US2003004319A1PendingUtilityA1
Mammalian growth factor
Est. expiryJun 16, 2007(expired)· nominal 20-yr term from priority
C07K 14/50
47
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Claims
Abstract
A mammalian growth factor, displaying homology to both basic and acidic fibroblast growth factor in a single polypeptide chain, is disclosed herein. The growth factor was isolated from cells transfected with the DNA extracted from Kaposi's Sarcoma cells.
Claims
exact text as granted — not AI-modifiedWhat is claimed is:
1 . A polypeptide having substantial homology to each of basic and acidic fibroblast growth factor said polypeptide having growth factor activity and having an amino acid sequence consisting essentially of the amino acid sequence of the expression product of a fragment of an oncogene isolated from Kaposi's sarcoma cells.
2 . A polypeptide comprising the amino acid sequence:
Met Ser Gly Pro Gly Thr Ala Ala Val Ala Leu Leu
Pro Ala Val Leu Leu Ala Leu Leu Ala Pro Trp Ala
Gly Arg Gly Gly Ala Ala Ala Pro Thr Ala Pro Asn
Gly Thr Leu Glu Ala Glu Leu Glu Arg Arg Trp Glu
Ser Leu Val Ala Leu Ser Leu Ala Arg Leu Pro Val
Ala Ala Gln Pro Lys Glu Ala Ala Val Gln Ser Gly
Ala Gly Asp Tyr Leu Leu Gly Ile Lys Arg Leu Arg
Arg Leu Tyr Cys Asn Val Gly Ile Gly Phe His Leu
Gln Ala Leu Pro Asp Gly Arg Ile Gly Gly Ala His
Ala Asp Thr Arg Asp Ser Leu Leu Glu Leu Ser Pro
Val Glu Arg Gly Val Val Ser Ile Phe Gly Val Ala
Ser Arg Phe Phe Val Ala Met Ser Ser Lys Gly Lys
Leu Tyr Gly Ser Pro Phe Phe Thr Asp Glu Cys Thr
Phe Lys Glu Ile Leu Leu Pro Asn Asn Tyr Asn Ala
Tyr Glu Ser Tyr Lys Tyr Pro Gly Met Phe Ile Ala
Leu Ser Lys Asn Gly Lys Thr Lys Lys Gly Asn Arg
Val Ser Pro Thr Met Lys Val Thr His Phe Leu Pro
Arg Leu.
3 . A gene coding for the polypeptide of claim 1 or 2.
4 . A polypeptide comprising the amino acid sequence
Ser Gly Ala Gly Asp Tyr Leu Leu Gly Ile Lys Arg
Leu Arg Arg Leu Tyr Cys Asn Val Gly Ile Gly Phe
His Leu Gln Ala Leu Pro Asp Gly Arg Ile Gly Gly
Ala His Ala Asp Thr Arg Asp Ser Leu Leu Glu Leu
Ser Pro Val Glu Arg Gly Val Val Ser Ile Phe Gly
Val Ala Ser Arg Phe Phe Val Ala Met Ser Ser Lys
Gly Lys Leu Tyr Gly Ser Pro Phe Phe Thr Asp Glu
Cys Thr Phe Lys Glu Ile Leu Leu Pro Asn Asn Tyr
Asn Ala Tyr Glu Ser Tyr Lys Tyr Pro Gly Met Phe
Ile Ala Leu Ser Lys Asn Gly Lys Thr Lys Lys Gly
Asn Arg Val Ser Pro Thr Met Lys Val Thr His Phe
Leu Pro Arg Leu.
5 . The polypeptide of claim 1 comprising the amino acid sequence:
Met Ser Gly Pro Gly Thr Ala Ala Val Ala Leu Leu Pro Ala Val
Leu Leu Ala Leu Leu Ala Pro Trp Ala Gly Arg Gly Gly Ala Ala
Ala Pro Thr Ala Pro Asn Gly Thr Leu Glu Ala Glu Leu Glu Arg
Arg Trp Glu Ser Leu Val Ala Leu Ser Leu Ala Arg Leu Pro Val
Ala Ala Gln Pro Lys Glu Ala Ala Val Gln Ser Gly Ala Gly Asp
Tyr Leu Leu Gly Ile Lys Arg Leu Arg Arg Leu Tyr Cys Asn Val
Gly Ile Gly Phe His Leu Gln Ala Leu Pro Asp Gly Arg Ile Gly
Gly Ala His Ala Asp Thr Arg Asp Ser Leu Leu Glu Leu Ser Pro
Val Glu Arg Gly Val Val Ser Ile Phe Gly Val Ala Ser Arg Phe
Phe Val Ala Met Ser Ser Lys Gly Lys Leu Tyr Gly Ser Pro Phe
Phe Thr Asp Glu Cys Thr Phe Lys Glu Ile Leu Leu Pro Asn Asn
Tyr Asn Ala Tyr Glu Ser Tyr Lys Tyr Pro Gly Met Phe Ile Ala
Leu Ser Lys Asn Gly Lys Thr Lys Lys Gly Asn Arg Val Ser Pro
Thr Met Lys Val Thr His Phe Leu Pro Arg Leu.
