Glucose metabolism in photoreceptor outer segments. Its role in phototransduction and in NADPH-requiring reactions

Glucose metabolism in the photoreceptor rod outer segment produces both ATP (GTP) and NADPH to support phototransduction and NADPH-requiring processes in this organelle. Glycolysis in isolated bovine rod outer segments produces 44.0 +/- 6.4 nmol of ATP/min/mg of protein or 5.7 mM ATP/min. This rate...

Full description

Saved in:
Bibliographic Details
Published inThe Journal of biological chemistry Vol. 269; no. 27; pp. 17954 - 17959
Main Authors Hsu, S C, Molday, R S
Format Journal Article
LanguageEnglish
Published Bethesda, MD American Society for Biochemistry and Molecular Biology 08.07.1994
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Glucose metabolism in the photoreceptor rod outer segment produces both ATP (GTP) and NADPH to support phototransduction and NADPH-requiring processes in this organelle. Glycolysis in isolated bovine rod outer segments produces 44.0 +/- 6.4 nmol of ATP/min/mg of protein or 5.7 mM ATP/min. This rate of ATP production is more than sufficient to maintain the basal rate of cGMP synthesis (0.86 mM cGMP/min) in the dark requiring 1.7 mM ATP/min. Following photoexcitation, the 4.5-fold increase in the turnover of cGMP requires an ATP synthesis rate of up to 7.7 mM ATP/min (Ames, A., Walseth, T. F., Heyman, R. A., Barad, M., Graeff, R. M., and Goldberg, N. D. (1986) J. Biol. Chem. 261, 13034-13042). Under these conditions the rate of ATP production by glycolysis as measured in isolated rod outer segments is not sufficient for the regeneration of cGMP. Additional energy is most likely provided by the phosphocreatine shuttle which transports high energy phosphate groups in the form of creatine phosphate from the rod inner segment to the rod outer segment for conversion to ATP. The hexose monophosphate pathway in bovine rod outer segments can produce up to 39.8 +/- 2.2 nmol of NADPH/min/mg of protein. This rate of NADPH production is sufficient to support both the reduction of retinal to retinol (1.2 +/- 0.2 nmol of NADPH/min/mg of protein) following the photobleaching of rhodopsin and glutathione reduction (1.1 +/- 0.1 nmol of NADPH/min/mg of protein) for the protection of rod outer segments from oxidative damage. These studies provide insight into the contribution of anaerobic glycolysis and the hexose monophosphate pathway in providing energy and nucleotides for phototransduction and other outer segment processes.
AbstractList Glucose metabolism in the photoreceptor rod outer segment produces both ATP (GTP) and NADPH to support phototransduction and NADPH-requiring processes in this organelle. Glycolysis in isolated bovine rod outer segments produces 44.0 +/- 6.4 nmol of ATP/min/mg of protein or 5.7 mM ATP/min. This rate of ATP production is more than sufficient to maintain the basal rate of cGMP synthesis (0.86 mM cGMP/min) in the dark requiring 1.7 mM ATP/min. Following photoexcitation, the 4.5-fold increase in the turnover of cGMP requires an ATP synthesis rate of up to 7.7 mM ATP/min (Ames, A., Walseth, T. F., Heyman, R. A., Barad, M., Graeff, R. M., and Goldberg, N. D. (1986) J. Biol. Chem. 261, 13034-13042). Under these conditions the rate of ATP production by glycolysis as measured in isolated rod outer segments is not sufficient for the regeneration of cGMP. Additional energy is most likely provided by the phosphocreatine shuttle which transports high energy phosphate groups in the form of creatine phosphate from the rod inner segment to the rod outer segment for conversion to ATP. The hexose monophosphate pathway in bovine rod outer segments can produce up to 39.8 +/- 2.2 nmol of NADPH/min/mg of protein. This rate of NADPH production is sufficient to support both the reduction of retinal to retinol (1.2 +/- 0.2 nmol of NADPH/min/mg of protein) following the photobleaching of rhodopsin and glutathione reduction (1.1 +/- 0.1 nmol of NADPH/min/mg of protein) for the protection of rod outer segments from oxidative damage. These studies provide insight into the contribution of anaerobic glycolysis and the hexose monophosphate pathway in providing energy and nucleotides for phototransduction and other outer segment processes.
