Synaptotagmin I increases the probability of vesicle fusion at low [Ca2+] in pituitary cells
Laboratory of Neuroendocrinology-Molecular Cell Physiology, Institute of Pathophysiology, Medical Faculty, 1000 Ljubljana; and Celica Biomedical Science Center, 1000 Ljubljana, Slovenia Synaptotagmin I (Syt I), a low-affinity Ca 2+ -binding protein, is thought to serve as the Ca 2+ sensor in the rel...
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| Veröffentlicht in: | American Journal of Physiology: Cell Physiology 2003-02, Vol.284 (2), p.C547-C554 |
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| container_title | American Journal of Physiology: Cell Physiology |
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| creator | Kreft, M Kuster, V Grilc, S Rupnik, M Milisav, I Zorec, R |
| description | Laboratory of Neuroendocrinology-Molecular Cell Physiology,
Institute of Pathophysiology, Medical Faculty, 1000 Ljubljana; and
Celica Biomedical Science Center, 1000 Ljubljana, Slovenia
Synaptotagmin I (Syt I),
a low-affinity Ca 2+ -binding protein, is thought to serve as
the Ca 2+ sensor in the release of neurotransmitter.
However, functional studies on the calyx of Held synapse revealed that
the rapid release of neurotransmitter requires only approximately
micromolar [Ca 2+ ], suggesting that Syt I may play a more
complex role in determining the high-affinity Ca 2+
dependence of exocytosis. Here we tested this hypothesis by studying pituitary cells, which possess high- and low-affinity
Ca 2+ -dependent exocytic pathways and express Syt I. Using
patch-clamp capacitance measurements to monitor secretion and the acute
antisense deletion of Syt I from differentiated cells, we have shown
that the rapid and the most Ca 2+ -sensitive pathway of
exocytosis in rat melanotrophs requires Syt I. Furthermore, stimulation
of the Ca 2+ -dependent exocytosis by cytosol dialysis with
solutions containing 1 µM [Ca 2+ ] was completely
abolished in the absence of Syt I. Similar results were obtained by the
preinjection of antibodies against the CAPS (Ca 2+ -dependent
activator protein for secretion) protein. These results indicate that
synaptotagmin I and CAPS proteins increase the probability of vesicle
fusion at low cytosolic [Ca 2+ ].
rat melanotrophs; exocytic module; membrane capacitance; calcium
sensor |
| doi_str_mv | 10.1152/ajpcell.00333.2002 |
| format | Article |
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Institute of Pathophysiology, Medical Faculty, 1000 Ljubljana; and
Celica Biomedical Science Center, 1000 Ljubljana, Slovenia
Synaptotagmin I (Syt I),
a low-affinity Ca 2+ -binding protein, is thought to serve as
the Ca 2+ sensor in the release of neurotransmitter.
However, functional studies on the calyx of Held synapse revealed that
the rapid release of neurotransmitter requires only approximately
micromolar [Ca 2+ ], suggesting that Syt I may play a more
complex role in determining the high-affinity Ca 2+
dependence of exocytosis. Here we tested this hypothesis by studying pituitary cells, which possess high- and low-affinity
Ca 2+ -dependent exocytic pathways and express Syt I. Using
patch-clamp capacitance measurements to monitor secretion and the acute
antisense deletion of Syt I from differentiated cells, we have shown
that the rapid and the most Ca 2+ -sensitive pathway of
exocytosis in rat melanotrophs requires Syt I. Furthermore, stimulation
of the Ca 2+ -dependent exocytosis by cytosol dialysis with
solutions containing 1 µM [Ca 2+ ] was completely
abolished in the absence of Syt I. Similar results were obtained by the
preinjection of antibodies against the CAPS (Ca 2+ -dependent
activator protein for secretion) protein. These results indicate that
synaptotagmin I and CAPS proteins increase the probability of vesicle
fusion at low cytosolic [Ca 2+ ].
