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Biomedical subjects

A G Brownell

Publications and source records attributed to A G Brownell.

9 recordsLinked to original sources
PubMed1990

Osteogenesis inhibitory protein: a (p)review.

An historical perspective concerning biologically active factors derived from the organic matrix of bone is presented. The emphasis is upon the first discovered of these, bone morphogenetic protein (BMP) and a protein which copurifies with BMP in the initial steps of chemical fractionation. This newly described protein has the biological role of inhibiting the activity of BMP both in vivo and in vitro. Thus it has been named osteogenesis inhibitory protein (OIP). A summary of the known activities of this protein is presented along with preliminary data which indicate the antimitotic nature of OIP.

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PubMed1988

Isolation, partial purification and in vitro characterization of osteogenic inhibitory protein.

A noncollagenous protein has been extracted and partially purified from adult cortical bone. This protein copurifies with another bone matrix protein, bone morphogenetic protein, until treatment with nonionic detergents. Characterization of the biological activity of this new protein has demonstrated it to be a potent osteogenic inhibitor in vitro. The inhibitor antagonizes the chondrogenic activity of devitalized, demineralized bone matrix as well as the activity of soluble bone morphogenetic protein. Bone matrix induced collagen and glycosaminoglycan synthesis are both inhibited in the presence of various concentrations of the osteogenic inhibitory protein. Inhibition of collagen synthesis required the presence of osteogenic inhibitory protein from the initiation of the tissue culture while glycosaminoglycan synthesis could be inhibited at any stage of differentiation. We postulate that this osteogenic inhibitory protein is essential in normal homeostatic bone metabolism, perhaps acting directly on bone morphogenetic protein.

Animals↗
PubMed1977

Cell surface carbohydrates of preimplantation embryos as assessed by lectin binding.

Preimplantation embryos were obtained from the uteri and oviducts of 2 strains of mice, Swiss CD-1 and B6CBA. After removal of the zona pellucida by treatment with pronase, FITC-lectins were bound to the embryonic cell surfaces at either 4 degrees C or 37 degrees C. Both morula and blastocyst stage embryos bound the following lectins, FITC-ConA, FITC-WGA, FITC-RCAII and FITC-RCAI. No difference in binding was observed between the morula stage and the blastocyst stage within each mouse strain for each specific lectin. However B6CBA embryos bound less FITC-ConA and FITC-WGA than the corresponding Swiss CD-1 embryos. The topographical arrangement of the lectin receptors was observed to differ between 4 degrees C and 37 degrees C for FITC-ConA, FITC-RCAII, and FITC-RCAI. While lectins bound at 4 degrees C showed a pattern of continuous labeling, the same lectin at 37 degrees C showed aggregation of lectin receptors into patches indicating lateral mobility of these receptors within the embryonic cell membranes. In contrast FITC-WGA bound at 4 degrees C and 37 degrees C demonstrated continuous labeling of embryos at both temperatures. FITC-fucose binding protein did not bind to Swiss CD-1 embryos. The invasiveness of trophoblastic cells of mouse blastocysts was studied by culturing isolated embryos without prior enzyme treatment on reconstituted collagen gels. After 4 days in BME containing only glutamine and bovine serum albumin as supplements, the embryos shed their zona pellucida and implanted into the collagen gel as indicated by zones of lysis in proximity to the embryonic cells when analyzed by scanning electron microscopy.

Animals↗
PubMed1977

Triple-helix formation on ribosome-bound nascent chains of procollagen: deuterium-hydrogen exchange studies.

Polyribosomes containing nascent [3H]proline-labeled collagen chains were isolated from chick embryo fibroblasts in culture. These nascent chains were nearly completely hydroxylated, as indicated by the presence of [3H]hydroxyproline and high hydroxyproline/proline ratios. The polyribosomes were suspended in D2O at 15 degrees and the infrared spectrum was determined using a reference cell containing collagen-depleted polyribosomes in D2O, matched to equal RNA content. The amide I and amide II bands were observed. When the polyribosomes were heated in D2O at 44 degrees in the infrared cells, the N--D amide II absorbance at 1480 cm-1 increased markedly, indicating that H leads to D exchange had occurred. Collagen-depleted polyribosomes showed no such changes in absorbance at 1450-1480 cm-1 upon heating. Polyribosomes recovered from the infrared cells after treatment at 44 degrees and cooling still contained collagen, as indicated by their [3H]hydroxyproline content. These data indicate that nascent collagen bound to the polyribosomes can assume a hydrogen-bonded structure. Taken with prior data showing that the nascent collagen was also resistant to pepsin digestion, it is suggested that the collagen examined is in triple-helix conformation. Because the nascent polyribosome-bound collagen is nearly fully hydroxylated, it must be considered that triple-helix formation can occur between nascent chains while they are attached to the endoplasmic reticulum surface and that chain association and triple-helix formation in vivo may well occur before rather than after release.

Animals↗
PubMed1976

Intracellular location of triple helix formation of collagen. Enzyme probe studies.

Primary cultures of chick embryo fibroblasts were used to study ribosomal events in the processing of procollagen. Polyribosomes from radiolabeled cells were subjected to enzyme probe analysis using collagenase and pepsin digestion to assess both the amount of procollagen present on the polyribosomes and the conformation of the molecule. The peptides rendered dialyzable by each enzyme treatment were analyzed for radioactive proline and hydroxyproline. Approximately 30% of the nascent proteins were collagenous. Although some hydroxyproline was dialyzable in the pepsin-treated material, a low ratio of hydroxyproline to proline (0.04) indicated that considerable amounts of noncollagenous proteins were digested. Polyribosomal material, previously treated with pepsin, was digested with purified collagenase. Similarly, collagenase-digested polyribosomes were treated with pepsin. The pepsin pretreatment released noncollagenous protein and served to purify the remaining ribosomally bound pepsin-resistant collagenous protein. Collagenase treatment of the pepsin-resistant ribosomally bound peptides released peptides with a hydroxyproline to proline ratio of 0.65, indicating that considerable hydroxylation of proline occurs on nascent ribosomally bound procollagen. This finding combined with the well documented stabilizing effect of hydroxyproline on the collagen triple helix and the demonstrated resistance of ribosomally bound procollagen to pepsin digestion indicates that the collagen triple helix may well form on the polyribosome.

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