Synaptophysin: Difference between revisions

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{{protein
{{Infobox_gene}}
| Name = synaptophysin
| caption =
| image =
| width =
| HGNCid = 11506
| Symbol = SYP
| AltSymbols =
| EntrezGene = 6855
| OMIM = 313475
| RefSeq = NM_003179
| UniProt = P08247
| PDB =
| ECnumber =
| Chromosome = X
| Arm = p
| Band = 11.23
| LocusSupplementaryData = -p11.22
}}
{{SI}}
{{CMG}}


==Overview==
'''Synaptophysin''', also known as the '''major synaptic vesicle protein p38''', is a  [[protein]] that in humans is encoded by the ''SYP'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SYP synaptophysin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6855| accessdate = }}</ref><ref name="pmid3120152">{{cite journal | vauthors = Südhof TC, Lottspeich F, Greengard P, Mehl E, Jahn R | title = The cDNA and derived amino acid sequences for rat and human synaptophysin | journal = Nucleic Acids Res. | volume = 15 | issue = 22 | pages = 9607 | date = November 1987 | pmid = 3120152 | pmc = 306499 | doi = 10.1093/nar/15.22.9607 }}</ref>
'''Synaptophysin''' is a [[synaptic vesicle]] [[glycoprotein]] with four transmembrane domains weighing 38[[Atomic mass unit|kDa]]. It is present in [[endocrine system|neuroendocrine cells]] and in virtually all neurons in the [[brain]] and [[spinal cord]] that participate in synaptic transmission. It acts as a marker for neuroendocrine tumors.
The [[gene]] for this protein is located on the [[X chromosome]] (Xp11.23-p11.22). The exact function of the protein is unknown: it interacts with the essential synaptic vesicle protein synaptobrevin, but when the synaptophysin gene is experimentally inactivated in animals, they still develop and function normally.


==External link==
== Genomics ==
 
The gene is located on the short arm of [[X chromosome]] (Xp11.23-p11.22). It is 12,406 bases in length and lies on the minus strand. The encoded protein has 313 amino acids with a predicted molecular weight of 33.845 [[Atomic mass unit|kDa]].
 
== Molecular biology ==
 
The protein is a [[synaptic vesicle]] [[glycoprotein]] with four transmembrane domains weighing 38kDa. It is present in [[endocrine system|neuroendocrine cells]] and in virtually all neurons in the [[brain]] and [[spinal cord]] that participate in synaptic transmission. It acts as a marker for neuroendocrine tumors, and its ubiquity at the synapse has led to the use of synaptophysin immunostaining for quantification of synapses.<ref name="pmid9023727">{{cite journal | vauthors = Calhoun ME, Jucker M, Martin LJ, Thinakaran G, Price DL, Mouton PR | title = Comparative evaluation of synaptophysin-based methods for quantification of synapses | journal = J. Neurocytol. | volume = 25 | issue = 12 | pages = 821–8 | date = December 1996 | pmid = 9023727 | doi = 10.1007/BF02284844 }}</ref>
 
The exact function of the protein is unknown: it interacts with the essential synaptic vesicle protein [[synaptobrevin]], but when the synaptophysin gene is experimentally inactivated in animals, they still develop and function normally.<ref name="pmid8643476">{{cite journal | vauthors = McMahon HT, Bolshakov VY, Janz R, Hammer RE, Siegelbaum SA, Südhof TC | title = Synaptophysin, a major synaptic vesicle protein, is not essential for neurotransmitter release | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 10 | pages = 4760–4 | date = May 1996 | pmid = 8643476 | pmc = 39352 | doi = 10.1073/pnas.93.10.4760 }}</ref> Recent research has shown, however, that elimination of synaptophysin in mice creates behavioral changes such as increased exploratory behavior, impaired object novelty recognition, and reduced spatial learning.<ref name="pmid19393300">{{cite journal | vauthors = Schmitt U, Tanimoto N, Seeliger M, Schaeffel F, Leube RE | title = Detection of behavioral alterations and learning deficits in mice lacking synaptophysin | journal = Neuroscience | volume = 162 | issue = 2 | pages = 234–43 | date = August 2009 | pmid = 19393300 | doi = 10.1016/j.neuroscience.2009.04.046 }}</ref>
 
