Caspase-3 and -6 expression and enzyme activity in hen granulosa cells
We have cloned and sequenced cDNAs corresponding to the complete coding regions of the chicken homologues to mammalian caspase-3 and caspase-6. Both caspases are included among members of the cysteine protease (caspase) family that are most closely identified with mediating apoptosis. The deduced am...
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| Veröffentlicht in: | Biology of reproduction 2000-03, Vol.62 (3), p.589-598 |
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| creator | Johnson, A.L Bridgham, J.T |
| description | We have cloned and sequenced cDNAs corresponding to the complete coding regions of the chicken homologues to mammalian caspase-3
and caspase-6. Both caspases are included among members of the cysteine protease (caspase) family that are most closely identified
with mediating apoptosis. The deduced amino acid sequences for chicken caspase-3 and -6 show 65% and 68% identity with the
respective human sequences, with complete conservation found within the QACRG active peptide region. Both caspase-3 and -6
are widely expressed within various tissues from the hen. Within the ovary, levels of caspase-3 and caspase-6 mRNA and protein
do not change significantly in theca tissue during follicle development. On the other hand, procaspase-3 and -6 protein levels
are elevated by 2- to 5-fold in preovulatory, compared to prehierarchal (6- to 8-mm diameter), follicle granulosa cells. Nevertheless,
the function of this family of cell death-inducing proteins requires activation of the proenzyme caspase, which occurs after
cleavage at predictable sites within the N-terminal domain. Accordingly, it was determined that okadaic acid, a pharmacologic
inducer of apoptotic cell death in cultured apoptosis-resistant, preovulatory follicle granulosa cells, induced both caspase-3-
and caspase-6-like activity within 8â16 h of treatment. By comparison, spontaneous apoptotic cell death that occurs in apoptosis-sensitive,
prehierarchal follicle granulosa cells after short-term suspension culture is accompanied by a more rapid increase (within
2 h) in both caspase-3- and -6-like activity. Treatment with 8-bromo-cAMP, which has previously been shown to attenuate, or
at least slow, the onset of apoptosis in prehierarchal follicle granulosa cells, mitigates this suspension culture-induced
increase in caspase activity. While the present results provide further support for the relationship between caspase activation
and apoptotic cell death in hen granulosa cells, the molecular ordering of enzymatic events and the caspase-specific substrates
remain to be elucidated. |
| doi_str_mv | 10.1095/biolreprod62.3.589 |
| format | Article |
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and caspase-6. Both caspases are included among members of the cysteine protease (caspase) family that are most closely identified
with mediating apoptosis. The deduced amino acid sequences for chicken caspase-3 and -6 show 65% and 68% identity with the
respective human sequences, with complete conservation found within the QACRG active peptide region. Both caspase-3 and -6
are widely expressed within various tissues from the hen. Within the ovary, levels of caspase-3 and caspase-6 mRNA and protein
do not change significantly in theca tissue during follicle development. On the other hand, procaspase-3 and -6 protein levels
are elevated by 2- to 5-fold in preovulatory, compared to prehierarchal (6- to 8-mm diameter), follicle granulosa cells. Nevertheless,
the function of this family of cell death-inducing proteins requires activation of the proenzyme caspase, which occurs after
cleavage at predictable sites within the N-terminal domain. Accordingly, it was determined that okadaic acid, a pharmacologic
inducer of apoptotic cell death in cultured apoptosis-resistant, preovulatory follicle granulosa cells, induced both caspase-3-
and caspase-6-like activity within 8â16 h of treatment. By comparison, spontaneous apoptotic cell death that occurs in apoptosis-sensitive,
prehierarchal follicle granulosa cells after short-term suspension culture is accompanied by a more rapid increase (within
2 h) in both caspase-3- and -6-like activity. Treatment with 8-bromo-cAMP, which has previously been shown to attenuate, or
