The present invention relates to a TGF-.beta.1
binding protein called r150. This
protein has a GPI-anchor contained in r150 itself and not on a tightly associated
protein and that it binds TGF-.beta.1 with an affinity comparable to those of the signaling receptors. Furthermore, the released (soluble) form of this
protein binds TGF-.beta.1 independent of the types I and II receptors. Also, the soluble form inhibits the binding of TGF-.beta. to its
receptor. In addition, evidence that r150 is released from the
cell surface by an endogenous
phospholipase C is provided. Also, the creation of a
mutant human keratinocyte cell line with a defect in GPI synthesis which displays reduced expression of r150 is described. Our results using these
mutant keratinocytes suggest that the membrane anchored form of r150 is a negative modulator of TGF-beta responses. These findings, taken together with the observation that r150 forms a heteromeric complex with the signaling receptors, suggest that this accessory
receptor in either its membrane anchored or soluble form may antagonize TGF-.beta. responses in human keratinocytes. Experiments with mutants confirmed that TGF.beta.1 activity can be modulated when the expression of the accessory
receptor r150 is silenced. The complete
nucleic acid and deduced
amino acid sequences are now provided. The r150 cloned
nucleic acid was used to study overexpression of r150. When r150
gene is overexpressed, TGF.beta. responses are increased. r150 and its derivatives or precursors (fragments, variants and nucleic acids encoding the same) will find a broad clinical utility, knowing that TGF.beta.1 is an important
cytokine.