4 results match your criteria: "The University of Melbourne and St. Vincent's Institute of Medical Research[Affiliation]"

Localization of RANKL (receptor activator of NF kappa B ligand) mRNA and protein in skeletal and extraskeletal tissues.

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.

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The mammalian Ca2+-dependent serine protease prohormone convertase PC8 is expressed ubiquitously, being transcribed as 3.5, 4.3 and 6.

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Transcriptional and posttranscriptional regulation of osteopontin gene expression in preosteoblasts by retinoic acid.

J 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.

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Localization of parathyroid hormone-related protein in osteoclasts by in situ hybridization and immunohistochemistry.

Bone

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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