== Clinical importance ==
 
This gene has been implicated in X linked intellectual disability.<ref name="pmid19377476">{{cite journal | vauthors = Tarpey PS, Smith R, Pleasance E, Whibley A, Edkins S, Hardy C, O'Meara S, Latimer C, Dicks E, Menzies A, Stephens P, Blow M, Greenman C, Xue Y, Tyler-Smith C, Thompson D, Gray K, Andrews J, Barthorpe S, Buck G, Cole J, Dunmore R, Jones D, Maddison M, Mironenko T, Turner R, Turrell K, Varian J, West S, Widaa S, Wray P, Teague J, Butler A, Jenkinson A, Jia M, Richardson D, Shepherd R, Wooster R, Tejada MI, Martinez F, Carvill G, Goliath R, de Brouwer AP, van Bokhoven H, Van Esch H, Chelly J, Raynaud M, Ropers HH, Abidi FE, Srivastava AK, Cox J, Luo Y, Mallya U, Moon J, Parnau J, Mohammed S, Tolmie JL, Shoubridge C, Corbett M, Gardner A, Haan E, Rujirabanjerd S, Shaw M, Vandeleur L, Fullston T, Easton DF, Boyle J, Partington M, Hackett A, Field M, Skinner C, Stevenson RE, Bobrow M, Turner G, Schwartz CE, Gecz J, Raymond FL, Futreal PA, Stratton MR | title = A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation | journal = Nat. Genet. | volume = 41 | issue = 5 | pages = 535–43 | date = May 2009 | pmid = 19377476 | pmc = 2872007 | doi = 10.1038/ng.367 }}</ref>
 
Using [[immunohistochemistry]], synaptophysin can be demonstrated in a range of neural and neuroendocrine tissues,<ref>{{cite journal|last1=Wiedenmann|first1=B|last2=Franke|first2=WW|last3=Kuhn|first3=C|last4=Moll|first4=R|last5=Gould|first5=VE|title=Synaptophysin: a marker protein for neuroendocrine cells and neoplasms.|journal=Proceedings of the National Academy of Sciences of the United States of America|date=May 1986|volume=83|issue=10|pages=3500–4|pmid=3010302|url=http://www.pnas.org/content/83/10/3500.full.pdf|pmc=323544|doi=10.1073/pnas.83.10.3500}}</ref> including cells of the [[adrenal medulla]] and [[pancreatic islet]]s. As a specific marker for these tissues, it can be used to identify tumours arising from them, such as [[neuroblastoma]], [[retinoblastoma]], [[phaeochromocytoma]], [[carcinoid]], [[small-cell carcinoma]], [[medulloblastoma]] and [[medullary thyroid carcinoma]], among others. Diagnostically, it is often used in combination with [[chromogranin A]].<ref name=Leong>{{cite book|author=Leong, Anthony S-Y|author2=Cooper, Kumarason|author3=Leong, F Joel W-M|year=2003|title=Manual of Diagnostic Cytology|edition=2|publisher=Greenwich Medical Media, Ltd.|pages=405–406|isbn=1-84110-100-1}}</ref>
 
== See also ==
 
* [[List of human genes]]
 
