Trombospondina 1: Diferenzas entre revisións

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Miguelferig (conversa | contribucións)
Miguelferig (conversa | contribucións)
Liña 107:
 
== Estrutura ==
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Thrombospondin's activity has been mapped to several domains, in particular the [[amino-terminal]] heparin-binding domain, the procollagen domain, the properdin-like type I repeats, and the globular [[carboxy-terminal]] domain. The protein also contains type II repeats with epidermal growth factor-like homology and type III repeats that contain an [[RGD motif|RGD]] sequence.<ref name="pmid17160353">{{cite journal | vauthors = Forslöw A, Liu Z, Sundqvist KG | title = Receptor communication within the lymphocyte plasma membrane: a role for the thrombospondin family of matricellular proteins | journal = Cellular and Molecular Life Sciences | volume = 64 | issue = 1 | pages = 66–76 | date = Jan 2007 | pmid = 17160353 | doi = 10.1007/s00018-006-6255-8 }}</ref>
 
Thrombospondin'sA activityactividade hasde beentrombospondina mappedfoi tomapeada severalen domainsvarios dominios, inen particularespecial theo dominio de unión á [[amino-terminalheparina]] heparin-binding[[amino domainterminal]], theo procollagendominio domainprocoláxeno, theas properdin-likerepeticións typesimilares Iá repeatsproperdina tipo 1, ande theo dominio globular [[carboxy-carboxi terminal]] domain. TheA proteinproteína alsotamén containscontén typerepeticións de tipo II repeatscon withhomoloxía epidermalsimilar growthao factor-like homologyde andcrecemento typeepidérmico e repeticións de tipo III repeatsque thatcontén containunha ansecuencia [[motivo RGD motif|RGD]] sequence.<ref name="pmid17160353">{{cite journal | vauthors = Forslöw A, Liu Z, Sundqvist KG | title = Receptor communication within the lymphocyte plasma membrane: a role for the thrombospondin family of matricellular proteins | journal = Cellular and Molecular Life Sciences | volume = 64 | issue = 1 | pages = 66–76 | date = Jan 2007 | pmid = 17160353 | doi = 10.1007/s00018-006-6255-8 }}</ref>
=== N-terminal ===
 
=== N-terminal ===
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The [[N-terminus|N-terminal]] heparin-binding domain of TSP1, when isolated as a 25[[kDa]] fragment, has been shown to be a potent inducer of cell migration at high concentrations. However, when the heparin-binding domain of TSP1 is cleaved, the remaining anti-angiogenic domains have been shown to have decreased anti-angiogenic activity at low concentrations where increased [[endothelial cell]] (EC) migration occurs. This may be explained in part by the ability of the heparin-binding domain to mediate attachment of TSP1 to cells, allowing the other domains to exert their effects. The separate roles that the heparin-binding region of TSP1 plays at high versus low concentrations may be in part responsible for regulating the two-faced nature of TSP1 and giving it a reputation of being both a positive and negative regulator of angiogenesis.<ref name="pmid7686555">{{cite journal | vauthors = Tolsma SS, Volpert OV, Good DJ, Frazier WA, Polverini PJ, Bouck N | title = Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity | journal = The Journal of Cell Biology | volume = 122 | issue = 2 | pages = 497–511 | date = Jul 1993 | pmid = 7686555 | pmc = 2119646 | doi = 10.1083/jcb.122.2.497 }}</ref>