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Biomedical subjects

S W Olson

Publications and source records attributed to S W Olson.

17 recordsLinked to original sources

Isolation of human tumor cells that produce cementum proteins in culture.

We have cultured cells from explants of a human cementum tumor. The cells obtained were multipolar, they formed network-like structures and they were alkaline-phosphatase positive. Immunostaining and Western blots using specific antibodies revealed that these cells produced bone sialoprotein and collagen types I and V, and they also mineralized in vitro. Conditioned medium was mitogenic to fibroblasts and mitogens present were separated by heparin-affinity chromatography. Based on affinity to heparin and antibody-inhibition studies, the heparin fractions were shown to contain cementum-derived growth factor, platelet-derived growth factor and fibroblast growth factors. The cementum tumor cells, but not gingival fibroblasts, were stained positively by an antibody to cementum-derived attachment protein. The attachment protein was separated by immunoaffinity chromatography, and Western blots revealed that the preparation contained 56-kDa and 43-kDa proteins as major bands. Cells pulse-labeled with radioactive amino acids contained a 43-kDa protein as the major component; however, this protein was absent after a cold chase in the presence of cycloheximide, but 56-kDa, 39-kDa and 26-kDa species became prominent. These data indicated that the 56-kDa cementum attachment protein is derived from a 43-kDa precursor. Our data show that the cells cultured from the cementum tumor represent cementum cells capable of synthesizing and secreting cementum proteins in culture.

Alkaline Phosphatase↗

Production of a monoclonal antibody to an attachment protein derived from human cementum.

Cementum is the mineralized structure that covers the surface of the roots of teeth; it serves as the attachment site for collagen fibers of adjacent soft connective tissues. Very little is known about how cementum formation is regulated or how it affects other periodontal structures. We have raised a monoclonal antibody that may aid in studies to determine the biology and function of cementum. Mice were immunized with a 55-kDa attachment protein partially purified from human cementum and a monoclonal antibody, H166, was produced. Incubation of tissue sections with this antibody and fluorescein isothiocyanate-conjugated secondary antibody revealed that it immunostains cementum but not dentin, gingiva, or periodontal ligament. Alveolar bone did not bind the antibody, although a few paravascular cells were positive. Long bones, kidney, liver, skin, and several other tissues were negative. Protein fractions separated from cementum extracts by binding to immobilized H166 column contained 55-, 49-, 39-, 29- to 31-, and 23- to 26-kDa components that cross-reacted with the antibody in Western blots; these components were previously shown to be derived from a common precursor. We conclude that the antibody recognizes a group of proteins related to 55-kDa attachment protein in cementum. Our data show that the antibody could serve as a marker for cementum.

Animals↗

Combined-degree programs: a valuable alternative for motivated students who choose medicine early.

The author reviews the history and philosophy of combined-degree programs and summarizes research on the performances of students in these programs. He notes that about one-fifth of U.S. medical schools offer programs that integrate premedical and medical school studies and lead to the award of both an undergraduate and an M.D. degree in six to eight years. The students in these programs perform as well as students electing traditional programs, if not better. The author concludes that university-affiliated medical schools might well consider establishing combined-degree programs as a means of (1) achieving better integration of the premedical and medical curricula and (2) allowing greater access to combined-degree programs for students mature enough early on to select careers in medicine.

Achievement↗

Time Course of mRNA Induction Elicited by Salt Stress in the Common Ice Plant (Mesembryanthemum crystallinum).

In the facultative halophyte Mesembryanthemum crystallinum (common ice plant), irrigation with solutions containing NaCl induces an alternate mode of carbon dioxide fixation, Crassulacean acid metabolism (CAM). The salt stress protocol which we have established facilitates the study of CAM induction and the correlation of changes in metabolism and gene expression. We have studied the time course of mRNA induction for phosphoenolpyruvate carboxylase (PEPCase) (gene: ppc) and several other enzymes of carbon metabolism during stress. While CAM is not fully established for at least 10 days after the start of stress, mRNA amounts for PEPCase and for other CAM enzymes, such as Pyruvate orthophosphate dikinase, increase between day 2 and 3 after stress induction. Increases continue for at least 5 days. Concomitant with the increase of CAM transcripts, fluctuations in the mRNA amounts for genes rbcS and cab were observed. Transcript levels for these proteins decreased several-fold during a 3 to 4 day period.

Journal Article↗

Salt Stress Increases the Level of Translatable mRNA for Phosphoenolpyruvate Carboxylase in Mesembryanthemum crystallinum.

Mesembryanthemum crystallinum responds to salt stress by switching from C(3) photosynthesis to Crassulacean acid metabolism (CAM). During this transition the activity of phosphoenolpyruvate carboxylase (PEPCase) increases in soluble protein extracts from leaf tissue. We monitored CAM induction in plants irrigated with 0.5 molar NaCl for 5 days during the fourth, fifth, and sixth week after germination. Our results indicate that the age of the plant influenced the response to salt stress. There was no increase in PEPCase protein or PEPCase enzyme activity when plants were irrigated with 0.5 molar NaCl during the fourth and fifth week after germination. However, PEPCase activity increased within 2 to 3 days when plants were salt stressed during the sixth week after germination. Immunoblot analysis with anti-PEPCase antibodies showed that PEPCase synthesis was induced in both expanded leaves and in newly developing axillary shoot tissue. The increase in PEPCase protein was paralleled by an increase in PEPCase mRNA as assayed by immunoprecipitation of PEPCase from the in vitro translation products of RNA from salt-stressed plants. These results demonstrate that salinity increased the level of PEPCase in leaf and shoot tissue via a stress-induced increase in the steady-state level of translatable mRNA for this enzyme.

Journal Article↗