Thrombospondin‐4 is expressed by early osteogenic tissues in the chick embryo

Tucker, Richard P.; Adams, Josephine C.; Lawler, Jack

doi:10.1002/aja.1002030410

Cited by 57 publications

(43 citation statements)

References 52 publications

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“…2E). Thus, unlike TSP-2 and TSP-4 (Tucker, 1993;Tucker et al, 1995), transcripts encoding TSP-1 and TSP-3 are relatively abundant in the early avian embryo and their expression correlates with early neural differentiation and neurite outgrowth, respectively. …”

Section: In Situ Localization Of Tsp-1 and Tsp-3 Mrnas In The E2 And mentioning

confidence: 99%

“…Accordingly, the thrombospondin literature has many contradictory reports of thrombospondin immunolocalization. For this reason, in situ hybridization has proven to be a useful method for studying patterns of thrombospondin gene expression and determining the potential sites of action for these molecules during development (Iruela-Arispe et al, 1993;Tucker, 1993;Qabar, 1994;Tucker et al, 1995). Here we describe two novel partial-length cDNAs to chicken TSP-1 and TSP-3.…”

Section: Introductionmentioning

confidence: 99%

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In situ localization of thrombospondin-1 and thrombospondin-3 transcripts in the avian embryo

et al. 1997

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Two novel cDNA probes to chicken thrombospondin‐1 (TSP‐1) and TSP‐3 were used to determine by in situ hybridization the origins of these extracellular matrix proteins during embryogenesis. Both TSP‐1 and TSP‐3 are expressed in embryonic cartilage. TSP‐1 expression is limited to early chondrocytes, in contrast to TSP‐3 mRNAs that are found in older proliferative and hypertrophic chondrocytes. TSP‐1 and TSP‐3 are expressed consecutively during neurogenesis as well, with the TSP‐1 probe hybridizing in proliferating neuroblasts, and TSP‐3 expressed by neurons as they are actively extending processes. A TSP‐1 hybridization signal reappears in subpopulations of neurons in the spinal cord and brain after the periods of active neurite extension and programmed cell death are complete. TSP‐1 is also expressed in the spinal cord floor plate, in mesenchyme surrounding the developing paramesonephric duct, at the tips of growing lung bronchioles, in lens, and in corneal endothelium. These observations indicate that there is little overlap in the expression patterns of TSP‐1 and TSP‐3 and that they are expressed consecutively during the development of cartilage and neurons. The pattern of TSP‐1 expression in avascular tissues and in the floor plate is consistent with possible roles for this glycoprotein in regulating angiogenesis and establishing morphogenetic gradients. Dev. Dyn. 208:326–337, 1997. © 1997 Wiley‐Liss, Inc.

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Section: In Situ Localization Of Tsp-1 and Tsp-3 Mrnas In The E2 And mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

In situ localization of thrombospondin-1 and thrombospondin-3 transcripts in the avian embryo

et al. 1997

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“…The family can be divided into two branches on the basis of structural considerations. TSP1 and TSP2 are homotrimers composed of monomer chains of ‫000,541ف‬ kD, whereas TSP3-5 are homopentamers with chains of lower molecular weight, because they lack several of the domains present in TSP1 and 2 (Bornstein and Sage 1994;Adams 1995). Virtually nothing is known of the functions of TSP3-5, except that mutations in the gene encoding TSP5/ COMP have been identified in some patients with either pseudoachondroplasia or multiple epiphyseal dysplasia (Briggs et al 1995;Hecht et al 1995).…”

mentioning

confidence: 99%

“…TSP2 was the second member of the TSP family to be identified (Bornstein et al 1991;Laherty et al 1992). Although studies of its expression during murine and avian development have been performed at the mRNA level (Laherty et al 1992;Iruela-Arispe et al 1993;Tucker 1993;Tucker et al 1995), the difficulty in obtaining the protein in pure form and in substantial quantities has hindered immunocytochemical and functional studies.…”

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confidence: 99%

The Distribution of the Matricellular Protein Thrombospondin 2 in Tissues of Embryonic and Adult Mice

Kyriakides

Zhu

Yang

et al. 1998

J Histochem Cytochem.