at least slow, the onset of apoptosis in prehierarchal follicle granulosa cells, mitigates this suspension culture-induced
increase in caspase activity. While the present results provide further support for the relationship between caspase activation
and apoptotic cell death in hen granulosa cells, the molecular ordering of enzymatic events and the caspase-specific substrates
remain to be elucidated.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1095/biolreprod62.3.589</identifier><identifier>PMID: 10684799</identifier><identifier>CODEN: BIREBV</identifier><language>eng</language><publisher>Madison, WI: Society for the Study of Reproduction</publisher><subject>8-Bromo Cyclic Adenosine Monophosphate - pharmacology ; 8-bromo-c-amp ; Amino Acid Sequence ; amino acid sequences ; Animals ; apoptosis ; Biological and medical sciences ; Blotting, Northern ; Caspase 3 ; Caspase 6 ; Caspase Inhibitors ; Caspases - genetics ; Caspases - metabolism ; Chickens - genetics ; Cloning, Molecular ; complementary DNA ; cyclic AMP ; Cysteine Proteinase Inhibitors - pharmacology ; cysteine proteinases ; enzyme activity ; enzyme inhibitors ; Female ; Fundamental and applied biological sciences. Psychology ; genbank/af082329 ; gene expression ; Gene Expression Regulation ; granulosa cells ; Granulosa Cells - drug effects ; Granulosa Cells - enzymology ; hens ; Humans ; messenger RNA ; Molecular Sequence Data ; Non mammalian vertebrate reproduction ; nucleotide sequences ; okadaic acid ; Okadaic Acid - pharmacology ; Oligopeptides - pharmacology ; ovarian follicles ; Ovulation ; prehierarchical follicles ; preovulatory follicles ; regulation ; RNA, Messenger ; Sequence Homology, Amino Acid ; Sequence Homology, Nucleic Acid ; Theca Cells - enzymology ; thecal cells ; Vertebrates: reproduction</subject><ispartof>Biology of reproduction, 2000-03, Vol.62 (3), p.589-598</ispartof><rights>2000 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></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=1288891$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10684799$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Johnson, A.L</creatorcontrib><creatorcontrib>Bridgham, J.T</creatorcontrib><title>Caspase-3 and -6 expression and enzyme activity in hen granulosa cells</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>We have cloned and sequenced cDNAs corresponding to the complete coding regions of the chicken homologues to mammalian caspase-3
and caspase-6. Both caspases are included among members of the cysteine protease (caspase) family that are most closely identified
with mediating apoptosis. The deduced amino acid sequences for chicken caspase-3 and -6 show 65% and 68% identity with the
respective human sequences, with complete conservation found within the QACRG active peptide region. Both caspase-3 and -6
are widely expressed within various tissues from the hen. Within the ovary, levels of caspase-3 and caspase-6 mRNA and protein
do not change significantly in theca tissue during follicle development. On the other hand, procaspase-3 and -6 protein levels
are elevated by 2- to 5-fold in preovulatory, compared to prehierarchal (6- to 8-mm diameter), follicle granulosa cells. Nevertheless,
the function of this family of cell death-inducing proteins requires activation of the proenzyme caspase, which occurs after
cleavage at predictable sites within the N-terminal domain. Accordingly, it was determined that okadaic acid, a pharmacologic
inducer of apoptotic cell death in cultured apoptosis-resistant, preovulatory follicle granulosa cells, induced both caspase-3-
and caspase-6-like activity within 8â16 h of treatment. By comparison, spontaneous apoptotic cell death that occurs in apoptosis-sensitive,
prehierarchal follicle granulosa cells after short-term suspension culture is accompanied by a more rapid increase (within
2 h) in both caspase-3- and -6-like activity. Treatment with 8-bromo-cAMP, which has previously been shown to attenuate, or
at least slow, the onset of apoptosis in prehierarchal follicle granulosa cells, mitigates this suspension culture-induced
increase in caspase activity. While the present results provide further support for the relationship between caspase activation
and apoptotic cell death in hen granulosa cells, the molecular ordering of enzymatic events and the caspase-specific substrates
