US2003027981A1PendingUtilityA1

Urokinase-type plasminogen activator receptor

39
Priority: Apr 7, 1989Filed: Jan 8, 2001Published: Feb 6, 2003
Est. expiryApr 7, 2009(expired)· nominal 20-yr term from priority
Inventors:Keld DanoFrancesco BlasiAnn Louring RoldanMaria Vittoria CubellisMaria Teresa MasucciEttore AppellaWolf-Dieter SchleuningNiels BehrendtEbbe RonnePeter KristensenJari PollanenEeva-Marjatta SalonenRoss StephensHannele TapiovaaraAntti VaheriLisbeth MollerVincent EllisLeif R.O Slashed.Ge LundMichael PlougCharles PykeLaszlo Patthy
G01N 33/5753C12N 9/6462A61K 38/00A61K 38/49A61K 39/3955C07K 14/705C07K 16/28C07K 16/2896C07K 2317/77C12Q 1/6886G01N 33/86G01N 2333/9723C12Y 304/21073C12Q 2600/158C07K 2317/76
39
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Claims

Abstract

A polypeptide presenting an epitope cross-reactive with an epitope of urokinase-type plasminogen activator receptor, and/or having uPA binding activity, is described.

Claims

exact text as granted — not AI-modified
1 . An isolated or purified polypeptide, soluble in aqueous solution, and having urokinase plasminogen activator (uPA) binding activity, 
 said polypeptide comprising a uPA-binding domain whose amino acid sequence is identical to (i) SEQ ID NO:3, or (ii) to the amino acid sequence of uPA binding 16 kDa glycosylated chymotryptic fragment of a mature uPA receptor, or which (iii) differs in amino acid sequence from (i) or (ii) above solely by one or more conservative substitutions,    said polypeptide consisting of an amino acid sequence which is not identical to sequence (A) or to the amino acid sequence of the polypeptide directly encoded by the u-PAR gene,    said polypeptide lacking a glycosyl-phosphatidyl inositol moiety functional as a cell surface anchor.    
     
     
         2 . The polypeptide of  claim 1  wherein said domain, if differing in amino acid sequence from (i) or (ii) above, does so solely by a single conservative amino acid substitution.  
     
     
         3 . The polypeptide of  claim 1  where said domain is identical to SEQ ID NO:3.  
     
     
         4 . The polypeptide of  claim 1  where the amino acid sequence of the polypeptide is identical to residues 1-286 of Sequence A, or differs therefrom solely by (1) a carboxy terminal truncation, (2) one or more conservative substitutions of amino acids, or (3) both (1) and (2) above.  
     
     
         5 . The polypeptide of  claim 2  where the amino acid sequence of the polypeptide is identical to residues 1-286 of Sequence A, or differs therefrom solely by (1) a carboxy terminal truncation, (2) one or more conservative substitutions of amino acids, or (3) both (1) and (2) above.  
     
     
         6 . The polypeptide of  claim 3  where the amino acid sequence of the polypeptide is identical to residues 1-286 of Sequence A, or differs therefrom solely by (1) a carboxy terminal truncation, (2) one or more conservative substitutions of amino acids, or (3) both (1) and (2) above.  
     
     
         7 . The polypeptide of  claim 4  wherein there is no more than a single conservative substitution according to (2) above.  
     
     
         8 . The polypeptide of  claim 1  where said amino acid sequence of said polypeptide is selected from the group consisting of residues 1-92, 1-280, 1-281, 1-282, 1-283, 1-284, 1-285, and 1-286 of Sequence A.  
     
     
         9 . The polypeptide of  claim 1  where the amino acid sequence of the polypeptide is identical to residues 1-281 of Sequence A, or differs therefrom solely by (1) a carboxy terminal truncation, (2) one or more conservative substitutions of amino acids, or (3) both (1) and (2) above.  
     
     
         10 . The polypeptide of  claim 2  where the amino acid sequence of the polypeptide is identical to residues 1-281 of Sequence A, or differs therefrom solely by (1) a carboxy terminal truncation, (2) one or more conservative substitutions of amino acids, or (3) both (1) and (2) above.  
     
     
         11 . The polypeptide of  claim 3  where the amino acid sequence of the polypeptide is identical to residues 1-281 of Sequence A, or differs therefrom solely by (1) a carboxy terminal truncation, (2) one or more conservative substitutions of amino acids, or (3) both (1) and (2) above.  
     