rat melanotrophs; exocytic module; membrane capacitance; calcium
sensor</description><identifier>ISSN: 0363-6143</identifier><identifier>EISSN: 1522-1563</identifier><identifier>DOI: 10.1152/ajpcell.00333.2002</identifier><identifier>PMID: 12388083</identifier><language>eng</language><publisher>United States</publisher><subject>Animals ; Calcium - deficiency ; Calcium Signaling - drug effects ; Calcium Signaling - physiology ; Calcium-Binding Proteins - antagonists & inhibitors ; Calcium-Binding Proteins - metabolism ; Cells, Cultured ; DNA, Complementary - genetics ; Endocytosis - drug effects ; Endocytosis - genetics ; Epithelial Cells - drug effects ; Epithelial Cells - metabolism ; Epithelial Cells - secretion ; Exocytosis - drug effects ; Exocytosis - genetics ; Male ; Membrane Glycoproteins - genetics ; Membrane Glycoproteins - metabolism ; Membrane Proteins - drug effects ; Membrane Proteins - metabolism ; Nerve Tissue Proteins - genetics ; Nerve Tissue Proteins - metabolism ; Oligonucleotides, Antisense ; Pituitary Gland - drug effects ; Pituitary Gland - metabolism ; Pituitary Gland - secretion ; Protein Isoforms - genetics ; Protein Isoforms - metabolism ; Rats ; RNA, Messenger - genetics ; Secretory Vesicles - drug effects ; Secretory Vesicles - metabolism ; SNARE Proteins ; Synaptotagmin I ; Synaptotagmins ; Vesicular Transport Proteins</subject><ispartof>American Journal of Physiology: Cell Physiology, 2003-02, Vol.284 (2), p.C547-C554</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c387t-c1e2e83756253183a4ad84e93c327544fe575f169dbc2c5065c95318e2ce2da03</citedby><cites>FETCH-LOGICAL-c387t-c1e2e83756253183a4ad84e93c327544fe575f169dbc2c5065c95318e2ce2da03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3039,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12388083$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kreft, M</creatorcontrib><creatorcontrib>Kuster, V</creatorcontrib><creatorcontrib>Grilc, S</creatorcontrib><creatorcontrib>Rupnik, M</creatorcontrib><creatorcontrib>Milisav, I</creatorcontrib><creatorcontrib>Zorec, R</creatorcontrib><title>Synaptotagmin I increases the probability of vesicle fusion at low [Ca2+] in pituitary cells</title><title>American Journal of Physiology: Cell Physiology</title><addtitle>Am J Physiol Cell Physiol</addtitle><description>Laboratory of Neuroendocrinology-Molecular Cell Physiology,
Institute of Pathophysiology, Medical Faculty, 1000 Ljubljana; and
Celica Biomedical Science Center, 1000 Ljubljana, Slovenia
Synaptotagmin I (Syt I),
a low-affinity Ca 2+ -binding protein, is thought to serve as
the Ca 2+ sensor in the release of neurotransmitter.
However, functional studies on the calyx of Held synapse revealed that
the rapid release of neurotransmitter requires only approximately
micromolar [Ca 2+ ], suggesting that Syt I may play a more
complex role in determining the high-affinity Ca 2+
dependence of exocytosis. Here we tested this hypothesis by studying pituitary cells, which possess high- and low-affinity
Ca 2+ -dependent exocytic pathways and express Syt I. Using
patch-clamp capacitance measurements to monitor secretion and the acute
antisense deletion of Syt I from differentiated cells, we have shown
that the rapid and the most Ca 2+ -sensitive pathway of
exocytosis in rat melanotrophs requires Syt I. Furthermore, stimulation
of the Ca 2+ -dependent exocytosis by cytosol dialysis with
solutions containing 1 µM [Ca 2+ ] was completely
abolished in the absence of Syt I. Similar results were obtained by the
preinjection of antibodies against the CAPS (Ca 2+ -dependent
activator protein for secretion) protein. These results indicate that
synaptotagmin I and CAPS proteins increase the probability of vesicle
fusion at low cytosolic [Ca 2+ ].
