Conservation in sequence and affinity of human and rodent PDGF ligands and receptors
Platelet-derived growth factor (PDGF) consists of two chains, PDGF-A and-B, which activate as homo- or heterodimers two receptors, α and β. To test PDGF function in vivo we have generated neutralizing monoclonal antibodies. When analyzed with rat PDGFs only antibodies raised against human PDGF-AA sh...
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| Autor*in: |
|---|
| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1993 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression - Amsterdam : Elsevier, 1173(1993), 3, Seite 294-302 |
| Übergeordnetes Werk: |
volume:1173 ; year:1993 ; number:3 ; pages:294-302 |
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| 520 | |a Platelet-derived growth factor (PDGF) consists of two chains, PDGF-A and-B, which activate as homo- or heterodimers two receptors, α and β. To test PDGF function in vivo we have generated neutralizing monoclonal antibodies. When analyzed with rat PDGFs only antibodies raised against human PDGF-AA showed cross-species activity. This correlated with complete amino acid sequence conservation of PDGF-A whereas rat PDGF-B differed in six positions when cloned rat PDGF cDNAs were compared with their human homologs within the receptor binding region. Extracellular domains of cloned rat PDGF α- and β-receptor cDNAs did not reflect this difference in cross-species ligand conservation. When rat extracellular domains were expressed as soluble proteins they bound human PDGF-BB with high affinity after immobilization of the purified proteins on solid phase. Dissociation constants were identical to those of their human homologs. Thus, high affinity binding of human PDGF-BB to extracellular domains does not depend on species origin but only on receptor type. | ||
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(DE-627)NLEJ186812574 (DE-599)GBVNLZ186812574 DE-627 ger DE-627 rakwb eng Conservation in sequence and affinity of human and rodent PDGF ligands and receptors 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Platelet-derived growth factor (PDGF) consists of two chains, PDGF-A and-B, which activate as homo- or heterodimers two receptors, α and β. To test PDGF function in vivo we have generated neutralizing monoclonal antibodies. When analyzed with rat PDGFs only antibodies raised against human PDGF-AA showed cross-species activity. This correlated with complete amino acid sequence conservation of PDGF-A whereas rat PDGF-B differed in six positions when cloned rat PDGF cDNAs were compared with their human homologs within the receptor binding region. Extracellular domains of cloned rat PDGF α- and β-receptor cDNAs did not reflect this difference in cross-species ligand conservation. When rat extracellular domains were expressed as soluble proteins they bound human PDGF-BB with high affinity after immobilization of the purified proteins on solid phase. Dissociation constants were identical to those of their human homologs. Thus, high affinity binding of human PDGF-BB to extracellular domains does not depend on species origin but only on receptor type. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Herren, B. oth Weyer, K.A. oth Rouge, M. oth Lotscher, P. oth Pech, M. oth in Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression Amsterdam : Elsevier 1173(1993), 3, Seite 294-302 (DE-627)NLEJ176932224 (DE-600)2209522-6 0167-4781 nnns volume:1173 year:1993 number:3 pages:294-302 http://linkinghub.elsevier.com/retrieve/pii/0167-4781(93)90127-Y GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1173 1993 3 294-302 |
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(DE-627)NLEJ186812574 (DE-599)GBVNLZ186812574 DE-627 ger DE-627 rakwb eng Conservation in sequence and affinity of human and rodent PDGF ligands and receptors 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Platelet-derived growth factor (PDGF) consists of two chains, PDGF-A and-B, which activate as homo- or heterodimers two receptors, α and β. To test PDGF function in vivo we have generated neutralizing monoclonal antibodies. When analyzed with rat PDGFs only antibodies raised against human PDGF-AA showed cross-species activity. This correlated with complete amino acid sequence conservation of PDGF-A whereas rat PDGF-B differed in six positions when cloned rat PDGF cDNAs were compared with their human homologs within the receptor binding region. Extracellular domains of cloned rat PDGF α- and β-receptor cDNAs did not reflect this difference in cross-species ligand conservation. When rat extracellular domains were expressed as soluble proteins they bound human PDGF-BB with high affinity after immobilization of the purified proteins on solid phase. Dissociation constants were identical to those of their human homologs. Thus, high affinity binding of human PDGF-BB to extracellular domains does not depend on species origin but only on receptor type. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Herren, B. oth Weyer, K.A. oth Rouge, M. oth Lotscher, P. oth Pech, M. oth in Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression Amsterdam : Elsevier 1173(1993), 3, Seite 294-302 (DE-627)NLEJ176932224 (DE-600)2209522-6 0167-4781 nnns volume:1173 year:1993 number:3 pages:294-302 http://linkinghub.elsevier.com/retrieve/pii/0167-4781(93)90127-Y GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1173 1993 3 294-302 |