6 . The polypeptide of claim 1 wherein said homology to each of said acidic and basic growth factors is at least about 35%.
7 . The polypeptide of claim 6 herein said homology is at least about 60% taking conservative substitutions into account.
8 . The polypeptide of claim 5 consisting essentially of said amino acid sequence.
9 . A purified, isolated DNA fragment comprising the nucleotide sequence:
ATG TCG GGG CCC GGG ACG GCC GCG GTA GCG CTG CTC CCG GCG GTC
CTG CTG GCC TTG CTG GCG CCC TGG GCG GGC CGA GGG GGC GCC GCC
GCA CCC ACT GCA CCC AAC GGC ACG CTG GAG GCC GAG CTG GAG CGC
CGC TGG GAG AGC CTG GTG GCG CTC TCG TTG GCG CGC CTG CCG GTG
GCA GCG CAG CCC AAG GAG GCG GCC GTC CAG AGC GGC GCC GGC GAC
TAC CTG CTG GGC ATC AAG CGG CTG CGG CGG CTC TAC TGC AAC GTG
GGC ATC GGC TTC CAC CTC CAG GCG CTC CCC GAC GGC CGC ATC GGC
GGC GCG CAC GCG GAC ACC CGC GAC AGC CTG CTG GAG CTC TCG CCC
GTG GAG CGG GGC GTG GTG AGC ATC TTC GGC GTG GCC AGC CGG TTC
TTC GTG GCC ATG AGC AGC AAG GGC AAG CTC TAT GGC TCG CCC TTC
TTC ACC GAT GAG TGC ACG TTC AAG GAG ATT CTC CTT CCC AAC AAC
TAC AAC GCC TAC GAG TCC TAC AAG TAC CCC GGC ATG TTC ATC GCC
CTG AGC AAG AAT GGG AAG ACC AAG AAG GGG AAC CGA GTG TCG CCC
ACC ATG AAG GTC ACC CAC TTC CTC CCC AGG CTG
and coding for a mammalian growth factor.
10 . A method for healing wounds or burns in mammals comprising administering to mammals in need of such treatment a cell-growth promoting effective amount of the polypeptide of claim 1 .
11 . The method of claim 10 wherein said polypeptide comprises the amino acid sequence:
Met Ser Gly Pro Gly Thr Ala Ala Val Ala Leu Leu
Pro Ala Val Leu Leu Ala Leu Leu Ala Pro Trp Ala
Gly Arg Gly Gly Ala Ala Ala Pro Thr Ala Pro Asn
Gly Thr Leu Glu Ala Glu Leu Glu Arg Arg Trp Glu
Ser Leu Val Ala Leu Ser Leu Ala Arg Leu Pro Val
Ala Ala Gln Pro Lys Glu Ala Ala Val Gln Ser Gly
Ala Gly Asp Tyr Leu Leu Gly Ile Lys Arg Leu Arg
Arg Leu Tyr Cys Asn Val Gly Ile Gly Phe His Leu
Gln Ala Leu Pro Asp Gly Arg Ile Gly Gly Ala His
Ala Asp Thr Arg Asp Ser Leu Leu Glu Leu Ser Pro
Val Glu Arg Gly Val Val Ser Ile Phe Gly Val Ala
Ser Arg Phe Phe Val Ala Met Ser Ser Lys Gly Lys
Leu Tyr Gly Ser Pro Phe Phe Thr Asp Glu Cys Thr
Phe Lys Glu Ile Leu Leu Pro Asn Asn Tyr Asn Ala
Tyr Glu Ser Tyr Lys Tyr Pro Gly Met Phe Ile Ala
Leu Ser Lys Asn Gly Lys Thr Lys Lys Gly Asn Arg
Val Ser Pro Thr Met Lys Val Thr His Phe Leu Pro
Arg Leu.
12 . The method of claim 10 comprising topically administering said polypeptide.