== Interactions ==
 
Synaptophysin has been shown to [[Protein-protein interaction|interact]] with [[AP1G1]]<ref name="pmid12498786">{{cite journal | vauthors = Horikawa HP, Kneussel M, El Far O, Betz H | title = Interaction of synaptophysin with the AP-1 adaptor protein gamma-adaptin | journal = Mol. Cell. Neurosci. | volume = 21 | issue = 3 | pages = 454–62 | date = November 2002 | pmid = 12498786 | doi = 10.1006/mcne.2002.1191 }}</ref> and [[SIAH2]].<ref name="pmid11786535">{{cite journal | vauthors = Wheeler TC, Chin LS, Li Y, Roudabush FL, Li L | title = Regulation of synaptophysin degradation by mammalian homologues of seven in absentia | journal = J. Biol. Chem. | volume = 277 | issue = 12 | pages = 10273–82 | date = March 2002 | pmid = 11786535 | doi = 10.1074/jbc.M107857200 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
* {{cite journal | vauthors = Kalina M, Lukinius A, Grimelius L, Höög A, Falkmer S | title = Ultrastructural localization of synaptophysin to the secretory granules of normal glucagon and insulin cells in human islets of Langerhans | journal = Ultrastructural pathology | volume = 15 | issue = 3 | pages = 215–9 | year = 1991 | pmid = 1908157 | doi = 10.3109/01913129109021883 }}
* {{cite journal | vauthors = Ozçelik T, Lafreniere RG, Archer BT, Johnston PA, Willard HF, Francke U, Südhof TC | title = Synaptophysin: structure of the human gene and assignment to the X chromosome in man and mouse | journal = Am. J. Hum. Genet. | volume = 47 | issue = 3 | pages = 551–61 | year = 1990 | pmid = 1975480 | pmc = 1683862 | doi =  }}
* {{cite journal | vauthors = Goto S, Hirano A, Pearson J | title = Calcineurin and synaptophysin in the human spinal cord of normal individuals and patients with familial dysautonomia | journal = Acta Neuropathol. | volume = 79 | issue = 6 | pages = 647–52 | year = 1990 | pmid = 2163183 | doi = 10.1007/BF00294243 }}
* {{cite journal | vauthors = de Koning JP, Schelen AM, Dong F, van Buitenen C, Burgering BM, Bos JL, Löwenberg B, Touw IP | title = Specific involvement of tyrosine 764 of human granulocyte colony-stimulating factor receptor in signal transduction mediated by p145/Shc/GRB2 or p90/GRB2 complexes | journal = Blood | volume = 87 | issue = 1 | pages = 132–40 | year = 1996 | pmid = 8547634 | doi =  }}
* {{cite journal | vauthors = Zhang PJ, Rosenblum MK | title = Synaptophysin expression in the human spinal cord. Diagnostic implications of an immunohistochemical study | journal = Am. J. Surg. Pathol. | volume = 20 | issue = 3 | pages = 273–6 | year = 1997 | pmid = 8772779 | doi = 10.1097/00000478-199603000-00002 }}
* {{cite journal | vauthors = Bouwens L, Lu WG, De Krijger R | title = Proliferation and differentiation in the human fetal endocrine pancreas | journal = Diabetologia | volume = 40 | issue = 4 | pages = 398–404 | year = 1997 | pmid = 9112016 | doi = 10.1007/s001250050693 }}
* {{cite journal | vauthors = Fisher SE, Ciccodicola A, Tanaka K, Curci A, Desicato S, D'urso M, Craig IW | title = Sequence-based exon prediction around the synaptophysin locus reveals a gene-rich area containing novel genes in human proximal Xp | journal = Genomics | volume = 45 | issue = 2 | pages = 340–7 | year = 1998 | pmid = 9344658 | doi = 10.1006/geno.1997.4941 }}
* {{cite journal | vauthors = Maggiano N, Lauriola L, Serra FG, Ricci R, Capelli A, Ranelletti FO | title = Detection of synaptophysin-producing cells in human thymus by immunohistochemistry and nonradioactive in situ hybridization | journal = J. Histochem. Cytochem. | volume = 47 | issue = 2 | pages = 237–43 | year = 1999 | pmid = 9889259 | doi = 10.1177/002215549904700212 }}
