High impact information on THBS1

• Vitronectin and thrombospondin promote retinal neurite outgrowth: developmental regulation and role of integrins [1].
• Attachment to thrombospondin was inhibited by heparin, suggesting that neurons also utilize a proteoglycan or sulfated glycolipid as a receptor for this glycoprotein [1].
• Of a battery of integrin ligands tested, only thrombospondin mimicked the effect of the extracellular matrix on substance P responsiveness [2].
• Because the mRNA for thrombospondin is present in the cells of the chicken amnion, this extracellular factor may normally suppress substance P responsiveness in amniotic smooth muscle [2].
• Substance P responsiveness of smooth muscle cells is regulated by the integrin ligand, thrombospondin [2].

Biological context of THBS1

• 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 [3].
• 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 [3].
• Thrombospondin -4 transcripts first appear in the mesenchyme surrounding bone anlage coinciding with the initial stages of osteogenesis [4].
• 2. Analysis of the amino acid sequence has revealed a novel member of the TRAP (thrombospondin-related anonymous protein) family, containing 16 thrombospondin type-1 repeats and 31 epidermal growth factor-like calcium binding domains [5].

Anatomical context of THBS1

• 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 [3].
• Cell contact-dependent activation of alpha3beta1 integrin modulates endothelial cell responses to thrombospondin-1 [6].
• The diverse origins of different thrombospondin gene family members imply distinctive roles for these proteins related to the growth and differentiation of cartilage, tendons, and bone [4].

Associations of THBS1 with chemical compounds

• 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 [3].
• Many conserved domains have been identified, including 27 thrombospondin type 1 repeats, 13 low-density lipoprotein receptor type A domains, one EMI domain (a cysteine-rich domain of extracellular proteins), three von Willebrand factor type D domains, and one cystine knot C-terminal domain [7].

Other interactions of THBS1

• Thrombospondin-1 and thrombospondin-2 have similar primary structure, but are expressed in different tissues at different times during development [4].
• E7-RGCs developed better on thrombospondin and vitronectin [8].
• E10-RGCs cultured on vitronectin grew better than on laminin; on thrombospondin and collagen, E10-RGCs grew like on laminin and on fibronectin they had a poor development [8].

References