and chronological age, and percentage of height for age was found. A greater delay in bone age was detected in undernourished children who had been small for date infants.

Age Determination by Skeleton↗
PubMed1991

Characterization of a cDNA for chicken osteopontin: expression during bone development, osteoblast differentiation, and tissue distribution.

The chicken bone phosphoprotein (approximately 66-kDa BPP) is a major noncollagenous component of bone and is the major phosphoprotein synthesized by cultured chicken embryo osteoblasts [Gotoh, Y., Gerstenfeld, L. C., & Glimcher, M. J. (1990) Eur. J. Biochem. 87, 49-58]. A cDNA clone for this protein was isolated from an expression library made from embryonic chicken bone mRNA. The complete primary protein sequence of 264 amino acids was deduced from the cDNA sequence inclusive of a 16 amino acid signal peptide sequence and terminated by 4 in-frame stop sequences. A sequence alignment indicated an approximate 35% overall similarity in protein sequence between the avian approximately 66-kDa BPP and the mammalian protein osteopontin, while at the nucleotide level 60% similarity was observed. Features of this sequence which showed the greatest similarity to mammalian osteopontin included a region in which seven of nine consecutive residues are aspartic acid, a recognition sequence for integrin-mediated cell binding (-Arg-Gly-Asp), and four possible recognition sequences for phosphorylation by casein kinase II. Hybridization analysis indicated a message of 1.5 kb found predominantly in bone and kidney. The mRNA was inducible in phorbol ester treated primary cultures of chondrocytes which show no expression under normal growth conditions. A temporal induction was seen during osteoblastic differentiation both in vivo and in vitro, thus suggesting that regulation of the approximately 66-kDa BPP is under transcriptional control during osteoblast development. In summary, both the protein's primary structure and its biological features suggest that it is the avian homologue to mammalian protein osteopontin.

Amino Acid Sequence↗
PubMedDate not supplied

The role of macrophages in osteoclast neogenesis in vivo: quantitative analysis of osteoclasts and macrophages in endochondral bone development in rats treated with hydrocortisone or calcitonin.

Osteoclasts and macrophages in endochondral bone of rats were analyzed after long-term treatment with hydrocortisone (HC) or elcatonin (ECT). The growth plate-metaphysis junction ( GPMJ ) of the HC-treated bones showed increased numbers of osteoclasts, but the incidence of osteoclast profiles with ruffled borders was low and the cells had fewer nuclei. The number of macrophages in the GPMJ of HC-treated bone did not significantly differ from that in the control. In the metaphyseal trabecular (MT) region macrophages were numerous, but osteoclasts were depleted. Compared to controls the ECT-treated osteoclasts in the GPMJ had an increased number of nuclei per cell, and the incidence of osteoclast profiles with ruffled borders was reduced. There was a small increase in the number of osteoclasts and a large increase in the number of macrophages. The osteoclasts in the MT regions of ECT-treated bones were significantly larger compared to controls. The macrophages did not differ in number from the controls. This investigation supports the proposal that the GPMJ is the principal site of osteoclasts neogenesis. Discrepancies in features of osteoclasts in the GPMJ and MT regions of each treatment group were probably due to a difference in peroid when the osteoclasts were exposed to the drugs.

Animals↗
PubMed1991

Effects of dietary amino acid levels on bone development in broiler chickens.

Studies with several species suggest that dietary protein may influence bone calcification. Six pens of six male broilers in two consecutive trials were fed from 1 to 21 days either .5 or 1.0% Ca in diets with 80, 90, 100, 110, or 120% of the amino acid (AA) standards suggested by Thomas et al. in 1986 at a constant .46% nonphytate P. The BW and feed conversion rate (FCR) were determined, and bone measurements were taken. Both AA and Ca levels influenced BW with an interaction of the two factors. The Ca level, but not AA level, influenced FCR. The lower Ca level inhibited feed intake. Increasing AA levels reduced bone ash but did not affect tibia breaking strength. There was an interaction of AA and Ca on tibia ash, tibia weight, and tibia length. The higher AA levels supported normal linear growth of the tibia but decreased rate of calcification, especially in the diets with .5% Ca. In diets with marginal Ca levels, higher AA levels may reduce bone calcification.

Amino Acids↗
PubMedDate not supplied

[Structural identity of the multinuclear chondro- and osteoclasts in developing bone].

Distributional peculiarities and the ultrastructure of multinuclear elastic cells have been studied in the developed thighbone of rat and rabbit fetuses and new-borns. Multinuclear chondro- and osteoclasts exhibit no noticeable structural specificity with respect to the resorption substrate and are considered to be one and the same type of clastic cells whose main function is to resorb the mineralized tissue.

Animals↗