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(DE-627)NLEJ186812574 (DE-599)GBVNLZ186812574 DE-627 ger DE-627 rakwb eng Conservation in sequence and affinity of human and rodent PDGF ligands and receptors 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Platelet-derived growth factor (PDGF) consists of two chains, PDGF-A and-B, which activate as homo- or heterodimers two receptors, α and β. To test PDGF function in vivo we have generated neutralizing monoclonal antibodies. When analyzed with rat PDGFs only antibodies raised against human PDGF-AA showed cross-species activity. This correlated with complete amino acid sequence conservation of PDGF-A whereas rat PDGF-B differed in six positions when cloned rat PDGF cDNAs were compared with their human homologs within the receptor binding region. Extracellular domains of cloned rat PDGF α- and β-receptor cDNAs did not reflect this difference in cross-species ligand conservation. When rat extracellular domains were expressed as soluble proteins they bound human PDGF-BB with high affinity after immobilization of the purified proteins on solid phase. Dissociation constants were identical to those of their human homologs. Thus, high affinity binding of human PDGF-BB to extracellular domains does not depend on species origin but only on receptor type. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Herren, B. oth Weyer, K.A. oth Rouge, M. oth Lotscher, P. oth Pech, M. oth in Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression Amsterdam : Elsevier 1173(1993), 3, Seite 294-302 (DE-627)NLEJ176932224 (DE-600)2209522-6 0167-4781 nnns volume:1173 year:1993 number:3 pages:294-302 http://linkinghub.elsevier.com/retrieve/pii/0167-4781(93)90127-Y GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1173 1993 3 294-302 |
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(DE-627)NLEJ186812574 (DE-599)GBVNLZ186812574 DE-627 ger DE-627 rakwb eng Conservation in sequence and affinity of human and rodent PDGF ligands and receptors 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Platelet-derived growth factor (PDGF) consists of two chains, PDGF-A and-B, which activate as homo- or heterodimers two receptors, α and β. To test PDGF function in vivo we have generated neutralizing monoclonal antibodies. When analyzed with rat PDGFs only antibodies raised against human PDGF-AA showed cross-species activity. This correlated with complete amino acid sequence conservation of PDGF-A whereas rat PDGF-B differed in six positions when cloned rat PDGF cDNAs were compared with their human homologs within the receptor binding region. Extracellular domains of cloned rat PDGF α- and β-receptor cDNAs did not reflect this difference in cross-species ligand conservation. When rat extracellular domains were expressed as soluble proteins they bound human PDGF-BB with high affinity after immobilization of the purified proteins on solid phase. Dissociation constants were identical to those of their human homologs. Thus, high affinity binding of human PDGF-BB to extracellular domains does not depend on species origin but only on receptor type. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Herren, B. oth Weyer, K.A. oth Rouge, M. oth Lotscher, P. oth Pech, M. oth in Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression Amsterdam : Elsevier 1173(1993), 3, Seite 294-302 (DE-627)NLEJ176932224 (DE-600)2209522-6 0167-4781 nnns volume:1173 year:1993 number:3 pages:294-302 http://linkinghub.elsevier.com/retrieve/pii/0167-4781(93)90127-Y GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1173 1993 3 294-302 |