* {{cite journal | vauthors = Portela-Gomes GM, Stridsberg M, Johansson H, Grimelius L | title = Co-localization of synaptophysin with different neuroendocrine hormones in the human gastrointestinal tract | journal = Histochem. Cell Biol. | volume = 111 | issue = 1 | pages = 49–54 | year = 1999 | pmid = 9930883 | doi = 10.1007/s004180050332 }}
* {{cite journal | vauthors = Davidsson P, Gottfries J, Bogdanovic N, Ekman R, Karlsson I, Gottfries CG, Blennow K | title = The synaptic-vesicle-specific proteins rab3a and synaptophysin are reduced in thalamus and related cortical brain regions in schizophrenic brains | journal = [[Schizophrenia Research]] | volume = 40 | issue = 1 | pages = 23–9 | year = 1999 | pmid = 10541003 | doi = 10.1016/S0920-9964(99)00037-7 }}
* {{cite journal | vauthors = Cassiman D, van Pelt J, De Vos R, Van Lommel F, Desmet V, Yap SH, Roskams T | title = Synaptophysin: A Novel Marker for Human and Rat Hepatic Stellate Cells | journal = Am. J. Pathol. | volume = 155 | issue = 6 | pages = 1831–9 | year = 1999 | pmid = 10595912 | pmc = 1866940 | doi = 10.1016/S0002-9440(10)65501-0 }}
* {{cite journal | vauthors = Thiele C, Hannah MJ, Fahrenholz F, Huttner WB | title = Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles | journal = Nat. Cell Biol. | volume = 2 | issue = 1 | pages = 42–9 | year = 2000 | pmid = 10620806 | doi = 10.1038/71366 }}
* {{cite journal | vauthors = Nag TC, Wadhwa S | title = Differential expression of syntaxin-1 and synaptophysin in the developing and adult human retina | journal = J. Biosci. | volume = 26 | issue = 2 | pages = 179–91 | year = 2001 | pmid = 11426054 | doi = 10.1007/BF02703642 }}
* {{cite journal | vauthors = Bhangu PS, Genever PG, Spencer GJ, Grewal TS, Skerry TM | title = Evidence for targeted vesicular glutamate exocytosis in osteoblasts | journal = Bone | volume = 29 | issue = 1 | pages = 16–23 | year = 2001 | pmid = 11472886 | doi = 10.1016/S8756-3282(01)00482-3 }}
* {{cite journal | vauthors = Roudenok V, Kühnel W | title = The development of synaptophysin immunoreactivity in the human sympathetic ganglia | journal = Ann. Anat. | volume = 183 | issue = 4 | pages = 345–51 | year = 2001 | pmid = 11508360 | doi = 10.1016/S0940-9602(01)80177-1 }}
* {{cite journal | vauthors = Wheeler TC, Chin LS, Li Y, Roudabush FL, Li L | title = Regulation of synaptophysin degradation by mammalian homologues of seven in absentia | journal = J. Biol. Chem. | volume = 277 | issue = 12 | pages = 10273–82 | year = 2002 | pmid = 11786535 | doi = 10.1074/jbc.M107857200 }}
* {{cite journal | vauthors = Ulfig N, Chan WY | title = Expression of a kinase anchoring protein 79 and synaptophysin in the developing human red nucleus | journal = Neurosignals | volume = 11 | issue = 2 | pages = 95–102 | year = 2003 | pmid = 12077483 | doi = 10.1159/000058546 }}
* {{cite journal | vauthors = Yao I, Iida J, Nishimura W, Hata Y | title = Synaptic and nuclear localization of brain-enriched guanylate kinase-associated protein | journal = J. Neurosci. | volume = 22 | issue = 13 | pages = 5354–64 | year = 2002 | pmid = 12097487 }}
* {{cite journal | vauthors = Wistow G, Bernstein SL, Wyatt MK, Ray S, Behal A, Touchman JW, Bouffard G, Smith D, Peterson K | title = Expressed sequence tag analysis of human retina for the NEIBank Project: retbindin, an abundant, novel retinal cDNA and alternative splicing of other retina-preferred gene transcripts | journal = Mol. Vis. | volume = 8 | issue =  | pages = 196–204 | year = 2002 | pmid = 12107411 | doi =  }}
{{refend}}
 
