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At least 235 records · Page 13Linked to original sources
PubMed1997

Detection of gelatinase B expression reveals osteoclastic bone resorption as a feature of early calvarial bone development.

Gelatinase B is a matrix metalloproteinase (MMP-9) produced by osteoclasts involved in bone resorption. Bone modeling, of which resorption is an integral part, is particularly evident in the intramembranous bones of the craniofacial region. To determine the role of osteoclasts in developing intramembranous bones we localized osteoclasts in calvariae from mice aged between embryonic day 16 and postnatal day 6, using gelatinase B and tartrate-resistant acid phosphatase activity (TRAP) as osteoclast markers. Through a combined approach of in situ hybridization and enzyme histochemistry, phenotypic differences between osteoclasts associated with calvarial bone were noted. Some cells expressed gelatinase B mRNA but were TRAP negative, whereas others demonstrated an overlap in enzyme profile exhibiting both TRAP activity and expressing gelatinase B mRNA. During more advanced development, most osteoclasts exhibited TRAP activity but did not express gelatinase B mRNA. The distribution of these cells differed, TRAP positive cells being detected in a widespread pattern at all ages, while gelatinase B transcripts were increasingly concentrated in areas of new and rapid bone growth, notably around the sutures. We propose the use of gelatinase B as an osteoclastic marker in the developing mouse. We conclude that gelatinase B may have a key role during early bone formation, the regulation of bone modeling, and perhaps in the maintenance of suture width.

Acid Phosphatase↗
PubMed1992

[Effect of vitamin D over-dosage on the tooth and bone development of rabbits].

The paper investigated the changes of rabbit's tooth and jaw tissues by vitamin-D poisoning experiment. The results showed the dentin, periodontium, jaw bone and long bone of rabbit were all changed. X-ray showed subperiosteum absorbation and periosteum reaction. The mineral content of the rabbit's epiphysis and long bone diaphysis in experiment group were lower than that of control group. The histopathological findings were irregular hyperplasia of dentin, arrange disturbance of periodontal fibers, absorbation of the alveolar bone and mal-ossification of long bones. The above changes were more significant during 30-45 days of rabbit poisoning, after 60 days of poisoning the above signs were gradually released.

Animals↗
PubMed1997

A novel G protein-coupled receptor with homology to neuropeptide and chemoattractant receptors expressed during bone development.

A novel G protein-coupled receptor was isolated from a cDNA derived from the cell line NH15-CA2 and a cDNA library from adult mouse brain using a PCR cloning strategy. The amino acid sequence of the candidate receptor DEZ showed homology to neuropeptide and chemoattractant receptors. Highest overall homology was found with the orphan receptor GPR-1 (65%), the angiotensin II receptor (62%), and the C5a anaphylatoxin receptor (60%). Northern blot analysis of dez revealed a predominant 2.6 kb mRNA species in NH15-CA2 cells. In situ hybridization experiments showed that dez is differentially regulated during development, with a prominent expression in developing osseous and cartilaginous tissue. It was also detectable in the adult parathyroid glands, hinting at a possible function in bone metabolism.

Amino Acid Sequence↗
PubMed2005

Bone development: interaction of molecular components and biophysical forces.

A deeper understanding of skeletal development comes from knowledge of the molecular components, cell and tissue structure, and biophysical and vascular mechanisms underlying physiologic function. Endochondral and intramembranous bone formation mechanisms are active during long bone synthesis. Most endochondral growth in length occurs at the physes by the coordinated actions of cell proliferation, matrix synthesis, and chondrocyte hypertrophy. Several intrinsic molecules act to modulate physeal structure and function whereas extrinsic molecules, such as hormones, provide systemic regulation of growth. Biophysical forces develop intrinsically within the growing bone, serving to enlarge it in three dimensions, while extrinsic forces resist and channel expansion into normal recognizable and functional forms. Newer imaging modalities, such as magnetic resonance imaging, are highly effective in assessing epiphyseal vascularity and differentiating fibrous, cartilaginous, mineralized and osseous tissues in prenatal and postnatal developing bone. This study illustrates the interplay between the molecular and biophysical aspects of normal bone growth, shows ways in which altered development leads to abnormal structures, and provides examples where biologic and biophysical interventions can affect bone development in favorable ways.

Biomechanical Phenomena↗
PubMed1983

Matrix sialoprotein of developing bone.

Using nondegradative isolation procedures, we purified and characterized a glycoprotein from fetal calf bone that is rich in sialic acid. This bone sialoprotein (BSP) has an apparent Mr = 70,000-80,000 and stains with Alcian blue and Stains All on sodium dodecyl sulfate gels but does not stain with Coomassie blue without prior treatment with neuraminidase. This glycoprotein contains 50% protein, 12% sialic acid, 7% glucosamine, and 6% galactosamine. Fetal calf BSP is rich in glutamate (19%), aspartate (15.4%), and glycine (11.8%) but, in contrast to osteonectin and the bone proteoglycan, has relatively low amounts of leucine (4.3%). Antisera raised against fetal calf BSP localized the glycoprotein by indirect immunofluorescence to developing bone trabeculae with an overall tissue distribution identical with that of osteonectin. On competition enzyme-linked immunosorbent assay analysis, BSP was 11.5% (+/-2.4%, S.E.) of mineral-bound (guanidine-EDTA-soluble) calf bone protein. Immunoreplicas (Western blots) of calf bone extracts suggest that more than 95% of the antigenicity resided in the Mr = 70,000-80,000 region with the remaining cross-reactivity in Alcian blue positive, Mr = approximately 20,000 and approximately 30,000 bands. Brief treatment of the Mr = 70,000-80,000 species with trypsin produced lower molecular weight, Alcian blue-staining products of similar size. No BSP was detected in guanidine extracts of various soft or unmineralized connective tissues, but dentin contained small amounts (0.4%) of the protein. Rat and fetal human bone were also observed to contain a sialoprotein with similar properties and a certain degree of cross-reactivity with the bovine BSP.