remain to be elucidated.</description><subject>8-Bromo Cyclic Adenosine Monophosphate - pharmacology</subject><subject>8-bromo-c-amp</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Animals</subject><subject>apoptosis</subject><subject>Biological and medical sciences</subject><subject>Blotting, Northern</subject><subject>Caspase 3</subject><subject>Caspase 6</subject><subject>Caspase Inhibitors</subject><subject>Caspases - genetics</subject><subject>Caspases - metabolism</subject><subject>Chickens - genetics</subject><subject>Cloning, Molecular</subject><subject>complementary DNA</subject><subject>cyclic AMP</subject><subject>Cysteine Proteinase Inhibitors - pharmacology</subject><subject>cysteine proteinases</subject><subject>enzyme activity</subject><subject>enzyme inhibitors</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genbank/af082329</subject><subject>gene expression</subject><subject>Gene Expression Regulation</subject><subject>granulosa cells</subject><subject>Granulosa Cells - drug effects</subject><subject>Granulosa Cells - enzymology</subject><subject>hens</subject><subject>Humans</subject><subject>messenger RNA</subject><subject>Molecular Sequence Data</subject><subject>Non mammalian vertebrate reproduction</subject><subject>nucleotide sequences</subject><subject>okadaic acid</subject><subject>Okadaic Acid - pharmacology</subject><subject>Oligopeptides - pharmacology</subject><subject>ovarian follicles</subject><subject>Ovulation</subject><subject>prehierarchical follicles</subject><subject>preovulatory follicles</subject><subject>regulation</subject><subject>RNA, Messenger</subject><subject>Sequence Homology, Amino Acid</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Theca Cells - enzymology</subject><subject>thecal cells</subject><subject>Vertebrates: reproduction</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpF0E1LAzEQBuAgiq3VP-BBc9Dj1kmymyZHKVaFggftecnmo41kP0iqa_31LrbiaWB4eHlnELokMCUgi7vKtyHaLraG0ymbFkIeoTEpqMxmlItjNAYAnjHG2QidpfQOQHJG2SkaEeAin0k5Rou5Sp1KNmNYNQZnHNuvLtqUfNv8bmzzvastVnrrP_12h32DN7bB66iaj9AmhbUNIZ2jE6dCsheHOUGrxcPb_Clbvjw-z--XmaMSthl1IBxwOwNNjQBhBdMCqHacidyBrBzNjRFaOMdzWlk7k0QSYYA4AwwEm6CrfW73UdXWlF30tYq78u-gAdwcgEpaBTfU1D79OyqEkGRgt3u28etN76MtU61CGFJZ2fc9pyUrh38O7nrvnGpLtY5D1OqVAmFAZUEkK9gPI81xbA</recordid><startdate>20000301</startdate><enddate>20000301</enddate><creator>Johnson, A.L</creator><creator>Bridgham, J.T</creator><general>Society for the Study of Reproduction</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>20000301</creationdate><title>Caspase-3 and -6 expression and enzyme activity in hen granulosa cells</title><author>Johnson, A.L ; Bridgham, J.T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f290t-2f08f06e70c2d808e83c802cf6384f09bf24dd8c8ff642bee791918d01fd03083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>8-Bromo Cyclic Adenosine Monophosphate - pharmacology</topic><topic>8-bromo-c-amp</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Animals</topic><topic>apoptosis</topic><topic>Biological and medical sciences</topic><topic>Blotting, Northern</topic><topic>Caspase 3</topic><topic>Caspase 6</topic><topic>Caspase Inhibitors</topic><topic>Caspases - genetics</topic><topic>Caspases - metabolism</topic><topic>Chickens - genetics</topic><topic>Cloning, Molecular</topic><topic>complementary DNA</topic><topic>cyclic AMP</topic><topic>Cysteine Proteinase Inhibitors - pharmacology</topic><topic>cysteine proteinases</topic><topic>enzyme activity</topic><topic>enzyme inhibitors</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genbank/af082329</topic><topic>gene expression</topic><topic>Gene Expression Regulation</topic><topic>granulosa cells</topic><topic>Granulosa Cells - drug effects</topic><topic>Granulosa Cells - enzymology</topic><topic>hens</topic><topic>Humans</topic><topic>messenger RNA</topic><topic>Molecular Sequence Data</topic><topic>Non mammalian vertebrate reproduction</topic><topic>nucleotide sequences</topic><topic>okadaic acid</topic><topic>Okadaic Acid - pharmacology</topic><topic>Oligopeptides - pharmacology</topic><topic>ovarian follicles</topic><topic>Ovulation</topic><topic>prehierarchical follicles</topic><topic>preovulatory follicles</topic><topic>regulation</topic><topic>RNA, Messenger</topic><topic>Sequence Homology, Amino Acid</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Theca Cells - enzymology</topic><topic>thecal cells</topic><topic>Vertebrates: reproduction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Johnson, A.L</creatorcontrib><creatorcontrib>Bridgham, J.T</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Johnson, A.L</au><au>Bridgham, J.T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Caspase-3 and -6 expression and enzyme activity in hen granulosa cells</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>2000-03-01</date><risdate>2000</risdate><volume>62</volume><issue>3</issue><spage>589</spage><epage>598</epage><pages>589-598</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><coden>BIREBV</coden><abstract>We have cloned and sequenced cDNAs corresponding to the complete coding regions of the chicken homologues to mammalian caspase-3
and caspase-6. Both caspases are included among members of the cysteine protease (caspase) family that are most closely identified
with mediating apoptosis. The deduced amino acid sequences for chicken caspase-3 and -6 show 65% and 68% identity with the
respective human sequences, with complete conservation found within the QACRG active peptide region. Both caspase-3 and -6
are widely expressed within various tissues from the hen. Within the ovary, levels of caspase-3 and caspase-6 mRNA and protein
do not change significantly in theca tissue during follicle development. On the other hand, procaspase-3 and -6 protein levels
are elevated by 2- to 5-fold in preovulatory, compared to prehierarchal (6- to 8-mm diameter), follicle granulosa cells. Nevertheless,
the function of this family of cell death-inducing proteins requires activation of the proenzyme caspase, which occurs after
cleavage at predictable sites within the N-terminal domain. Accordingly, it was determined that okadaic acid, a pharmacologic
inducer of apoptotic cell death in cultured apoptosis-resistant, preovulatory follicle granulosa cells, induced both caspase-3-
and caspase-6-like activity within 8â16 h of treatment. By comparison, spontaneous apoptotic cell death that occurs in apoptosis-sensitive,
prehierarchal follicle granulosa cells after short-term suspension culture is accompanied by a more rapid increase (within
2 h) in both caspase-3- and -6-like activity. Treatment with 8-bromo-cAMP, which has previously been shown to attenuate, or
at least slow, the onset of apoptosis in prehierarchal follicle granulosa cells, mitigates this suspension culture-induced
increase in caspase activity. While the present results provide further support for the relationship between caspase activation
and apoptotic cell death in hen granulosa cells, the molecular ordering of enzymatic events and the caspase-specific substrates
remain to be elucidated.</abstract><cop>Madison, WI</cop><pub>Society for the Study of Reproduction</pub><pmid>10684799</pmid><doi>10.1095/biolreprod62.3.589</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biology of reproduction, 2000-03, Vol.62 (3), p.589-598 |
| issn | 0006-3363 1529-7268 |
| language | eng |
| recordid | cdi_pubmed_primary_10684799 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; BioOne Complete; Oxford University Press Journals All Titles (1996-Current) |
| subjects | 8-Bromo Cyclic Adenosine Monophosphate - pharmacology 8-bromo-c-amp Amino Acid Sequence amino acid sequences Animals apoptosis Biological and medical sciences Blotting, Northern Caspase 3 Caspase 6 Caspase Inhibitors Caspases - genetics Caspases - metabolism Chickens - genetics Cloning, Molecular complementary DNA cyclic AMP Cysteine Proteinase Inhibitors - pharmacology cysteine proteinases enzyme activity enzyme inhibitors Female Fundamental and applied biological sciences. Psychology genbank/af082329 gene expression Gene Expression Regulation granulosa cells Granulosa Cells - drug effects Granulosa Cells - enzymology hens Humans messenger RNA Molecular Sequence Data Non mammalian vertebrate reproduction nucleotide sequences okadaic acid Okadaic Acid - pharmacology Oligopeptides - pharmacology ovarian follicles Ovulation prehierarchical follicles preovulatory follicles regulation RNA, Messenger Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid Theca Cells - enzymology thecal cells Vertebrates: reproduction |
| title | Caspase-3 and -6 expression and enzyme activity in hen granulosa cells |
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