Glucose metabolism in the photoreceptor rod outer segment produces both ATP (GTP) and NADPH to support phototransduction and NADPH-requiring processes in this organelle. Glycolysis in isolated bovine rod outer segments produces 44.0 +/- 6.4 nmol of ATP/min/mg of protein or 5.7 mM ATP/min. This rate of ATP production is more than sufficient to maintain the basal rate of cGMP synthesis (0.86 mM cGMP/min) in the dark requiring 1.7 mM ATP/min. Following photoexcitation, the 4.5-fold increase in the turnover of cGMP requires an ATP synthesis rate of up to 7.7 mM ATP/min (Ames, A., Walseth, T. F., Heyman, R. A., Barad, M., Graeff, R. M., and Goldberg, N. D. (1986) J. Biol. Chem. 261, 13034-13042). Under these conditions the rate of ATP production by glycolysis as measured in isolated rod outer segments is not sufficient for the regeneration of cGMP. Additional energy is most likely provided by the phosphocreatine shuttle which transports high energy phosphate groups in the form of creatine phosphate from the rod inner segment to the rod outer segment for conversion to ATP. The hexose monophosphate pathway in bovine rod outer segments can produce up to 39.8 +/- 2.2 nmol of NADPH/min/mg of protein. This rate of NADPH production is sufficient to support both the reduction of retinal to retinol (1.2 +/- 0.2 nmol of NADPH/min/mg of protein) following the photobleaching of rhodopsin and glutathione reduction (1.1 +/- 0.1 nmol of NADPH/min/mg of protein) for the protection of rod outer segments from oxidative damage. These studies provide insight into the contribution of anaerobic glycolysis and the hexose monophosphate pathway in providing energy and nucleotides for phototransduction and other outer segment processes.
Glucose metabolism in the photoreceptor rod outer segment produces both ATP (GTP) and NADPH to support phototransduction and NADPH-requiring processes in this organelle. Glycolysis in isolated bovine rod outer segments produces 44.0 plus or minus 6.4 nmol of ATP/min/mg of protein or 5.7 mM ATP/min. This rate of ATP production is more than sufficient to maintain the basal rate of cGMP synthesis (0.86 mM cGMP/min) in the dark requiring 1.7 mM ATP/min. Following photoexcitation, the 4.5-fold increase in the turnover of cGMP requires an ATP synthesis rate of up to 7.7 mM ATP/min. Under these conditions the rate of ATP production by glycolysis as measured in isolated rod outer segments is not sufficient for the regeneration of cGMP. Additional energy is most likely provided by the phosphocreatine shuttle which transports high energy phosphate groups in the form of creatine phosphate from the rod inner segment to the rod outer segment for conversion to ATP. The hexose monophosphate pathway in bovine rod outer segments can produce up to 39.8 plus or minus 2.2 nmol of NADPH/min/mg of protein. This rate of NADPH production is sufficient to support both the reduction of retinal to retinol following the photobleaching of rhodopsin and glutathione reduction for the protection of rod outer segments from oxidative damage. These studies provide insight into the contribution of anaerobic glycolysis and the hexose monophosphate pathway in providing energy and nucleotides for phototransduction and other outer segment processes.