== External links ==
* {{MeshName|Synaptophysin}}
* {{MeshName|Synaptophysin}}


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{{Nerve tissue protein}}


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Latest revision as of 15:17, 18 October 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Synaptophysin, also known as the major synaptic vesicle protein p38, is a protein that in humans is encoded by the SYP gene.[1][2]

Genomics

The gene is located on the short arm of X chromosome (Xp11.23-p11.22). It is 12,406 bases in length and lies on the minus strand. The encoded protein has 313 amino acids with a predicted molecular weight of 33.845 kDa.

Molecular biology

The protein is a synaptic vesicle glycoprotein with four transmembrane domains weighing 38kDa. It is present in neuroendocrine cells and in virtually all neurons in the brain and spinal cord that participate in synaptic transmission. It acts as a marker for neuroendocrine tumors, and its ubiquity at the synapse has led to the use of synaptophysin immunostaining for quantification of synapses.[3]

The exact function of the protein is unknown: it interacts with the essential synaptic vesicle protein synaptobrevin, but when the synaptophysin gene is experimentally inactivated in animals, they still develop and function normally.[4] Recent research has shown, however, that elimination of synaptophysin in mice creates behavioral changes such as increased exploratory behavior, impaired object novelty recognition, and reduced spatial learning.[5]

Clinical importance

This gene has been implicated in X linked intellectual disability.[6]

Using immunohistochemistry, synaptophysin can be demonstrated in a range of neural and neuroendocrine tissues,[7] including cells of the adrenal medulla and pancreatic islets. As a specific marker for these tissues, it can be used to identify tumours arising from them, such as neuroblastoma, retinoblastoma, phaeochromocytoma, carcinoid, small-cell carcinoma, medulloblastoma and medullary thyroid carcinoma, among others. Diagnostically, it is often used in combination with chromogranin A.[8]

See also

Interactions

Synaptophysin has been shown to interact with AP1G1[9] and SIAH2.[10]