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(DE-627)NLEJ186812574 (DE-599)GBVNLZ186812574 DE-627 ger DE-627 rakwb eng Conservation in sequence and affinity of human and rodent PDGF ligands and receptors 1993 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Platelet-derived growth factor (PDGF) consists of two chains, PDGF-A and-B, which activate as homo- or heterodimers two receptors, α and β. To test PDGF function in vivo we have generated neutralizing monoclonal antibodies. When analyzed with rat PDGFs only antibodies raised against human PDGF-AA showed cross-species activity. This correlated with complete amino acid sequence conservation of PDGF-A whereas rat PDGF-B differed in six positions when cloned rat PDGF cDNAs were compared with their human homologs within the receptor binding region. Extracellular domains of cloned rat PDGF α- and β-receptor cDNAs did not reflect this difference in cross-species ligand conservation. When rat extracellular domains were expressed as soluble proteins they bound human PDGF-BB with high affinity after immobilization of the purified proteins on solid phase. Dissociation constants were identical to those of their human homologs. Thus, high affinity binding of human PDGF-BB to extracellular domains does not depend on species origin but only on receptor type. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Herren, B. oth Weyer, K.A. oth Rouge, M. oth Lotscher, P. oth Pech, M. oth in Biochimica et Biophysica Acta (BBA)/Gene Structure and Expression Amsterdam : Elsevier 1173(1993), 3, Seite 294-302 (DE-627)NLEJ176932224 (DE-600)2209522-6 0167-4781 nnns volume:1173 year:1993 number:3 pages:294-302 http://linkinghub.elsevier.com/retrieve/pii/0167-4781(93)90127-Y GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 1173 1993 3 294-302 |
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conservation in sequence and affinity of human and rodent pdgf ligands and receptors |
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Conservation in sequence and affinity of human and rodent PDGF ligands and receptors |
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Platelet-derived growth factor (PDGF) consists of two chains, PDGF-A and-B, which activate as homo- or heterodimers two receptors, α and β. To test PDGF function in vivo we have generated neutralizing monoclonal antibodies. When analyzed with rat PDGFs only antibodies raised against human PDGF-AA showed cross-species activity. This correlated with complete amino acid sequence conservation of PDGF-A whereas rat PDGF-B differed in six positions when cloned rat PDGF cDNAs were compared with their human homologs within the receptor binding region. Extracellular domains of cloned rat PDGF α- and β-receptor cDNAs did not reflect this difference in cross-species ligand conservation. When rat extracellular domains were expressed as soluble proteins they bound human PDGF-BB with high affinity after immobilization of the purified proteins on solid phase. Dissociation constants were identical to those of their human homologs. Thus, high affinity binding of human PDGF-BB to extracellular domains does not depend on species origin but only on receptor type. |
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Platelet-derived growth factor (PDGF) consists of two chains, PDGF-A and-B, which activate as homo- or heterodimers two receptors, α and β. To test PDGF function in vivo we have generated neutralizing monoclonal antibodies. When analyzed with rat PDGFs only antibodies raised against human PDGF-AA showed cross-species activity. This correlated with complete amino acid sequence conservation of PDGF-A whereas rat PDGF-B differed in six positions when cloned rat PDGF cDNAs were compared with their human homologs within the receptor binding region. Extracellular domains of cloned rat PDGF α- and β-receptor cDNAs did not reflect this difference in cross-species ligand conservation. When rat extracellular domains were expressed as soluble proteins they bound human PDGF-BB with high affinity after immobilization of the purified proteins on solid phase. Dissociation constants were identical to those of their human homologs. Thus, high affinity binding of human PDGF-BB to extracellular domains does not depend on species origin but only on receptor type. |
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Platelet-derived growth factor (PDGF) consists of two chains, PDGF-A and-B, which activate as homo- or heterodimers two receptors, α and β. To test PDGF function in vivo we have generated neutralizing monoclonal antibodies. When analyzed with rat PDGFs only antibodies raised against human PDGF-AA showed cross-species activity. This correlated with complete amino acid sequence conservation of PDGF-A whereas rat PDGF-B differed in six positions when cloned rat PDGF cDNAs were compared with their human homologs within the receptor binding region. Extracellular domains of cloned rat PDGF α- and β-receptor cDNAs did not reflect this difference in cross-species ligand conservation. When rat extracellular domains were expressed as soluble proteins they bound human PDGF-BB with high affinity after immobilization of the purified proteins on solid phase. Dissociation constants were identical to those of their human homologs. Thus, high affinity binding of human PDGF-BB to extracellular domains does not depend on species origin but only on receptor type. |
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