13 . The method of claim 10 comprising an angiogenesis-promoting effective amount of said polypeptide.
14 . A pharmaceutical formulation for promoting healing of wounds or burns in mammals comprising as an active ingredient a cell-growth promoting effective amount of a member selected from the group consisting of the polypeptide of claim 1 and physiologically acceptable salts thereof.
15 . The formulation of claim 14 further comprising a physiologically acceptable carrier.
16 . The pharmaceutical formulation of claim 14 further comprising a water-miscible antibacterial agent.
17 . The pharmaceutical formulation of claim 14 comprising between about 0.01 micrograms and about 10 micrograms of said polypeptide.
18 . A method for promoting cell growth in a cell culture comprising introducing into said culture a cell growth-promoting effective amount of the polypeptide of claim 1 .
19 . A polypeptide comprising the amino acid sequence:
X - Thr Ala Pro Asn Gly Thr Leu Glu Ala Glu Leu
Glu Arg Arg Trp Glu Ser Leu Val Ala Leu Ser Leu
Ala Arg Leu Pro Val Ala Ala Gln Pro Lys Glu Ala
Ala Val Gln Ser Gly Ala Gly Asp Tyr Leu Leu Gly
Ile Lys Arg Leu Arg Arg Leu Tyr Cys Asn Val Gly
Ile Gly Phe His Leu Gln Ala Leu Pro Asp Gly Arg
Ile Gly Gly Ala His Ala Asp Thr Arg Asp Ser Leu
Leu Glu Leu Ser Pro Val Glu Arg Gly Val Val Ser
Ile Phe Gly Val Ala Ser Arg Phe Phe Val Ala Met
Ser Ser Lys Gly Lys Leu Tyr Gly Ser Pro Phe Phe
Thr Asp Glu Cys Thr Phe Lys Glu Ile Leu Leu Pro
Asn Asn Tyr Asn Ala Tyr Glu Ser Tyr Lys Tyr Pro
Gly Met Phe Ile Ala Leu Ser Lys Asn Gly Lys Thr
Lys Lys Gly Asn Arg Val Ser Pro Thr Met Lys Val
Thr His Phe Leu Pro Arg Leu;
wherein X is selected from the group consisting of Ala-Pro or Pro.
20 . A method for healing wounds or burns in mammals comprising administering to mammals in need of such treatment a cell-growth promoting effective amount of the polypeptide of claim 19 .
21 . The method of claim 20 comprising topically administering said growth factor.
22 . A pharmaceutical formulation for promoting healing of wounds or burns in mammals comprising as an active ingredient a cell-growth promoting effective amount of a member selected from the group consisting of the polypeptide of claim 19 and physiologically acceptable salts thereof.
23 . The formulation of claim 22 further comprising a physiologically acceptable carrier.
24 . The pharmaceutical formulation of claim 22 further comprising a water-miscible antibacterial agent.
25 . The pharmaceutical formulation of claim 22 comprising between about 0.01 micrograms and about 10 micrograms of said polypeptide.
26 . A method for promoting cell growth in a cell culture comprising introducing into said culture a cell growth-promoting effective amount of the polypeptide of claim 19 .
27 . The method of claim 20 further comprising administering an amount of heparin effective to stabilize said polypeptide.
28 . The formulation of claim 24 further comprising an amount of heparin effective to stabilize said polypeptide.
29 . The polypeptide of claim 19 wherein said polypeptide is further characterized by having the ability to induce the production of plasminogen activator in endothelial cells in culture.
30 . A procaryotic or eukaryotic host cell transformed or transfected with a DNA sequence according to claim 9 in a manner allowing the host cell to express a polypeptide having substantial homology to each of acidic and basic fibroblast growth factor activity and having an amino acid sequence consisting essentially of the amino acid sequence of the expression product of a fragment of an oncogene isolated from Kaposi's Sarcoma cells.
31 . A procaryotic or eukaryotic host cell stably transformed with a DNA vector according to claim 30 .
32 . A purified and isolated DNA sequence consisting essentially of a DNA sequence encoding a polypeptide having substantial homology to each of acidic and basic fibroblast growth factor activity and having an amino acid sequence consisting essentially of the amino acid sequence of the expression product of a fragment of an oncogene isolated from Kaposi's Sarcoma cells.
33 . A transformed or transfected COS cell according to claim 31 .
34 . A transformed or transfected N3H3T3 cell according to claim 31 .
35 . Transformed or transfected E. coli cell according to claim 31 .Join the waitlist — get patent alerts
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