References

  1. ↑ "Entrez Gene: SYP synaptophysin".
  2. ↑ Südhof TC, Lottspeich F, Greengard P, Mehl E, Jahn R (November 1987). "The cDNA and derived amino acid sequences for rat and human synaptophysin". Nucleic Acids Res. 15 (22): 9607. doi:10.1093/nar/15.22.9607. PMC 306499. PMID 3120152.
  3. ↑ Calhoun ME, Jucker M, Martin LJ, Thinakaran G, Price DL, Mouton PR (December 1996). "Comparative evaluation of synaptophysin-based methods for quantification of synapses". J. Neurocytol. 25 (12): 821–8. doi:10.1007/BF02284844. PMID 9023727.
  4. ↑ McMahon HT, Bolshakov VY, Janz R, Hammer RE, Siegelbaum SA, Südhof TC (May 1996). "Synaptophysin, a major synaptic vesicle protein, is not essential for neurotransmitter release". Proc. Natl. Acad. Sci. U.S.A. 93 (10): 4760–4. doi:10.1073/pnas.93.10.4760. PMC 39352. PMID 8643476.
  5. ↑ Schmitt U, Tanimoto N, Seeliger M, Schaeffel F, Leube RE (August 2009). "Detection of behavioral alterations and learning deficits in mice lacking synaptophysin". Neuroscience. 162 (2): 234–43. doi:10.1016/j.neuroscience.2009.04.046. PMID 19393300.
  6. ↑ Tarpey PS, Smith R, Pleasance E, Whibley A, Edkins S, Hardy C, O'Meara S, Latimer C, Dicks E, Menzies A, Stephens P, Blow M, Greenman C, Xue Y, Tyler-Smith C, Thompson D, Gray K, Andrews J, Barthorpe S, Buck G, Cole J, Dunmore R, Jones D, Maddison M, Mironenko T, Turner R, Turrell K, Varian J, West S, Widaa S, Wray P, Teague J, Butler A, Jenkinson A, Jia M, Richardson D, Shepherd R, Wooster R, Tejada MI, Martinez F, Carvill G, Goliath R, de Brouwer AP, van Bokhoven H, Van Esch H, Chelly J, Raynaud M, Ropers HH, Abidi FE, Srivastava AK, Cox J, Luo Y, Mallya U, Moon J, Parnau J, Mohammed S, Tolmie JL, Shoubridge C, Corbett M, Gardner A, Haan E, Rujirabanjerd S, Shaw M, Vandeleur L, Fullston T, Easton DF, Boyle J, Partington M, Hackett A, Field M, Skinner C, Stevenson RE, Bobrow M, Turner G, Schwartz CE, Gecz J, Raymond FL, Futreal PA, Stratton MR (May 2009). "A systematic, large-scale resequencing screen of X-chromosome coding exons in mental retardation". Nat. Genet. 41 (5): 535–43. doi:10.1038/ng.367. PMC 2872007. PMID 19377476.
  7. ↑ Wiedenmann, B; Franke, WW; Kuhn, C; Moll, R; Gould, VE (May 1986). "Synaptophysin: a marker protein for neuroendocrine cells and neoplasms" (PDF). Proceedings of the National Academy of Sciences of the United States of America. 83 (10): 3500–4. doi:10.1073/pnas.83.10.3500. PMC 323544. PMID 3010302.
  8. ↑ Leong, Anthony S-Y; Cooper, Kumarason; Leong, F Joel W-M (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd. pp. 405–406. ISBN 1-84110-100-1.
  9. ↑ Horikawa HP, Kneussel M, El Far O, Betz H (November 2002). "Interaction of synaptophysin with the AP-1 adaptor protein gamma-adaptin". Mol. Cell. Neurosci. 21 (3): 454–62. doi:10.1006/mcne.2002.1191. PMID 12498786.
  10. ↑ Wheeler TC, Chin LS, Li Y, Roudabush FL, Li L (March 2002). "Regulation of synaptophysin degradation by mammalian homologues of seven in absentia". J. Biol. Chem. 277 (12): 10273–82. doi:10.1074/jbc.M107857200. PMID 11786535.

