FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2040907586> ?p ?o ?g. }

• W2040907586 endingPage "154" @default.
• W2040907586 startingPage "152" @default.
• W2040907586 abstract "Thrombospondins (TSPs) belong to a family of five, secreted, modular glycoproteins encoded by separate genes (Adams and Lawler, 2004, 2011). Group A TSPs (TSP1 and TSP2) are homotrimers, whereas group B TSPs (TSP3, -4, and -5/COMP) are homopentamers (Adams, 2001), and all are secreted as disulfide-bonded complexes. Although the five members of the TSP family differ with respect to structure, cell type, and temporal expression, all TSPs bind to components of the extracellular matrix as well as to a number of cell surface receptors, enabling TSPs to modulate cellular behaviors in a wide array of tissue contexts. TSPs are the prototype of the matricellular protein (Bornstein, 1995) and have been the subject of intense study for four decades.First identified in 1971 as protein released from thrombin-stimulated platelets, TSP1 (thrombin sensitive protein) was initially studied for its role in platelet aggregation and related hemostatic functions (Baenziger et al., 1971; Gartner and Dockter, 1984; Lahav et al., 1982; Lawler et al., 1978; Phillips et al., 1980). The eponym thrombospondin was proposed by Lawler and co-workers (Lawler et al., 1978) who isolated intact thrombospondin complexes from thrombin-treated platelets in physiological saline. Thrombospondin is a filamentous glycoprotein ~70 nm long and binds to heparin-affinity columns, and thus, to heparan sulfate proteoglycans in vivo (Fig. 1). Over the next two decades, it was discovered that TSP1 is synthesized and secreted by endothelial cells as well as other cell types in culture (Asch et al., 1986; Jaffe et al., 1982; Jaffe et al., 1985; Jaffe et al., 1983; McPherson et al., 1981; Mosher et al., 1982; Raugi and Lovett, 1987). The expression of TSP1 by diverse cell types, identification of interacting proteins, and the subsequent recognition that TSP1 binds to specific cell surface molecules in a saturable manner (Asch et al., 1987; McKeown-Longo et al., 1984; Murphy-Ullrich and Mosher, 1987; Roberts et al., 1985; Silverstein et al., 1984) provided the first evidence that TSPs might regulate cell behavior through direct interactions with cell surface receptors to activate intracellular signaling pathways: these first known receptors turned out to be CD36 (GP88) and heparan sulfate proteolgycans (syndecans) and established precedents for identification of other TSP receptors (Asch et al., 1987; Asch et al., 1992; Chung et al., 1999; Godyna et al., 1995; Goicoechea et al., 2000; Lawler and Hynes, 1989; Lawler et al., 1988; Murphy-Ullrich et al., 1988; Sun et al., 1989; Tuszynski et al., 1993; Wang and Frazier, 1998). Subsequent work showed that TSP1 expression is regulated by growth factors (PDGF, TGF-β), that TSP1 can enhance cellular responses to growth factors such as EGF, antagonize VEGF signaling, or variably regulate FGF family signaling (Gupta et al., 1999; Iruela-Arispe et al., 1999; Majack et al., 1985, 1986; Orr et al., 2003; Penttinen et al., 1988; Taraboletti et al., 1992). Elegant biochemistry, protein structural studies, and cloning and sequencing of the TSP1 gene further elucidated relationships between discrete modular domains of TSPs and specific cellular functions as well as regulators of gene expression (Bornstein et al., 1990; Dixit et al., 1986; Frazier et al., 1987; Lawler, 1986; Slane et al., 1988; Sun and Mosher, 1991). Together these early findings stimulated many diverse and fruitful avenues of investigation which have yielded surprising insights into the diverse functions of this remarkable family of proteins.Fig. 1Model of TSP1 monomer showing the N-terminal laminin G-like domain, the oligomerization region of interchain disulfide bonding, the procolllagen-like, von Willebrand factor_C module, the properdin-like type 1 (TSR) repeats, the EGF-like repeats, and the ...This thematic series of interrelated mini-reviews will focus on recent additions to the armamentarium of TSP functions.The review by Mosher and Adams (2012, this issue) employs both evolutionary and structural perspectives to discern the functions of thrombospondins as well as other matricellular proteins, especially in the context of the complex network of intermolecular interactions occurring in the extracellular matrix and at the cell surface.The review by Roberts and co-workers (2012, this issue) highlights the role of TSP1 as a regulator of local and systemic physiology through its ability to attenuate nitric oxide signaling. The identification of TSP1 as a regulator of nitric oxide signaling has significantly broadened our understanding of the role of TSP1, especially in vascular physiology and pathology.The review by Risher and Eroglu (2012, this issue) discusses exciting, novel findings documenting a role for TSP in synaptogenesis through interactions between astrocyte-secreted TSPs and their neuronal receptor, calcium channel subunit α2δ-1, also a receptor for gabapentin. Collectively, these new findings have implications for neuronal development and responses to CNS injury.Finally, Sweetwyne and Murphy-Ullrich (2012, this issue) focus on distinct roles for TSP1 mediated by different domains which impact basic cellular processes key for wound healing, tissue repair, and fibrosis. These entail stimulation of collagen expression through the N-terminal domain calreticulin-binding sequence, transactivation of EGF receptor by the EGF-like domains, and regulation of latent TGF-β activation by the TSR type 1 repeats.Many of these findings were initially presented at the 2010 FASEB Summer Research Conference on Thrombospondins and Other Matricellular Proteins in Tissue Organization and Homeostasis. Clearly, despite several decades of research, the thrombospondins continue to surprise us with their broad and clinically-significant roles in physiology and disease. The field of matrix biology has been enriched by the often unexpected roles of thrombospondins in normal development and physiology and in the pathophysiology of diverse disease processes." @default.