Author S C Hsu
R S Molday
Author_xml – sequence: 1
  givenname: S C
  surname: Hsu
  fullname: Hsu, S C
  organization: Department of Biochemistry and Molecular Biology, Faculty of Medicine, University of British Columbia, Vancouver, Canada
– sequence: 2
  givenname: R S
  surname: Molday
  fullname: Molday, R S
BackLink http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4234881$$DView record in Pascal Francis
https://www.ncbi.nlm.nih.gov/pubmed/8027053$$D View this record in MEDLINE/PubMed
BookMark eNqFkUtr3DAUhUVJSSdJf0JAi1LahVM9LWsZkuYBoS0kgdkJWb6aUbGtiSRT-u_jmQzTZe_mLM53H9xzgo7GOAJC55RcUELrb4-EMFppJpsvVH3lTBBWLd-hBSUNr7ikyyO0OCAf0EnOv8lcQtNjdNwQpojkC5Ru-8nFDHiAYtvYhzzgMOLNOpaYwMFmFhynAglnWA0wlnyB70vGKfZwIEuyY-4mV0IcsR27rfHj8vrXXZXgZQopjCucwO78fIbee9tn-LjXU_R88_3p6q56-Hl7f3X5UDkhSKlA2s4KroFaJbWSrCXQaSsVnY_3vlZEMVlLqgX4RgAhlBPqnWqJF75hnp-iz29zNym-TJCLGUJ20Pd2hDhlo2qpmNDivyCtNee0ljMo30CXYs4JvNmkMNj011BitqGYXShm-3FDldmFYpZz3_l-wdQO0B269inM_qe9b7OzvZ-_6UI-YIJx0TT0H7YOq_WfkMC0Ibo1DIbV2jA1r9RS8FfnsKMb
CODEN JBCHA3
CitedBy_id crossref_primary_10_1073_pnas_2202485119
crossref_primary_10_3390_ijms21041503
crossref_primary_10_1096_fba_2019_00093
crossref_primary_10_1152_ajpcell_00137_2005
crossref_primary_10_1111_j_1600_079X_1999_tb00582_x
crossref_primary_10_1006_bbrc_2000_2160
crossref_primary_10_1074_jbc_M501338200
crossref_primary_10_1085_jgp_200910267
crossref_primary_10_1177_002215540205000408
crossref_primary_10_1085_jgp_200409078
crossref_primary_10_1016_j_biocel_2009_08_013
crossref_primary_10_1152_physrev_00021_2004
crossref_primary_10_1016_S0165_0173_00_00038_2
crossref_primary_10_1016_S1011_1344_02_00238_5
crossref_primary_10_1080_02713680500477347
crossref_primary_10_1002_cbf_2943
crossref_primary_10_1016_j_mehy_2011_12_012
crossref_primary_10_1523_JNEUROSCI_2848_10_2010
crossref_primary_10_1074_jbc_275_15_11034
crossref_primary_10_1111_j_0953_816X_2004_03417_x
crossref_primary_10_1073_pnas_0806593105
crossref_primary_10_1074_mcp_M110_002469
crossref_primary_10_1083_jcb_200504008
crossref_primary_10_3390_biom14060654
crossref_primary_10_1016_j_neuron_2006_12_021
crossref_primary_10_1085_jgp_200609557
crossref_primary_10_1016_S1350_9462_98_00010_X
crossref_primary_10_1007_s11033_022_07256_w
crossref_primary_10_1021_acs_jproteome_7b00741
crossref_primary_10_1016_S0014_4835_03_00147_7
crossref_primary_10_1038_nchembio_1114
crossref_primary_10_1038_s41598_023_37938_9
crossref_primary_10_1016_j_biochi_2011_05_020
crossref_primary_10_1529_biophysj_104_054254
crossref_primary_10_1016_j_biochi_2014_02_007
crossref_primary_10_1016_j_freeradbiomed_2018_01_029
crossref_primary_10_3389_fimmu_2017_00505
crossref_primary_10_1074_jbc_M113_511295
crossref_primary_10_1111_ceo_12952
crossref_primary_10_1364_JOSAA_13_000566
crossref_primary_10_1007_s10571_013_9926_7
crossref_primary_10_1242_jcs_072389
crossref_primary_10_1016_0042_6989_96_00052_1
crossref_primary_10_1002_biof_166
crossref_primary_10_1007_s11892_015_0686_2
crossref_primary_10_1016_S0005_2728_01_00160_8