rat melanotrophs; exocytic module; membrane capacitance; calcium
sensor</description><subject>Animals</subject><subject>Calcium - deficiency</subject><subject>Calcium Signaling - drug effects</subject><subject>Calcium Signaling - physiology</subject><subject>Calcium-Binding Proteins - antagonists & inhibitors</subject><subject>Calcium-Binding Proteins - metabolism</subject><subject>Cells, Cultured</subject><subject>DNA, Complementary - genetics</subject><subject>Endocytosis - drug effects</subject><subject>Endocytosis - genetics</subject><subject>Epithelial Cells - drug effects</subject><subject>Epithelial Cells - metabolism</subject><subject>Epithelial Cells - secretion</subject><subject>Exocytosis - drug effects</subject><subject>Exocytosis - genetics</subject><subject>Male</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Membrane Proteins - drug effects</subject><subject>Membrane Proteins - metabolism</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Oligonucleotides, Antisense</subject><subject>Pituitary Gland - drug effects</subject><subject>Pituitary Gland - metabolism</subject><subject>Pituitary Gland - secretion</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><subject>Rats</subject><subject>RNA, Messenger - genetics</subject><subject>Secretory Vesicles - drug effects</subject><subject>Secretory Vesicles - metabolism</subject><subject>SNARE Proteins</subject><subject>Synaptotagmin I</subject><subject>Synaptotagmins</subject><subject>Vesicular Transport Proteins</subject><issn>0363-6143</issn><issn>1522-1563</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1v1DAURS1ERYfCH2CBvGJTZWq_F-djiUYUKlViQVkBsjzOy4wrTxJihzb_HocZ6IrVW7xzr64OY2-kWEup4MrcD5a8XwuBiGsQAp6xVXpAJlWBz9lKYIFZIXM8Zy9DuBdC5FDUL9i5BKwqUeGKff8yd2aIfTS7g-v4DXedHckECjzuiQ9jvzVb512ced_yXxSc9cTbKbi-4yZy3z_wbxsDlz9Skg8uTi6acebLsPCKnbXGB3p9uhfs6_WHu82n7Pbzx5vN-9vMYlXGzEoCqrBUBSiUFZrcNFVONVqEUuV5S6pUrSzqZmvBKlEoWy8ggSVojMAL9u7Ym-b-nChEfXBhWWA66qegS6iLUso6gXAE7diHMFKrh9Ed0l4thV6c6pNT_cepXpym0NtT-7Q9UPMUOUlMQHYE9m63f3Aj6WE_J0G-383_CqHKNeiNysvE1__nryfv7-gx_g0-5fTQtPgbNHeY6g</recordid><startdate>20030201</startdate><enddate>20030201</enddate><creator>Kreft, M</creator><creator>Kuster, V</creator><creator>Grilc, S</creator><creator>Rupnik, M</creator><creator>Milisav, I</creator><creator>Zorec, R</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20030201</creationdate><title>Synaptotagmin I increases the probability of vesicle fusion at low [Ca2+] in pituitary cells</title><author>Kreft, M ; Kuster, V ; Grilc, S ; Rupnik, M ; Milisav, I ; Zorec, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c387t-c1e2e83756253183a4ad84e93c327544fe575f169dbc2c5065c95318e2ce2da03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Calcium - deficiency</topic><topic>Calcium Signaling - drug effects</topic><topic>Calcium Signaling - physiology</topic><topic>Calcium-Binding Proteins - antagonists & inhibitors</topic><topic>Calcium-Binding Proteins - metabolism</topic><topic>Cells, Cultured</topic><topic>DNA, Complementary - genetics</topic><topic>Endocytosis - drug effects</topic><topic>Endocytosis - genetics</topic><topic>Epithelial Cells - drug effects</topic><topic>Epithelial Cells - metabolism</topic><topic>Epithelial Cells - secretion</topic><topic>Exocytosis - drug effects</topic><topic>Exocytosis - genetics</topic><topic>Male</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Membrane Proteins - drug effects</topic><topic>Membrane Proteins - metabolism</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Oligonucleotides, Antisense</topic><topic>Pituitary Gland - drug effects</topic><topic>Pituitary Gland - metabolism</topic><topic>Pituitary Gland - secretion</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><topic>Rats</topic><topic>RNA, Messenger - genetics</topic><topic>Secretory Vesicles - drug effects</topic><topic>Secretory Vesicles - metabolism</topic><topic>SNARE Proteins</topic><topic>Synaptotagmin