Amino Acids↗
PubMed1996

Haploinsufficiency of parathyroid hormone-related peptide (PTHrP) results in abnormal postnatal bone development.

Although apparently phenotypically normal at birth, mice heterozygous for inactivation of the gene encoding parathyroid hormone-related peptide (PTHrP) develop haplotype insufficiency by 3 months of age. In addition to histologic and morphologic abnormalities similar to those seen in homozygous mutants, heterozygous animals demonstrated alterations in trabecular bone and bone marrow. These included metaphyseal bone spicules which were diminished in volume, irregularly distributed, and less well developed than those seen in age-matched controls as well as bone marrow, which contained an inordinate number of adipocytes. A substantial reduction in PTHrP mRNA was detected in heterozygous tissue, while circulating parathyroid hormone (PTH) and calcium concentrations were normal. Thus, while a physiologic concentration of PTH was capable of maintaining calcium homeostasis, it was incapable of compensating for PTHrP haploinsufficiency in developing bone. In normal animals, both PTHrP and the PTH/PTHrP receptor were expressed predominantly in chondrocytes situated throughout the proliferative zone of the tibial growth plate. In the metaphysis, the PTH/PTHrP receptor was identified on osteoblasts and preosteoblastic cells situated in the bone marrow, while PTHrP was expressed only by osteoblasts. These observations indicate that postnatal bone development involves susceptible pathways that display exquisite sensitivity to critical levels of PTHrP and imply that the skeletal effects of PTH are influenced by locally produced PTHrP. Moreover, identification of both the ligand and its N-terminal receptor in metaphyseal osteoblasts and their progenitors suggests an autocrine/paracrine role for the protein in osteoblast differentiation and/or function. Impairment in this function as a consequence of PTHrP haploinsufficiency may critically influence the course of bone formation, resulting in altered trabecular architecture and perhaps low bone mass and increased bone fragility.

Age Factors↗
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↗
PubMed2005

Expression of voltage sensitive calcium channel (VSCC) L-type Cav1.2 (alpha1C) and T-type Cav3.2 (alpha1H) subunits during mouse bone development.

Voltage-sensitive calcium channels (VSCCs) are key regulators of osteoblast plasma membrane Ca(2+) permeability and are under control of calcitropic hormones. Subtype specific antibodies were used to probe L-type Ca(v)1.2 (alpha(1C)) and T-type Ca(v)3.2 (alpha(1H)) subunit expression during mouse skeletal development. Commencing from E14.5 and continuing through skeletal maturity, immunoreactivity of Ca(v)1.2 (alpha(1C)) subunits was evident in regions of rapid long bone growth, including the perichondrium, periosteum, chondro-osseous junction and trabecular bones. Ca(v)3.2 (alpha(1H)) subunits appeared simultaneously and followed a similar distribution pattern. Both subunits were observed in osteoblasts and chondrocytes under high magnification. Interestingly, Ca(v)3.2 (alpha(1H)) subunits were present, but Ca(v)1.2 (alpha(1C)) subunits were absent from osteocytes. Western Blot and immunohistochemical assessment of in vitro cell culture models of osteogenesis and chondrogenesis confirmed the in vivo observations. We conclude that both L-type Ca(v)1.2 (alpha(1C)) and T-type Ca(v)3.2 (alpha(1H)) VSCCs are dynamically regulated in bones and cartilages during endochondral bone development.

Animals↗
PubMed2004

Nutrition influences bone development from infancy through toddler years.

During the last decade a greater appreciation has developed for determining factors that influence bone accretion in healthy children. Nutritional factors that may contribute to bone accretion in infants and toddlers include maternal nutritional status during pregnancy, type of infant feeding, calcium and phosphorus content of infant formula, introduction of weaning foods, and diet during the toddler and preschool years. Maternal vitamin D deficiency during pregnancy is associated with disturbances in neonatal calcium homeostasis, and maternal calcium deficiency leads to reduced neonatal bone mineral content (BMC). Preterm infants are at increased risk of osteopenia, and, although the use of high mineral formula has reduced the risk of osteopenia in these infants, it has not eliminated it. The reason for the long-term bone deficiency among preterm infants is not clear, although lower physical activity levels have been suggested as a potential cause. Studies find that human milk-fed infants have lower bone accretion than do formula-fed infants; that the greater the mineral content of formula, the greater the bone accretion; and that the inclusion of palm olein oil in infant formula may reduce bone mineral accretion. Bone accretion is not influenced by the timing of the introduction of weaning foods, despite higher serum parathyroid hormone (PTH) concentrations among infants who receive solids earlier. There is evidence of calcium intake-by-gene and calcium intake-by-physical activity interactions among toddlers and young children. The long-term effects of these early nutritional influences on later bone health are unknown.

Bone Development↗
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↗