crossref_primary_10_1111_j_1600_0420_1997_tb00761_x
crossref_primary_10_1111_boc_201300003
crossref_primary_10_1016_j_visres_2006_08_024
crossref_primary_10_1074_mcp_M700571_MCP200
crossref_primary_10_1007_s11596_013_1086_y
crossref_primary_10_1079_PNS19960023
crossref_primary_10_1016_S1011_1344_99_00200_6
crossref_primary_10_1021_pr7006939
crossref_primary_10_1080_02713683_2020_1809001
crossref_primary_10_1111_ceo_13336
crossref_primary_10_1117_1_2982528
crossref_primary_10_1039_b306774m
crossref_primary_10_3390_antiox10050661
Cites_doi 10.1002/jcp.1040730103
10.1016/0005-2744(69)90280-0
10.1016/0003-9861(83)90295-3
10.1016/0014-5793(89)80687-8
10.1016/S0021-9258(20)64292-2
10.1016/S0021-9258(18)54699-8
10.1016/S0021-9258(19)63279-5
10.1016/S0076-6879(82)90117-3
10.1016/S0021-9258(18)69267-1
10.1016/S0021-9258(19)61742-4
10.1073/pnas.71.9.3584
10.1016/S0076-6879(82)90116-1
10.1016/0304-4157(73)90006-3
10.1085/jgp.77.6.667
10.1016/S0021-9258(19)86096-9
10.1016/S0076-6879(82)90119-7
10.1016/S0076-6879(82)90098-2
10.1016/S0021-9258(18)70565-6
10.1016/0005-2736(70)90118-5
10.1073/pnas.83.11.3816
10.1016/S0021-9258(18)81273-X
10.1016/0005-2744(74)90213-7
10.1016/0079-6107(89)90016-3
10.1016/0304-4165(81)90298-1
10.1016/0092-8674(85)90085-6
10.1016/S0021-9258(18)51808-1
10.1111/j.1471-4159.1960.tb13363.x
10.1111/j.1471-4159.1968.tb08963.x
10.1016/S0021-9258(18)65313-X
10.1085/jgp.37.2.189
10.1111/j.1432-1033.1971.tb01360.x
10.1016/0026-2862(72)90069-6
10.1016/0005-2787(76)90517-7
10.1016/0014-5793(90)81286-W
10.1016/S0021-9258(19)38299-7
10.1016/0304-4165(69)90093-2
10.1016/S0021-9258(18)33840-7
10.1016/0005-2736(79)90182-2
10.1016/0005-2736(73)90285-X
10.1111/j.1471-4159.1970.tb02195.x
10.1038/280398a0
10.1021/bi00101a009
ContentType Journal Article
Copyright 1994 INIST-CNRS
Copyright_xml – notice: 1994 INIST-CNRS
DBID IQODW
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7TK
7X8
DOI 10.1016/S0021-9258(17)32402-X
DatabaseName Pascal-Francis
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
Neurosciences Abstracts
MEDLINE - Academic
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Neurosciences Abstracts
MEDLINE - Academic
DatabaseTitleList MEDLINE

Neurosciences Abstracts
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Anatomy & Physiology
Chemistry
EISSN 1083-351X
EndPage 17959
ExternalDocumentID 10_1016_S0021_9258_17_32402_X
8027053
4234881
269_27_17954
Genre Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID -
02
08R
186
2WC
3O-
53G
55
5BI
5GY
5RE
5VS
85S
AARDX
AAWZA
ABFLS
ABOCM
ABPPZ
ABPTK
ABUFD
ABZEH
ACNCT
ADACO
ADBBV
ADBIT
ADCOW
AEILP
AENEX
AFFNX
AFMIJ
AIZTS
ALMA_UNASSIGNED_HOLDINGS
C1A
CJ0
CS3
DIK
DL
DU5
DZ
E3Z
EBS
EJD
ET
F20
F5P
FA8
FRP
GJ
GX1
H13
HH5
IH2
J5H
KM
KQ8
L7B
LI
MVM
MYA
N9A
NHB
O0-
OHM
OHT
OK1
P-O
P0W
P2P
R.V
RHF
RHI
RNS
RPM
SJN
TBC
TN5
UHB
UPT
UQL
VH1
VQA
WH7
WOQ
X
X7M
XFK
XHC
XJT
Y6R
YZZ
ZA5
ZGI
ZY4
---
-DZ
-ET
-~X
.55
.GJ
0SF
18M
29J
34G
39C
4.4
41~
6TJ
79B
AAEDW
AAFWJ
AAUGY
AAXUO
AAYJJ
AAYOK
ABDNZ
ABFSI
ABRJW
ABTAH
ACGFO
ACSFO
ACYGS
ADIYS
ADNWM
AEXQZ
AFDAS
AFOSN
AFPKN
AI.