I</topic><topic>Synaptotagmins</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kreft, M</creatorcontrib><creatorcontrib>Kuster, V</creatorcontrib><creatorcontrib>Grilc, S</creatorcontrib><creatorcontrib>Rupnik, M</creatorcontrib><creatorcontrib>Milisav, I</creatorcontrib><creatorcontrib>Zorec, R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>American Journal of Physiology: Cell Physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kreft, M</au><au>Kuster, V</au><au>Grilc, S</au><au>Rupnik, M</au><au>Milisav, I</au><au>Zorec, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Synaptotagmin I increases the probability of vesicle fusion at low [Ca2+] in pituitary cells</atitle><jtitle>American Journal of Physiology: Cell Physiology</jtitle><addtitle>Am J Physiol Cell Physiol</addtitle><date>2003-02-01</date><risdate>2003</risdate><volume>284</volume><issue>2</issue><spage>C547</spage><epage>C554</epage><pages>C547-C554</pages><issn>0363-6143</issn><eissn>1522-1563</eissn><abstract>Laboratory of Neuroendocrinology-Molecular Cell Physiology,
Institute of Pathophysiology, Medical Faculty, 1000 Ljubljana; and
Celica Biomedical Science Center, 1000 Ljubljana, Slovenia
Synaptotagmin I (Syt I),
a low-affinity Ca 2+ -binding protein, is thought to serve as
the Ca 2+ sensor in the release of neurotransmitter.
However, functional studies on the calyx of Held synapse revealed that
the rapid release of neurotransmitter requires only approximately
micromolar [Ca 2+ ], suggesting that Syt I may play a more
complex role in determining the high-affinity Ca 2+
dependence of exocytosis. Here we tested this hypothesis by studying pituitary cells, which possess high- and low-affinity
Ca 2+ -dependent exocytic pathways and express Syt I. Using
patch-clamp capacitance measurements to monitor secretion and the acute
antisense deletion of Syt I from differentiated cells, we have shown
that the rapid and the most Ca 2+ -sensitive pathway of
exocytosis in rat melanotrophs requires Syt I. Furthermore, stimulation
of the Ca 2+ -dependent exocytosis by cytosol dialysis with
solutions containing 1 µM [Ca 2+ ] was completely
abolished in the absence of Syt I. Similar results were obtained by the
preinjection of antibodies against the CAPS (Ca 2+ -dependent
activator protein for secretion) protein. These results indicate that
synaptotagmin I and CAPS proteins increase the probability of vesicle
fusion at low cytosolic [Ca 2+ ].
rat melanotrophs; exocytic module; membrane capacitance; calcium
sensor</abstract><cop>United States</cop><pmid>12388083</pmid><doi>10.1152/ajpcell.00333.2002</doi></addata></record> |
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| identifier | ISSN: 0363-6143 |
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| source | MEDLINE; American Physiological Society; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Calcium - deficiency Calcium Signaling - drug effects Calcium Signaling - physiology Calcium-Binding Proteins - antagonists & inhibitors Calcium-Binding Proteins - metabolism Cells, Cultured DNA, Complementary - genetics Endocytosis - drug effects Endocytosis - genetics Epithelial Cells - drug effects Epithelial Cells - metabolism Epithelial Cells - secretion Exocytosis - drug effects Exocytosis - genetics Male Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Membrane Proteins - drug effects Membrane Proteins - metabolism Nerve Tissue Proteins - genetics Nerve Tissue Proteins - metabolism Oligonucleotides, Antisense Pituitary Gland - drug effects Pituitary Gland - metabolism Pituitary Gland - secretion Protein Isoforms - genetics Protein Isoforms - metabolism Rats RNA, Messenger - genetics Secretory Vesicles - drug effects Secretory Vesicles - metabolism SNARE Proteins Synaptotagmin I Synaptotagmins Vesicular Transport Proteins |
| title | Synaptotagmin I increases the probability of vesicle fusion at low [Ca2+] in pituitary cells |
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