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Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization
We have reported previously the isolation and preliminary characterization of a 40-kDa cyclosporin A (CsA)-binding protein, cyclophilin-40 (CyP-40). To determine the sequence of this protein, degenerate oligonucleotide primers based on bovine brain CyP-40 tryptic peptides were used to generate a pol...
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| Published in: | The Journal of biological chemistry 1993-06, Vol.268 (17), p.12303-12310 |
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| container_end_page | 12310 |
| container_issue | 17 |
| container_start_page | 12303 |
| container_title | The Journal of biological chemistry |
| container_volume | 268 |
| creator | KIEFFER, L. J SENG, T. W WEI LI OSTERMAN, D. G HANDSCHUMACHER, R. E BAYNEY, R. M |
| description | We have reported previously the isolation and preliminary characterization of a 40-kDa cyclosporin A (CsA)-binding protein,
cyclophilin-40 (CyP-40). To determine the sequence of this protein, degenerate oligonucleotide primers based on bovine brain
CyP-40 tryptic peptides were used to generate a polymerase chain reaction fragment of CyP-40 cDNA. This was used to isolate
the complete cDNA from a human pancreatic islet cell library. Northern analysis indicated ubiquitous distribution of CyP-40
mRNA throughout human tissues. The CyP-18 domain of CyP-40 is most similar to maize CyP (64.3% identity), whereas 150 amino
acids of the non-CyP-18 domain of CyP-40 share 30.7% identity with P59, a member of the steroid receptor complex. Failure
to detect glycosylation and mass spectroscopy with isolated CyP-40 indicate minimal, if any, posttranslational modification.
Employing a new assay for calcineurin protein phosphatase activity to compare the effects of CyP-40.CsA and CyP-18.CsA complexes,
IC50 values of 320 nM +/- 20 and 195 nM +/- 15, respectively, were obtained. A chemical cross-linking study revealed that
CyP-40 competes for 125I-CyP-18 binding to calcineurin in the presence of CsA. The homology of CyP-40 to P59 suggests that
CyP-40 might be involved in modulating the activity of biologically important receptors. |
| doi_str_mv | 10.1016/S0021-9258(18)31389-9 |
| format | article |
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cyclophilin-40 (CyP-40). To determine the sequence of this protein, degenerate oligonucleotide primers based on bovine brain
CyP-40 tryptic peptides were used to generate a polymerase chain reaction fragment of CyP-40 cDNA. This was used to isolate
the complete cDNA from a human pancreatic islet cell library. Northern analysis indicated ubiquitous distribution of CyP-40
mRNA throughout human tissues. The CyP-18 domain of CyP-40 is most similar to maize CyP (64.3% identity), whereas 150 amino
acids of the non-CyP-18 domain of CyP-40 share 30.7% identity with P59, a member of the steroid receptor complex. Failure
to detect glycosylation and mass spectroscopy with isolated CyP-40 indicate minimal, if any, posttranslational modification.