     
         12 . The polypeptide of  claim 1 , said polypeptide being glycosylated.  
     
     
         13 . The polypeptide of  claim 1 , in sequencably pure form.  
     
     
         14 . The polypeptide of  claim 1  where the amino acid sequence of the polypeptide is identical to residues 1-286 of sequence A, or differs therefrom solely by a carboxy terminal truncation.  
     
     
         15 . The polypeptide of  claim 9  where the amino acid sequence of the polypeptide is identical to residues 1-281 of sequence A, or differs therefrom solely by a carboxy terminal truncation.  
     
     
         16 . A polypeptide according to  claim 1  provided with a detectable label.  
     
     
         17 . A polypeptide according to  claim 1 , coupled to a solid support.  
     
     
         18 . The polypeptide of  claim 1 , which lacks sequences identical to residues 93-281 of sequence (A) or differing therefrom solely by one or more conservative substitutions.  
     
     
         19 . The polypeptide of  claim 1 , said polypeptide comprising 
 (a) the amino acid sequence of SEQ ID NO:3, or    (b) an amino acid sequence encoded by a DNA sequence which hybridizes, under hybridization conditions of 5× SSC and 50° C., to a probe complementary to the messenger RNA natively encoded by the portion of human u-PAR gene which encodes SEQ ID NO:3.    
     
     
         20 . The polypeptide of  claim 1 , said polypeptide comprising 
 (a) the amino acid sequence of SEQ ID NO:3, or    (b) an amino acid sequence encoded by a DNA sequence which hybridizes, under hybridization conditions of 2× SSC and 65° C., to a probe complementary to the messenger RNA natively encoded by the portion of human u-PAR gene which encodes SEQ ID NO:3.    
     
     
         21 . An isolated or purified polypeptide, soluble in aqueous solution, and having urokinase plasminogen activator (uPA) binding activity, 
 said polypeptide comprising a uPA-binding domain whose amino acid sequence is identical to (i) SEQ ID NO:3, or (ii) to the amino acid sequence of uPA binding 16 kDa glycosylated chymotryptic fragment of a mature uPA receptor, or which (iii) differs in amino acid sequence from (i) or (ii) above solely by one or more conservative substitutions.    
     
     
         22 . The polypeptide of  claim 21 , where said polypeptide lacks a glycosyl-phosphatidyl inositol moiety functional as a cell surface anchor.  
     
     
         23 . The polypeptide of  claim 22  where said amino acid sequence of said polypeptide consists of said uPA binding domain.  
     
     
         24 . The polypeptide of  claim 22  where said amino acid sequence consists of residues 1-281 of sequence A.  
     
     
         25 . The polypeptide of  claim 22  where said amino acid sequence consists of residues 1-282 of sequence A.  
     
     
         26 . The polypeptide of  claim 22  where said amino acid sequence consists of residues 1-283 of sequence A.  
     
     
         27 . The polypeptide of  claim 22  where said amino acid sequence consists of residues 1-284 of sequence A.  
     
     
         28 . The polypeptide of  claim 22  where said amino acid sequence consists of residues 1-285 of sequence A.  
     
     
         29 . The polypeptide of  claim 22  where said amino acid sequence consists of residues 1-286 of sequence A.  
     
     
         30 . A composition comprising a polypeptide according to  claim 21 , and an anticancer agent.  
     
     
         31 . The polypeptide of  claim 1 , which lacks a functional domain essentially corresponding to the second domain of u-PAR, and which lacks a functional domain essentially corresponding to the third domain of u-PAR.  
     
     
         32 . The polypeptide of  claim 21  whose amino acid sequence differs from amino acids 1-313 of sequence (1) solely by one or more replacements or deletions of amino acids.  
     
     
         33 . The polypeptide of  claim 21  which lacks anti-inflammatory activity.  
     
     
         34 . The polypeptide of  claim 1  which is in glycosylated form.  
     
     
         35 . The polypeptide of  claim 34  which shows, in an SDS-PAGE at a load of approximately one microgram, substantially one and only one silver stained band having an apparent molecular weight in the range of about 55-60 kDa.  
     
     
         36 . The polypeptide of  claim 21  which is in glycosylated form.  
     
     
         37 . The polypeptide of  claim 36  which shows, in an SDS-PAGE at a load of approximately one microgram, substantially one and only one silver stained band having an apparent molecular weight in the range of about 55-60 kDa.

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