Distribution of lipids associated with mineralization in the bovine epiphyseal growth plate

Boskey, Adele L.; Posner, Aaron S.; Lane, Joseph M.; Goldberg, Mark R.; Cordella, D.M.

doi:10.1016/0003-9861(80)90285-4

Cited by 48 publications

(15 citation statements)

References 31 publications

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“…The results of this study support previous observations [7,17] that there are zonal differences in the lipid composition of epiphyseal cartilage which can Proteolipid or phospholipid extracted from upper or lower growth centers was incubated in bicarbonate buffered metastable calcium phosphate solution for 5 days at 37~ After centrifugation, pellets were washed with deionized water, lyophilized, and subjected to wide-angle X-ray diffraction. Values indicate the number of samples showing the presence of hydroxyapatite as a fraction of the total samples analyzed.…”

Section: Discussionsupporting

confidence: 89%

Proteolipid-lipid relationships in normal and vitamin D-deficient chick cartilage

Boyan

Ritter

1984

Calcif Tissue Int

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Previous studies have shown that in vitro calcification of chick epiphyseal cartilage matrix vesicles is proteolipid-dependent. The purpose of this research is to examine the role of proteolipid in cartilage calcification in vivo by comparing the proteolipid concentration of normal and vitamin D-deficient chick epiphyseal cartilage, the relationship of proteolipid to other tissue lipids, and its ability to support in vitro apatite formation. Proteolipid was isolated from the upper growth centers (reserve cell zone, upper proliferative zone) and lower growth centers (lower proliferative, hypertrophic, and calcified cartilage zones) of long-bone epiphyses from 3-week-old normal and rachitic male white leghorn chicks by Sephadex LH-20 chromatography of the crude phospholipid component of the total lipid extract. In both normal and rachitic tissue the proteolipid/dry weight and proteolipid/total lipid ratios were greater in the lower growth center than in the upper zones. No statistically significant change in the proteolipid/total lipid ratio in rachitic tissues relative to comparable cell zones in normal cartilages was observed. However, there was an increase in the nonproteolipid phospholipid content of rachitic tissues, altering the relative proteolipid/phospholipid composition. Whereas proteolipids from normal tissue supported in vitro calcification, proteolipids from rachitic tissues did not, indicating a direct effect of vitamin D on proteolipid structure. These data support the hypothesis that failure of rachitic cartilage to calcify in vivo may be due in part to alterations in phospholipid and proteolipid metabolism.

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Section: Discussionsupporting

confidence: 89%

Proteolipid-lipid relationships in normal and vitamin D-deficient chick cartilage

Boyan

Ritter

1984

Calcif Tissue Int

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“…That they may have a function is indicated by recent studies by Sarig et al (50), who suggest that cholesterol plays a role in pathological mineralization. Previous reports (23)(24)(25)(26)(27) had noted that the acidic phospholipids interact and form complexes with the initial mineral phase, yet data presented here indicate that these lipids can be removed by detergent extraction. Since the NC was shown to be rich in calcium and phosphate, we assessed its nature by direct analysis of various native MV preparations (i.e.…”

Section: Discussionmentioning

confidence: 45%

“…Varying proportions of the predominant lipid associated with the mineral, PS, are complexed with Ca 2ϩ and P i (22)(23)(24). These Ca 2ϩ -PS-P i complexes (CPLX) are present in bone, cartilage, and other mineralized tissues (25) and are especially enriched in MV (26). In vitro experiments have shown that both CPLX and ACP, when incubated in synthetic lymphs, can lead to formation of HAP (18,27,28).…”

Section: ؉mentioning

confidence: 99%

Physicochemical Characterization of the Nucleational Core of Matrix Vesicles

Genge

Dunkelberger

et al. 1997

Journal of Biological Chemistry

139

154

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While previous studies revealed that matrix vesicles (MV) contain a nucleational core (NC) that converts to apatite when incubated with synthetic cartilage lymph, the initial mineral phase present in MV is not well characterized. This study explored the physicochemical nature of this Ca 2؉ and P i -rich NC. MV, isolated from growth plate cartilage, were analyzed directly by solidstate 31 P NMR, or incubated with hydrazine or NaOCl to remove organic constituents. Other samples of MV were subjected to sequential treatments with enzymes, salt solutions, and detergents to expose the NC. We examined the NC using transmission electron microscopy, energy-dispersive analysis with x-rays, and electron and x-ray diffraction, Fourier transform-infrared spectroscopy, high performance thin-layer chromatographic analysis, and SDS-polyacrylamide gel electrophoresis. We found that most of the MV proteins and lipids could be removed without destroying the NC; however, NaOCl treatment annihilated its activity. SDS-polyacrylamide gel electrophoresis showed that annexin V, a phosphatidylserine (PS)-dependent Ca 2؉ -binding protein, was the major protein in the NC; high performance thin-layer chromatographic analysis revealed that the detergents removed the majority of the polar lipids, but left significant free cholesterol and fatty acids, and small but critical amounts of PS. Transmission electron microscopy showed that the NC was composed of clusters of ϳ1.0 nm subunits, which energy-dispersive analysis with x-rays revealed contained Ca and P i with a Ca/P ratio of 1.06 ؎ 0.01. Electron diffraction, x-ray diffraction, and Fourier transform-infrared analysis all indicated that the NC was noncrystalline.

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“…This hypothesis is based both on the distribution of these complexes in mineralizing tissues [3][4][5][6][7] and on their behavior in vitro [8][9]. They are increased in concentration in actively mineralizing tissues, specifically in the region of the lower half of the bovine epiphyseal growth plate [6], in the area adjacent to the calcification front in human articular cartilage [7], and in healing fracture callus during the chondroid-osteoid stage [5]. In vitro, Ca-PL-PO4 complexes isolated from these tissues cause hydroxyapatite deposition in metastable calcium phosphate solutions [8].…”

mentioning

confidence: 99%

Changes in lipids during matrix: Induced endochondral bone formation

Boskey

Reddi

1983

Calcif Tissue Int

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The changes in lipids occurring during the process of endochondral ossification have been characterized by studying the discrete phases of matrix-induced endochondral bone formation in the rat. Calcium-acidic phospholipid-phosphate complexes were shown to increase in concentration during cartilage calcification (day 9) and to peak in content during early bone formation (days 11-13), the times during which the rate of mineral deposition, as indicated by the change in ash weight was greatest. These data support the hypothesis that the calcium-acidic phospholipid-phosphate complexes play a role in the in vivo initiation of hydroxyapatite deposition. The overall lipid composition of the induced matrix newly formed cartilage (days 7-9) was comparable to that of normal cartilage, with the phospholipid composition matching that of chondrocyte plasma membranes. Times of vascular invasion and formation of marrow cavities were marked by elevated total lipid and triglyceride contents.

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Distribution of lipids associated with mineralization in the bovine epiphyseal growth plate

Cited by 48 publications

References 31 publications

Proteolipid-lipid relationships in normal and vitamin D-deficient chick cartilage

Proteolipid-lipid relationships in normal and vitamin D-deficient chick cartilage

Physicochemical Characterization of the Nucleational Core of Matrix Vesicles

Changes in lipids during matrix: Induced endochondral bone formation

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