AMRAJ
AOIJS
BAWUL
BTFSW
E.L
FDB
GROUPED_DOAJ
HYE
IQODW
QZG
ROL
TR2
UKR
W8F
WHG
XSW
YQT
YSK
YWH
YYP
ZE2
~02
~KM
0R~
AALRI
ADVLN
AITUG
AKRWK
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7TK
7X8
ID FETCH-LOGICAL-c440t-e5ada439e1a759752b0ed9a571802ff67072565194ef84e001301fc7b0f4f82f3
ISSN 0021-9258
IngestDate Fri Oct 25 01:58:15 EDT 2024
Fri Oct 25 22:13:59 EDT 2024
Fri Dec 06 06:27:27 EST 2024
Sat Sep 28 08:29:58 EDT 2024
Sun Oct 29 17:08:47 EDT 2023
Tue Jan 05 14:51:57 EST 2021
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 27
Keywords NADPH
Photoreception
Bovine
Rod
Glucose
Signal transduction
Vertebrata
Mammalia
Glycolysis
Artiodactyla
ATP
Retinal
Ungulata
Language English
License CC BY 4.0
http://creativecommons.org/licenses/by/4.0
https://www.elsevier.com/tdm/userlicense/1.0
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c440t-e5ada439e1a759752b0ed9a571802ff67072565194ef84e001301fc7b0f4f82f3
Notes ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
OpenAccessLink https://doi.org/10.1016/s0021-9258(17)32402-x
PMID 8027053
PQID 16933165
PQPubID 23462
PageCount 6
ParticipantIDs proquest_miscellaneous_76572494
proquest_miscellaneous_16933165
crossref_primary_10_1016_S0021_9258_17_32402_X
pubmed_primary_8027053
pascalfrancis_primary_4234881
highwire_biochem_269_27_17954
ProviderPackageCode RHF
RHI
PublicationCentury 1900
PublicationDate 1994-07-08
PublicationDateYYYYMMDD 1994-07-08
PublicationDate_xml – month: 07
  year: 1994
  text: 1994-07-08
  day: 08
PublicationDecade 1990
PublicationPlace Bethesda, MD
PublicationPlace_xml – name: Bethesda, MD
– name: United States
PublicationTitle The Journal of biological chemistry
PublicationTitleAlternate J Biol Chem
PublicationYear 1994
Publisher American Society for Biochemistry and Molecular Biology
Publisher_xml – name: American Society for Biochemistry and Molecular Biology
References Harris (10.1016/S0021-9258(17)32402-X_bib20) 1982; 90
Kagan (10.1016/S0021-9258(17)32402-X_bib42) 1973; 330
Dontsov (10.1016/S0021-9258(17)32402-X_bib39) 1978; 43
Lee (10.1016/S0021-9258(17)32402-X_bib53) 1982; 90
Srere (10.1016/S0021-9258(17)32402-X_bib50) 1990; 268
Magnani (10.1016/S0021-9258(17)32402-X_bib52) 1980; 255
De Luca (10.1016/S0021-9258(17)32402-X_bib51) 1983; 226
Ii (10.1016/S0021-9258(17)32402-X_bib34) 1974; 350
Schnetkamp (10.1016/S0021-9258(17)32402-X_bib4) 1981; 672
Hsu (10.1016/S0021-9258(17)32402-X_bib12) 1990; 265
Winkler (10.1016/S0021-9258(17)32402-X_bib10) 1981
