Eintrag weiter verarbeiten
Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments
Gespeichert in:
| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , |
| In: | European Journal of Biochemistry, 238, 1996, 3, S. 613-622 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Kutuzov, Mikhail A. Bennett, Nelly Kutuzov, Mikhail A. Bennett, Nelly |
|---|---|
| author |
Kutuzov, Mikhail A. Bennett, Nelly |
| spellingShingle |
Kutuzov, Mikhail A. Bennett, Nelly European Journal of Biochemistry Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments Biochemistry |
| author_sort |
kutuzov, mikhail a. |
| spelling |
Kutuzov, Mikhail A. Bennett, Nelly 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1996.0613w.x <jats:p>We describe the presence in bovine retinal rod outer segments of a phosphatase which dephosphorylates phosphoopsin with an efficiency similar to that of PP2A, and which is stimulated by submicromolar levels of Ca<jats:sup>2+</jats:sup> (half‐maximal activation, 0.4–0.5 μM). This enzyme is designated Ca<jats:sup>2+</jats:sup>‐activated opsin phosphatase (CAOP). CAOP has a molecular mass of 70–75 kDa as determined by gel filtration on Superose 12 and exhibits reversible Ca<jats:sup>2+</jats:sup>‐dependent oligomerization. An unidentified protein of approximately 25 kDa is necessary for full activity of CAOP and for cooperative binding of Ca<jats:sup>2+</jats:sup> (<jats:italic>h</jats:italic> > 2). CAOP does not require Mg<jats:sup>2+</jats:sup> and is inhibited by okadaic acid (median inhibitory concentration > 25 μM), which suggests that it is related to the PP1/2A/2B class of protein phosphatases. Like PP2B, CAOP is inhibited by trifluoperazine (median inhibitory concentration 40 μM), but calmodulin has no effect on CAOP activity, and CAOP is inhibited by mastoparan at much higher concentrations than PP2B. This combination of properties suggests that CAOP is not identical to any characterized protein phosphatase. Since the cytoplasmic concentration of Ca<jats:sup>2+</jats:sup> in, retinal rod outer segments is reduced upon excitation by light, the existence of a Ca<jats:sup>2+</jats:sup>‐sensitive opsin phosphatase activity suggests that light‐dependent Ca<jats:sup>2+</jats:sup> levels may control rhodopsin dephosphorylation.</jats:p> Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments European Journal of Biochemistry |
| doi_str_mv |
10.1111/j.1432-1033.1996.0613w.x |
| facet_avail |
Online Free |
| finc_class_facet |
Chemie und Pharmazie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4xOTk2LjA2MTN3Lng |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4xOTk2LjA2MTN3Lng |
| institution |
DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Rs1 DE-Pl11 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 |
| imprint |
Wiley, 1996 |
| imprint_str_mv |
Wiley, 1996 |
| issn |
0014-2956 1432-1033 |
| issn_str_mv |
0014-2956 1432-1033 |
| language |
English |
| mega_collection |
Wiley (CrossRef) |
| match_str |
kutuzov1996calciumactivatedopsinphosphataseactivityinretinalrodoutersegments |
| publishDateSort |
1996 |
| publisher |
Wiley |
| recordtype |
ai |
| record_format |
ai |
| series |
European Journal of Biochemistry |
| source_id |
49 |
| title |
Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_unstemmed |
Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_full |
Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_fullStr |
Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_full_unstemmed |
Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_short |
Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_sort |
calcium‐activated opsin phosphatase activity in retinal rod outer segments |
| topic |
Biochemistry |
| url |
http://dx.doi.org/10.1111/j.1432-1033.1996.0613w.x |
| publishDate |
1996 |
| physical |
613-622 |
| description |
<jats:p>We describe the presence in bovine retinal rod outer segments of a phosphatase which dephosphorylates phosphoopsin with an efficiency similar to that of PP2A, and which is stimulated by submicromolar levels of Ca<jats:sup>2+</jats:sup> (half‐maximal activation, 0.4–0.5 μM). This enzyme is designated Ca<jats:sup>2+</jats:sup>‐activated opsin phosphatase (CAOP). CAOP has a molecular mass of 70–75 kDa as determined by gel filtration on Superose 12 and exhibits reversible Ca<jats:sup>2+</jats:sup>‐dependent oligomerization. An unidentified protein of approximately 25 kDa is necessary for full activity of CAOP and for cooperative binding of Ca<jats:sup>2+</jats:sup> (<jats:italic>h</jats:italic> > 2). CAOP does not require Mg<jats:sup>2+</jats:sup> and is inhibited by okadaic acid (median inhibitory concentration > 25 μM), which suggests that it is related to the PP1/2A/2B class of protein phosphatases. Like PP2B, CAOP is inhibited by trifluoperazine (median inhibitory concentration 40 μM), but calmodulin has no effect on CAOP activity, and CAOP is inhibited by mastoparan at much higher concentrations than PP2B. This combination of properties suggests that CAOP is not identical to any characterized protein phosphatase. Since the cytoplasmic concentration of Ca<jats:sup>2+</jats:sup> in, retinal rod outer segments is reduced upon excitation by light, the existence of a Ca<jats:sup>2+</jats:sup>‐sensitive opsin phosphatase activity suggests that light‐dependent Ca<jats:sup>2+</jats:sup> levels may control rhodopsin dephosphorylation.</jats:p> |
| container_issue |
3 |
| container_start_page |
613 |
| container_title |
European Journal of Biochemistry |
| container_volume |