• W2040907586 created "2016-06-24" @default.
• W2040907586 creator A5017416196 @default.
• W2040907586 creator A5030553564 @default.
• W2040907586 date "2012-04-01" @default.
• W2040907586 modified "2023-09-23" @default.
• W2040907586 title "Thrombospondins in physiology and disease: New tricks for old dogs" @default.
• W2040907586 cites W1489446974 @default.
• W2040907586 cites W1505957065 @default.
• W2040907586 cites W1519311536 @default.
• W2040907586 cites W1534240923 @default.
• W2040907586 cites W1540432147 @default.
• W2040907586 cites W1568527001 @default.
• W2040907586 cites W1577635103 @default.
• W2040907586 cites W1613957108 @default.
• W2040907586 cites W1964204236 @default.
• W2040907586 cites W1976566546 @default.
• W2040907586 cites W1979229054 @default.
• W2040907586 cites W1980915493 @default.
• W2040907586 cites W1984042384 @default.
• W2040907586 cites W1995971227 @default.
• W2040907586 cites W1998207166 @default.
• W2040907586 cites W2004329603 @default.
• W2040907586 cites W2007799501 @default.
• W2040907586 cites W2030011981 @default.
• W2040907586 cites W2062005186 @default.
• W2040907586 cites W2062852060 @default.
• W2040907586 cites W2063170261 @default.
• W2040907586 cites W2072626278 @default.
• W2040907586 cites W2072890248 @default.
• W2040907586 cites W2072902494 @default.
• W2040907586 cites W2074858207 @default.
• W2040907586 cites W2075386107 @default.
• W2040907586 cites W2083568793 @default.
• W2040907586 cites W2085931182 @default.
• W2040907586 cites W2093586592 @default.
• W2040907586 cites W2101650166 @default.
• W2040907586 cites W2102786937 @default.
• W2040907586 cites W2104272971 @default.
• W2040907586 cites W2111344261 @default.
• W2040907586 cites W2124594265 @default.
• W2040907586 cites W2132679962 @default.
• W2040907586 cites W2142610113 @default.
• W2040907586 cites W2145015359 @default.
• W2040907586 cites W2155825119 @default.
• W2040907586 cites W2167259460 @default.
• W2040907586 cites W2167899389 @default.
• W2040907586 cites W3116925564 @default.
• W2040907586 cites W4211045489 @default.
• W2040907586 cites W4229500213 @default.
• W2040907586 cites W4256132137 @default.
• W2040907586 cites W95482459 @default.
• W2040907586 cites W95576175 @default.
• W2040907586 doi "https://doi.org/10.1016/j.matbio.2012.01.002" @default.
• W2040907586 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3615564" @default.
• W2040907586 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22265891" @default.
• W2040907586 hasPublicationYear "2012" @default.
• W2040907586 type Work @default.
• W2040907586 sameAs 2040907586 @default.
• W2040907586 citedByCount "45" @default.
• W2040907586 countsByYear W20409075862012 @default.
• W2040907586 countsByYear W20409075862013 @default.
• W2040907586 countsByYear W20409075862014 @default.
• W2040907586 countsByYear W20409075862015 @default.
• W2040907586 countsByYear W20409075862016 @default.
• W2040907586 countsByYear W20409075862017 @default.
• W2040907586 countsByYear W20409075862018 @default.
• W2040907586 countsByYear W20409075862019 @default.
• W2040907586 countsByYear W20409075862020 @default.
• W2040907586 countsByYear W20409075862021 @default.
• W2040907586 countsByYear W20409075862022 @default.
• W2040907586 countsByYear W20409075862023 @default.
• W2040907586 crossrefType "journal-article" @default.
• W2040907586 hasAuthorship W2040907586A5017416196 @default.
• W2040907586 hasAuthorship W2040907586A5030553564 @default.
• W2040907586 hasBestOaLocation W20409075862 @default.
• W2040907586 hasConcept C109523444 @default.
• W2040907586 hasConcept C142724271 @default.
• W2040907586 hasConcept C167814343 @default.
• W2040907586 hasConcept C169760540 @default.
• W2040907586 hasConcept C2779134260 @default.
• W2040907586 hasConcept C2910422434 @default.
• W2040907586 hasConcept C42407357 @default.
• W2040907586 hasConcept C54355233 @default.
• W2040907586 hasConcept C55728118 @default.
• W2040907586 hasConcept C71924100 @default.
• W2040907586 hasConcept C86803240 @default.
• W2040907586 hasConceptScore W2040907586C109523444 @default.
• W2040907586 hasConceptScore W2040907586C142724271 @default.
• W2040907586 hasConceptScore W2040907586C167814343 @default.
• W2040907586 hasConceptScore W2040907586C169760540 @default.
• W2040907586 hasConceptScore W2040907586C2779134260 @default.
• W2040907586 hasConceptScore W2040907586C2910422434 @default.
• W2040907586 hasConceptScore W2040907586C42407357 @default.
• W2040907586 hasConceptScore W2040907586C54355233 @default.
• W2040907586 hasConceptScore W2040907586C55728118 @default.
• W2040907586 hasConceptScore W2040907586C71924100 @default.
• W2040907586 hasConceptScore W2040907586C86803240 @default.

• next