Employing a new assay for calcineurin protein phosphatase activity to compare the effects of CyP-40.CsA and CyP-18.CsA complexes,
IC50 values of 320 nM +/- 20 and 195 nM +/- 15, respectively, were obtained. A chemical cross-linking study revealed that
CyP-40 competes for 125I-CyP-18 binding to calcineurin in the presence of CsA. The homology of CyP-40 to P59 suggests that
CyP-40 might be involved in modulating the activity of biologically important receptors.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)31389-9</identifier><identifier>PMID: 8509368</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Isomerases - chemistry ; Amino Acid Isomerases - genetics ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Base Sequence ; Binding and carrier proteins ; Biological and medical sciences ; Brain - metabolism ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Cattle ; cDNA ; Cloning, Molecular ; cyclophilin-40 ; Cyclophilins ; Cyclosporine - metabolism ; DNA ; Fundamental and applied biological sciences. Psychology ; genes ; homology ; Humans ; man ; Molecular Sequence Data ; nucleotide sequence ; Oligodeoxyribonucleotides ; P59 component ; pancreas ; Pancreas - metabolism ; Peptidyl-Prolyl Isomerase F ; Peptidylprolyl Isomerase ; Proteins ; receptors ; Receptors, Steroid - chemistry ; Sequence Homology, Amino Acid ; steroids</subject><ispartof>The Journal of biological chemistry, 1993-06, Vol.268 (17), p.12303-12310</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-c1392f6e34a941736b98419ef7ace1b9a62786519d989f28d55b6cb28c998e6d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4820538$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8509368$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KIEFFER, L. J</creatorcontrib><creatorcontrib>SENG, T. W</creatorcontrib><creatorcontrib>WEI LI</creatorcontrib><creatorcontrib>OSTERMAN, D. G</creatorcontrib><creatorcontrib>HANDSCHUMACHER, R. E</creatorcontrib><creatorcontrib>BAYNEY, R. M</creatorcontrib><title>Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>We have reported previously the isolation and preliminary characterization of a 40-kDa cyclosporin A (CsA)-binding protein,
cyclophilin-40 (CyP-40). To determine the sequence of this protein, degenerate oligonucleotide primers based on bovine brain
CyP-40 tryptic peptides were used to generate a polymerase chain reaction fragment of CyP-40 cDNA. This was used to isolate
the complete cDNA from a human pancreatic islet cell library. Northern analysis indicated ubiquitous distribution of CyP-40
mRNA throughout human tissues. The CyP-18 domain of CyP-40 is most similar to maize CyP (64.3% identity), whereas 150 amino
acids of the non-CyP-18 domain of CyP-40 share 30.7% identity with P59, a member of the steroid receptor complex. Failure
to detect glycosylation and mass spectroscopy with isolated CyP-40 indicate minimal, if any, posttranslational modification.
Employing a new assay for calcineurin protein phosphatase activity to compare the effects of CyP-40.CsA and CyP-18.CsA complexes,
IC50 values of 320 nM +/- 20 and 195 nM +/- 15, respectively, were obtained. A chemical cross-linking study revealed that
CyP-40 competes for 125I-CyP-18 binding to calcineurin in the presence of CsA. The homology of CyP-40 to P59 suggests that
CyP-40 might be involved in modulating the activity of biologically important receptors.</description><subject>Amino Acid Isomerases - chemistry</subject><subject>Amino Acid Isomerases - genetics</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Brain - metabolism</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Cattle</subject><subject>cDNA</subject><subject>Cloning, Molecular</subject><subject>cyclophilin-40</subject><subject>Cyclophilins</subject><subject>Cyclosporine - metabolism</subject><subject>DNA</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>homology</subject><subject>Humans</subject><subject>man</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequence</subject><subject>Oligodeoxyribonucleotides</subject><subject>P59 component</subject><subject>pancreas</subject><subject>Pancreas - metabolism</subject><subject>Peptidyl-Prolyl Isomerase F</subject><subject>Peptidylprolyl Isomerase</subject><subject>Proteins</subject><subject>receptors</subject><subject>Receptors, Steroid - chemistry</subject><subject>Sequence Homology, Amino Acid</subject><subject>steroids</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><recordid>eNqFkd1uFCEYhonR1G31EppwYIxNnMrPwMBhs_4mjZqoiWeEYZgdDANTYFPXi_Capdt145mcEPielzfkAeAco0uMMH_1BSGCG0mYeIHFBcVUyEY-ACuMBG0ow98fgtUReQxOc_6B6molPgEngiFJuViB3-ud8XGZnHehadFLqOGSYrEuwFtXJjjFOfq42cESYZks_MwkNHFeYrChwDjuL3OxKboBJmvsUmLaE97-vIRrH4MLm7-gef3xCuowwHGb6rmCk07a1Lj7pYuL4Ql4NGqf7dPDfga-vX3zdf2-uf707sP66roxbYtKYzCVZOSWtlq2uKO8l6LF0o6dNhb3UnPSCc6wHKSQIxEDYz03PRFGSmH5QM_A8_t362dvtjYXNbtsrPc62LjNqmOd6Cgi_wUx57WCoAqye9CkmHOyo1qSm3XaKYzUnTC1F6bubCgs1F6YkjV3fijY9rMdjqmDoTp_dpjrbLQfkw7G5SPWCoIY_Qeb3Ga6dcmq3kUz2VkRXvs6hQlFlP4BP7KqGA</recordid><startdate>19930615</startdate><enddate>19930615</enddate><creator>KIEFFER, L. 