Easterby (10.1016/S0021-9258(17)32402-X_bib19) 1982; 90
Kulbe (10.1016/S0021-9258(17)32402-X_bib21) 1982; 90
Wald (10.1016/S0021-9258(17)32402-X_bib24) 1953; 37
Shichi (10.1016/S0021-9258(17)32402-X_bib44) 1983
Lopez-Escalera (10.1016/S0021-9258(17)32402-X_bib14) 1991; 30
Schnetkamp (10.1016/S0021-9258(17)32402-X_bib29) 1979; 552
Robinson (10.1016/S0021-9258(17)32402-X_bib25) 1979; 280
Gaetani (10.1016/S0021-9258(17)32402-X_bib48) 1974; 71
Daemen (10.1016/S0021-9258(17)32402-X_bib40) 1973; 300
Bresnick (10.1016/S0021-9258(17)32402-X_bib41) 1970; 9
Winkler (10.1016/S0021-9258(17)32402-X_bib11) 1981; 77
Wallimann (10.1016/S0021-9258(17)32402-X_bib8) 1986; 83
Thomson (10.1016/S0021-9258(17)32402-X_bib17) 1977; 22
Lowry (10.1016/S0021-9258(17)32402-X_bib5) 1956; 220
Hsu (10.1016/S0021-9258(17)32402-X_bib13) 1991; 266
Scott (10.1016/S0021-9258(17)32402-X_bib32) 1963; 238
Harrison (10.1016/S0021-9258(17)32402-X_bib36) 1991; 266
Brin (10.1016/S0021-9258(17)32402-X_bib45) 1958; 230
Futterman (10.1016/S0021-9258(17)32402-X_bib3) 1970; 17
Acan (10.1016/S0021-9258(17)32402-X_bib33) 1989; 250
Matchinsky (10.1016/S0021-9258(17)32402-X_bib27) 1968; 15
Gregersen (10.1016/S0021-9258(17)32402-X_bib26) 1961
Clegg (10.1016/S0021-9258(17)32402-X_bib16) 1988; 255
Ames (10.1016/S0021-9258(17)32402-X_bib35) 1986; 261
Farnsworth (10.1016/S0021-9258(17)32402-X_bib43) 1976; 443
Futterman (10.1016/S0021-9258(17)32402-X_bib18) 1961; 236
McConnell (10.1016/S0021-9258(17)32402-X_bib2) 1969; 184
Murphy (10.1016/S0021-9258(17)32402-X_bib46) 1960; 55
Kahn (10.1016/S0021-9258(17)32402-X_bib22) 1982; 90
Nielsen (10.1016/S0021-9258(17)32402-X_bib28) 1970; 211
Nicotra (10.1016/S0021-9258(17)32402-X_bib31) 1982; 257
Lolley (10.1016/S0021-9258(17)32402-X_bib7) 1969; 73
Lowry (10.1016/S0021-9258(17)32402-X_bib6) 1961; 236
Berne (10.1016/S0021-9258(17)32402-X_bib38) 1988
Staal (10.1016/S0021-9258(17)32402-X_bib23) 1969; 185
Evans (10.1016/S0021-9258(17)32402-X_bib37) 1972; 4
Futterman (10.1016/S0021-9258(17)32402-X_bib1) 1963; 238
Molday (10.1016/S0021-9258(17)32402-X_bib15) 1987; 28
Keleti (10.1016/S0021-9258(17)32402-X_bib49) 1989; 53
Albrecht (10.1016/S0021-9258(17)32402-X_bib47) 1971; 20
Tombes (10.1016/S0021-9258(17)32402-X_bib9) 1985; 41
Cohen (10.1016/S0021-9258(17)32402-X_bib30) 1960; 5
References_xml – volume: 73
  start-page: 9
  year: 1969
  ident: 10.1016/S0021-9258(17)32402-X_bib7
  publication-title: J. Cellular Physiol.