238 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792336108025020417 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T14:54:44.602Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Calcium%E2%80%90activated+Opsin+Phosphatase+Activity+in+Retinal+Rod+Outer+Segments&rft.date=1996-06-01&genre=article&issn=1432-1033&volume=238&issue=3&spage=613&epage=622&pages=613-622&jtitle=European+Journal+of+Biochemistry&atitle=Calcium%E2%80%90activated+Opsin+Phosphatase+Activity+in+Retinal+Rod+Outer+Segments&aulast=Bennett&aufirst=Nelly&rft_id=info%3Adoi%2F10.1111%2Fj.1432-1033.1996.0613w.x&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792336108025020417 |
| author | Kutuzov, Mikhail A., Bennett, Nelly |
| author_facet | Kutuzov, Mikhail A., Bennett, Nelly, Kutuzov, Mikhail A., Bennett, Nelly |
| author_sort | kutuzov, mikhail a. |
| container_issue | 3 |
| container_start_page | 613 |
| container_title | European Journal of Biochemistry |
| container_volume | 238 |
| description | <jats:p>We describe the presence in bovine retinal rod outer segments of a phosphatase which dephosphorylates phosphoopsin with an efficiency similar to that of PP2A, and which is stimulated by submicromolar levels of Ca<jats:sup>2+</jats:sup> (half‐maximal activation, 0.4–0.5 μM). This enzyme is designated Ca<jats:sup>2+</jats:sup>‐activated opsin phosphatase (CAOP). CAOP has a molecular mass of 70–75 kDa as determined by gel filtration on Superose 12 and exhibits reversible Ca<jats:sup>2+</jats:sup>‐dependent oligomerization. An unidentified protein of approximately 25 kDa is necessary for full activity of CAOP and for cooperative binding of Ca<jats:sup>2+</jats:sup> (<jats:italic>h</jats:italic> > 2). CAOP does not require Mg<jats:sup>2+</jats:sup> and is inhibited by okadaic acid (median inhibitory concentration > 25 μM), which suggests that it is related to the PP1/2A/2B class of protein phosphatases. Like PP2B, CAOP is inhibited by trifluoperazine (median inhibitory concentration 40 μM), but calmodulin has no effect on CAOP activity, and CAOP is inhibited by mastoparan at much higher concentrations than PP2B. This combination of properties suggests that CAOP is not identical to any characterized protein phosphatase. Since the cytoplasmic concentration of Ca<jats:sup>2+</jats:sup> in, retinal rod outer segments is reduced upon excitation by light, the existence of a Ca<jats:sup>2+</jats:sup>‐sensitive opsin phosphatase activity suggests that light‐dependent Ca<jats:sup>2+</jats:sup> levels may control rhodopsin dephosphorylation.</jats:p> |
| doi_str_mv | 10.1111/j.1432-1033.1996.0613w.x |
| facet_avail | Online, Free |
| finc_class_facet | Chemie und Pharmazie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4xOTk2LjA2MTN3Lng |
| imprint | Wiley, 1996 |
| imprint_str_mv | Wiley, 1996 |
| institution | DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Rs1, DE-Pl11, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1 |
| issn | 0014-2956, 1432-1033 |
| issn_str_mv | 0014-2956, 1432-1033 |
| language | English |
| last_indexed | 2024-03-01T14:54:44.602Z |
| match_str | kutuzov1996calciumactivatedopsinphosphataseactivityinretinalrodoutersegments |
| mega_collection | Wiley (CrossRef) |
| physical | 613-622 |
| publishDate | 1996 |
| publishDateSort | 1996 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | European Journal of Biochemistry |
| source_id | 49 |
| spelling | Kutuzov, Mikhail A. Bennett, Nelly 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1996.0613w.x <jats:p>We describe the presence in bovine retinal rod outer segments of a phosphatase which dephosphorylates phosphoopsin with an efficiency similar to that of PP2A, and which is stimulated by submicromolar levels of Ca<jats:sup>2+</jats:sup> (half‐maximal activation, 0.4–0.5 μM). This enzyme is designated Ca<jats:sup>2+</jats:sup>‐activated opsin phosphatase (CAOP). CAOP has a molecular mass of 70–75 kDa as determined by gel filtration on Superose 12 and exhibits reversible Ca<jats:sup>2+</jats:sup>‐dependent oligomerization. An unidentified protein of approximately 25 kDa is necessary for full activity of CAOP and for cooperative binding of Ca<jats:sup>2+</jats:sup> (<jats:italic>h</jats:italic> > 2). CAOP does not require Mg<jats:sup>2+</jats:sup> and is inhibited by okadaic acid (median inhibitory concentration > 25 μM), which suggests that it is related to the PP1/2A/2B class of protein phosphatases. Like PP2B, CAOP is inhibited by trifluoperazine (median inhibitory concentration 40 μM), but calmodulin has no effect on CAOP activity, and CAOP is inhibited by mastoparan at much higher concentrations than PP2B. This combination of properties suggests that CAOP is not identical to any characterized protein phosphatase. Since the cytoplasmic concentration of Ca<jats:sup>2+</jats:sup> in, retinal rod outer segments is reduced upon excitation by light, the existence of a Ca<jats:sup>2+</jats:sup>‐sensitive opsin phosphatase activity suggests that light‐dependent Ca<jats:sup>2+</jats:sup> levels may control rhodopsin dephosphorylation.</jats:p> Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments European Journal of Biochemistry |
| spellingShingle | Kutuzov, Mikhail A., Bennett, Nelly, European Journal of Biochemistry, Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments, Biochemistry |
| title | Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_full | Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_fullStr | Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_full_unstemmed | Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_short | Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| title_sort | calcium‐activated opsin phosphatase activity in retinal rod outer segments |
| title_unstemmed | Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1111/j.1432-1033.1996.0613w.x |