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M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-c1392f6e34a941736b98419ef7ace1b9a62786519d989f28d55b6cb28c998e6d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Isomerases - chemistry</topic><topic>Amino Acid Isomerases - genetics</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>Brain - metabolism</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - genetics</topic><topic>Cattle</topic><topic>cDNA</topic><topic>Cloning, Molecular</topic><topic>cyclophilin-40</topic><topic>Cyclophilins</topic><topic>Cyclosporine - metabolism</topic><topic>DNA</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>homology</topic><topic>Humans</topic><topic>man</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequence</topic><topic>Oligodeoxyribonucleotides</topic><topic>P59 component</topic><topic>pancreas</topic><topic>Pancreas - metabolism</topic><topic>Peptidyl-Prolyl Isomerase F</topic><topic>Peptidylprolyl Isomerase</topic><topic>Proteins</topic><topic>receptors</topic><topic>Receptors, Steroid - chemistry</topic><topic>Sequence Homology, Amino Acid</topic><topic>steroids</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KIEFFER, L. J</creatorcontrib><creatorcontrib>SENG, T. W</creatorcontrib><creatorcontrib>WEI LI</creatorcontrib><creatorcontrib>OSTERMAN, D. G</creatorcontrib><creatorcontrib>HANDSCHUMACHER, R. E</creatorcontrib><creatorcontrib>BAYNEY, R. 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M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1993-06-15</date><risdate>1993</risdate><volume>268</volume><issue>17</issue><spage>12303</spage><epage>12310</epage><pages>12303-12310</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have reported previously the isolation and preliminary characterization of a 40-kDa cyclosporin A (CsA)-binding protein,
cyclophilin-40 (CyP-40). To determine the sequence of this protein, degenerate oligonucleotide primers based on bovine brain
CyP-40 tryptic peptides were used to generate a polymerase chain reaction fragment of CyP-40 cDNA. This was used to isolate
the complete cDNA from a human pancreatic islet cell library. Northern analysis indicated ubiquitous distribution of CyP-40
mRNA throughout human tissues. The CyP-18 domain of CyP-40 is most similar to maize CyP (64.3% identity), whereas 150 amino
acids of the non-CyP-18 domain of CyP-40 share 30.7% identity with P59, a member of the steroid receptor complex. Failure
to detect glycosylation and mass spectroscopy with isolated CyP-40 indicate minimal, if any, posttranslational modification.
Employing a new assay for calcineurin protein phosphatase activity to compare the effects of CyP-40.CsA and CyP-18.CsA complexes,
IC50 values of 320 nM +/- 20 and 195 nM +/- 15, respectively, were obtained. A chemical cross-linking study revealed that
CyP-40 competes for 125I-CyP-18 binding to calcineurin in the presence of CsA. The homology of CyP-40 to P59 suggests that
CyP-40 might be involved in modulating the activity of biologically important receptors.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>8509368</pmid><doi>10.1016/S0021-9258(18)31389-9</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1993-06, Vol.268 (17), p.12303-12310 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75787302 |
| source | ScienceDirect Journals |
| subjects | Amino Acid Isomerases - chemistry Amino Acid Isomerases - genetics Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Base Sequence Binding and carrier proteins Biological and medical sciences Brain - metabolism Carrier Proteins - chemistry Carrier Proteins - genetics Cattle cDNA Cloning, Molecular cyclophilin-40 Cyclophilins Cyclosporine - metabolism DNA Fundamental and applied biological sciences. Psychology genes homology Humans man Molecular Sequence Data nucleotide sequence Oligodeoxyribonucleotides P59 component pancreas Pancreas - metabolism Peptidyl-Prolyl Isomerase F Peptidylprolyl Isomerase Proteins receptors Receptors, Steroid - chemistry Sequence Homology, Amino Acid steroids |
| title | Cyclophilin-40, a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterization |
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