Further reading

  • Kalina M, Lukinius A, Grimelius L, Höög A, Falkmer S (1991). "Ultrastructural localization of synaptophysin to the secretory granules of normal glucagon and insulin cells in human islets of Langerhans". Ultrastructural pathology. 15 (3): 215–9. doi:10.3109/01913129109021883. PMID 1908157.
  • Ozçelik T, Lafreniere RG, Archer BT, Johnston PA, Willard HF, Francke U, Südhof TC (1990). "Synaptophysin: structure of the human gene and assignment to the X chromosome in man and mouse". Am. J. Hum. Genet. 47 (3): 551–61. PMC 1683862. PMID 1975480.
  • Goto S, Hirano A, Pearson J (1990). "Calcineurin and synaptophysin in the human spinal cord of normal individuals and patients with familial dysautonomia". Acta Neuropathol. 79 (6): 647–52. doi:10.1007/BF00294243. PMID 2163183.
  • de Koning JP, Schelen AM, Dong F, van Buitenen C, Burgering BM, Bos JL, Löwenberg B, Touw IP (1996). "Specific involvement of tyrosine 764 of human granulocyte colony-stimulating factor receptor in signal transduction mediated by p145/Shc/GRB2 or p90/GRB2 complexes". Blood. 87 (1): 132–40. PMID 8547634.
  • Zhang PJ, Rosenblum MK (1997). "Synaptophysin expression in the human spinal cord. Diagnostic implications of an immunohistochemical study". Am. J. Surg. Pathol. 20 (3): 273–6. doi:10.1097/00000478-199603000-00002. PMID 8772779.
  • Bouwens L, Lu WG, De Krijger R (1997). "Proliferation and differentiation in the human fetal endocrine pancreas". Diabetologia. 40 (4): 398–404. doi:10.1007/s001250050693. PMID 9112016.
  • Fisher SE, Ciccodicola A, Tanaka K, Curci A, Desicato S, D'urso M, Craig IW (1998). "Sequence-based exon prediction around the synaptophysin locus reveals a gene-rich area containing novel genes in human proximal Xp". Genomics. 45 (2): 340–7. doi:10.1006/geno.1997.4941. PMID 9344658.
  • Maggiano N, Lauriola L, Serra FG, Ricci R, Capelli A, Ranelletti FO (1999). "Detection of synaptophysin-producing cells in human thymus by immunohistochemistry and nonradioactive in situ hybridization". J. Histochem. Cytochem. 47 (2): 237–43. doi:10.1177/002215549904700212. PMID 9889259.
  • Portela-Gomes GM, Stridsberg M, Johansson H, Grimelius L (1999). "Co-localization of synaptophysin with different neuroendocrine hormones in the human gastrointestinal tract". Histochem. Cell Biol. 111 (1): 49–54. doi:10.1007/s004180050332. PMID 9930883.
  • Davidsson P, Gottfries J, Bogdanovic N, Ekman R, Karlsson I, Gottfries CG, Blennow K (1999). "The synaptic-vesicle-specific proteins rab3a and synaptophysin are reduced in thalamus and related cortical brain regions in schizophrenic brains". Schizophrenia Research. 40 (1): 23–9. doi:10.1016/S0920-9964(99)00037-7. PMID 10541003.
  • Cassiman D, van Pelt J, De Vos R, Van Lommel F, Desmet V, Yap SH, Roskams T (1999). "Synaptophysin: A Novel Marker for Human and Rat Hepatic Stellate Cells". Am. J. Pathol. 155 (6): 1831–9. doi:10.1016/S0002-9440(10)65501-0. PMC 1866940. PMID 10595912.
  • Thiele C, Hannah MJ, Fahrenholz F, Huttner WB (2000). "Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles". Nat. Cell Biol. 2 (1): 42–9. doi:10.1038/71366. PMID 10620806.
  • Nag TC, Wadhwa S (2001). "Differential expression of syntaxin-1 and synaptophysin in the developing and adult human retina". J. Biosci. 26 (2): 179–91. doi:10.1007/BF02703642. PMID 11426054.
  • Bhangu PS, Genever PG, Spencer GJ, Grewal TS, Skerry TM (2001). "Evidence for targeted vesicular glutamate exocytosis in osteoblasts". Bone. 29 (1): 16–23. doi:10.1016/S8756-3282(01)00482-3. PMID 11472886.
  • Roudenok V, Kühnel W (2001). "The development of synaptophysin immunoreactivity in the human sympathetic ganglia". Ann. Anat. 183 (4): 345–51. doi:10.1016/S0940-9602(01)80177-1. PMID 11508360.
  • Wheeler TC, Chin LS, Li Y, Roudabush FL, Li L (2002). "Regulation of synaptophysin degradation by mammalian homologues of seven in absentia". J. Biol. Chem. 277 (12): 10273–82. doi:10.1074/jbc.M107857200. PMID 11786535.
  • Ulfig N, Chan WY (2003). "Expression of a kinase anchoring protein 79 and synaptophysin in the developing human red nucleus". Neurosignals. 11 (2): 95–102. doi:10.1159/000058546. PMID 12077483.
  • Yao I, Iida J, Nishimura W, Hata Y (2002). "Synaptic and nuclear localization of brain-enriched guanylate kinase-associated protein". J. Neurosci. 22 (13): 5354–64. PMID 12097487.
  • Wistow G, Bernstein SL, Wyatt MK, Ray S, Behal A, Touchman JW, Bouffard G, Smith D, Peterson K (2002). "Expressed sequence tag analysis of human retina for the NEIBank Project: retbindin, an abundant, novel retinal cDNA and alternative splicing of other retina-preferred gene transcripts". Mol. Vis. 8: 196–204. PMID 12107411.

External links

Retrieved from "https://www.wikidoc.org/index.php?title=Synaptophysin&oldid=1534361"