4 results match your criteria: "The University of Melbourne and St. Vincent's Institute of Medical Research[Affiliation]"
Bone
November 1999
Department of Medicine, The University of Melbourne and St. Vincent's Institute of Medical Research, St. Vincent's Hospital, Fitzroy, Victoria, Australia.
RANKL (receptor activator of NFkappaB ligand) is a membrane-associated osteoblastic molecule, and along with macrophage-colony-stimulating factor, is crucial for osteoclast formation. RANKL is known to be strongly expressed in osteoblasts and lymphoid tissues. We have sought to determine the skeletal and extraskeletal sites of production of RANKL mRNA and protein using the techniques of in situ hybridization and immunohistochemistry.
View Article and Find Full Text PDFBiochem J
December 1998
Department of Medicine, The University of Melbourne and St. Vincent's Institute of Medical Research, 41 Victoria Parade, Fitzroy, Victoria, Australia, 3065.
The mammalian Ca2+-dependent serine protease prohormone convertase PC8 is expressed ubiquitously, being transcribed as 3.5, 4.3 and 6.
View Article and Find Full Text PDFJ Cell Physiol
July 1998
Department of Medicine, The University of Melbourne and St. Vincent's Institute of Medical Research, St. Vincent's Hospital, Fitzroy, Victoria, Australia.
This study examines the relative importance of transcriptional and posttranscriptional actions of retinoic acid (RA) in the regulation of osteopontin gene expression in a rat clonal preosteoblastic cell line, UMR 201. Nuclear run-on analysis demonstrated constitutive expression of the osteopontin gene which was increased by threefold after 4 hr treatment with 1 microM RA, returning to a basal level by 24 hr. However, Northern blot analysis, performed concurrently, showed that RA progressively increased the steady-state osteopontin mRNA level beginning 2 hr before any increase in gene transcription and peaking at 24 hr.
View Article and Find Full Text PDFBone
March 1998
Department of Medicine, The University of Melbourne and St. Vincent's Institute of Medical Research, St. Vincent's Hospital, Fitzroy, Victoria, Australia.
Using immunohistology with two specific antisera raised against N-terminal parathyroid hormone-related protein (PTHrP) and in situ hybridization (riboprobe to common coding exon), evidence is provided for the expression of PTHrP by mouse, rabbit, and human osteoclasts derived from several in vitro and in vivo sources. In cocultures of mouse bone marrow and calvarial cells treated with 1,25-dihydroxyvitamin D3, the generated osteoclasts expressed both PTHrP messenger RNA (mRNA) and protein. In addition, PTHrP was detected in the majority of actively resorbing osteoclasts in sections of newborn and adult mouse long bones.
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