High impact information on Sulf1

• The binding sites consist of relatively small tracts of variably sulfated glucosamine and uronic acid residues in specific arrangements [1].
• Glutactin, a new acidic sulfated glycoprotein, was isolated from Drosophila Kc cell culture media [2].
• Using Alcian Blue, a histochemical stain that detects sulfated glycans, we observed a novel, pipe-dependent macromolecule in the embryonic salivary glands [3].
• Each of the two homologues include a CCK-gastrin-like C-terminal pentapeptide and a conserved sequence corresponding to the sulfated tyrosine in bioactive CCK [4].
• YP2 secreted from mouse fibroblasts was found to be exclusively sulfated on tyrosine residues [5].

Biological context of Sulf1

• Ftz/Ftz-F1 activate Sulf1 expression in blastoderm embryos via composite binding sites [6].
• The role of heparan sulfated proteoglycans, endocytosis and novel exovesicles called argosomes in regulating morphogen distribution will also be discussed [7].

Anatomical context of Sulf1

• Mouse fibroblasts, transfected with Drosophila YP2 genomic DNA inserted into the eucaryotic expression vector pSV2, secreted the fly protein in sulfated form [5].
• Papilin: a Drosophila proteoglycan-like sulfated glycoprotein from basement membranes [8].

Associations of Sulf1 with chemical compounds

• After separation of total fly protein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, proteins with sulfated carbohydrates and proteins containing tyrosine sulfate were found in all the molecular weight ranges analyzed [9].
• The unsulfated [Leu(7)]-DSK-1 was ca. 3000-fold less potent than its sulfated counterpart which stresses the importance of the sulfate moiety for the biological activity of drosulfakinin [10].

Regulatory relationships of Sulf1

• When expressed in mammalian cells, DSK-R1 was activated by a sulfated, Met(7-->Leu(7)-substituted analog of drosulfakinin-1, FDDY(SO(3)H)GHLRF-NH(2) ([Leu(7)]-DSK-1S) [10].

Other interactions of Sulf1

• The DSK-R1 was specific for the insect sulfakinin since two related vertebrate sulfated peptides, human CCK-8 and gastrin-II, were found inactive when tested at concentrations up to 10(-5) M [10].

References