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SUMMARYMice that lack the matricellular protein thrombospondin 2 (TSP2) develop a pleiotropic phenotype characterized by morphological changes in connective tissues, an increase in vascular density, and a propensity for bleeding. Furthermore, dermal cells derived from TSP2-null mice display adhesion defects, a finding that implicates TSP2 in cell-matrix interactions. To gain a better understanding of the participation of TSP2 in the development and maturation of the mouse, we examined its distribution in embryonic and adult tissues. Special attention was paid to the presence of TSP2 in collagen fibers, because collagen fibrils in the TSP2-null mouse appear to be irregular in size and contour by electron microscopy. Immunohistochemical analysis of Day 15 and Day 18 embryos revealed TSP2 in areas of chondrogenesis, osteogenesis, and vasculogenesis, and in dermal and other connective tissue-forming cells. Distinctly different patterns of deposition of TSP2 were observed in areas of developing cartilage and bone at Days 15 and 18 of embryonic development. A survey of adult tissues revealed TSP2 in dermal fibroblasts, articular chondrocytes, Purkinje cells in the cerebellum, Leidig cells in the testis, and in the adrenal cortex. Dermal fibroblasts were also shown to synthesize TSP2 in vitro. The distribution of TSP2 during development is in keeping with its participation in the formation of a variety of connective tissues. In adult tissues, TSP2 is located in the pericellular environment, where it can potentially influence the cell-matrix interactions associated with cell movement and tissue repair. (J Histochem Cytochem 46:1007-1015, 1998)

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“…51 27 THBS4 Thrombospondin-4 ↓ TSP4 transcript first appears in the mesenchyme surrounding bone anlage coinciding with the initial stages of osteogenesis. 52 28 CTSG Cathepsin G ↑ Cathepsin G activity at the tumor-bone interface plays an important role in mammary tumor-induced osteolysis. 53 …”

Section: Thbs2mentioning

confidence: 99%

Differential proteomic analysis of a human breast tumor and its matched bone metastasis identifies cell membrane and extracellular proteins associated with bone metastasis

et al. 2012

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The classical fate of metastasizing breast cancer cells is to seed and form secondary colonies in bones. The molecules closely associated with these processes are predominantly present at the cell surface and in the extracellular space, establishing the first contacts with the target tissue. In this study, we had the rare opportunity to analyze a bone metastatic lesion and its corresponding breast primary tumor obtained simultaneously from the same patient. Using mass spectrometry, we undertook a proteomic study on cell surface and extracellular proteinenriched material. We provide a repertoire of significantly modulated proteins, some with yet unknown roles in the bone metastatic process as well as proteins notably involved in cancer cell invasiveness and in bone metabolism. The comparison of these clinical data with those previously obtained using a human osteotropic breast cancer cell line highlighted an overlapping group of proteins. Certain differentially expressed proteins are validated in the present study using immunohistochemistry on a retrospective collection of breast tumors and matched bone metastases. Our exclusive set of selected proteins supports the set-up of further investigations on both clinical samples and experimental bone metastasis models that will help to reveal the finely coordinated expression of proteins that favor the development of metastases in the bone microenvironment.

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Thrombospondin‐4 is expressed by early osteogenic tissues in the chick embryo

Cited by 57 publications

References 52 publications

In situ localization of thrombospondin-1 and thrombospondin-3 transcripts in the avian embryo

In situ localization of thrombospondin-1 and thrombospondin-3 transcripts in the avian embryo

The Distribution of the Matricellular Protein Thrombospondin 2 in Tissues of Embryonic and Adult Mice

Differential proteomic analysis of a human breast tumor and its matched bone metastasis identifies cell membrane and extracellular proteins associated with bone metastasis

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