  doi: 10.1002/jcp.1040730103
  contributor:
    fullname: Lolley
– volume: 185
  start-page: 39
  year: 1969
  ident: 10.1016/S0021-9258(17)32402-X_bib23
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0005-2744(69)90280-0
  contributor:
    fullname: Staal
– volume: 226
  start-page: 285
  year: 1983
  ident: 10.1016/S0021-9258(17)32402-X_bib51
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1016/0003-9861(83)90295-3
  contributor:
    fullname: De Luca
– volume: 250
  start-page: 72
  year: 1989
  ident: 10.1016/S0021-9258(17)32402-X_bib33
  publication-title: FEBS Lett.
  doi: 10.1016/0014-5793(89)80687-8
  contributor:
    fullname: Acan
– volume: 266
  start-page: 4106
  year: 1991
  ident: 10.1016/S0021-9258(17)32402-X_bib36
  publication-title: J. Biol. Chem
  doi: 10.1016/S0021-9258(20)64292-2
  contributor:
    fullname: Harrison
– volume: 266
  start-page: 21745
  year: 1991
  ident: 10.1016/S0021-9258(17)32402-X_bib13
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)54699-8
  contributor:
    fullname: Hsu
– volume: 236
  start-page: 1652
  year: 1961
  ident: 10.1016/S0021-9258(17)32402-X_bib18
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)63279-5
  contributor:
    fullname: Futterman
– start-page: 227
  year: 1981
  ident: 10.1016/S0021-9258(17)32402-X_bib10
  contributor:
    fullname: Winkler
– volume: 90
  start-page: 121
  year: 1982
  ident: 10.1016/S0021-9258(17)32402-X_bib53
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(82)90117-3
  contributor:
    fullname: Lee
– volume: 255
  start-page: 335
  year: 1988
  ident: 10.1016/S0021-9258(17)32402-X_bib16
  publication-title: Biochem. J.
  contributor:
    fullname: Clegg
– volume: 261
  start-page: 13034
  year: 1986
  ident: 10.1016/S0021-9258(17)32402-X_bib35
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)69267-1
  contributor:
    fullname: Ames
– volume: 236
  start-page: 2813
  year: 1961
  ident: 10.1016/S0021-9258(17)32402-X_bib6
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)61742-4
  contributor:
    fullname: Lowry
– volume: 71
  start-page: 3584
  year: 1974
  ident: 10.1016/S0021-9258(17)32402-X_bib48
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.71.9.3584
  contributor:
    fullname: Gaetani
– volume: 90
  start-page: 115
  year: 1982
  ident: 10.1016/S0021-9258(17)32402-X_bib21
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(82)90116-1
  contributor:
    fullname: Kulbe
– volume: 300
  start-page: 255
  year: 1973
  ident: 10.1016/S0021-9258(17)32402-X_bib40
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0304-4157(73)90006-3
  contributor:
    fullname: Daemen
– volume: 77
  start-page: 667
  year: 1981
  ident: 10.1016/S0021-9258(17)32402-X_bib11
  publication-title: J. Gen. Physiol.
  doi: 10.1085/jgp.77.6.667
  contributor:
    fullname: Winkler
– volume: 255
  start-page: 1752
  year: 1980
  ident: 10.1016/S0021-9258(17)32402-X_bib52
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)86096-9
  contributor:
    fullname: Magnani
– start-page: 359
  year: 1988
  ident: 10.1016/S0021-9258(17)32402-X_bib38
  contributor:
    fullname: Berne
– volume: 90
  start-page: 131
  year: 1982
  ident: 10.1016/S0021-9258(17)32402-X_bib22
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(82)90119-7
  contributor:
    fullname: Kahn
– volume: 9
  start-page: 372
  year: 1970
  ident: 10.1016/S0021-9258(17)32402-X_bib41
  publication-title: Invest. Ophthalmol.
  contributor:
    fullname: Bresnick
– volume: 90
  start-page: 11
  year: 1982
  ident: 10.1016/S0021-9258(17)32402-X_bib19
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(82)90098-2
  contributor:
    fullname: Easterby
– volume: 43
  start-page: 471
  year: 1978
  ident: 10.1016/S0021-9258(17)32402-X_bib39
  publication-title: Biochemistry U. S. S. R.
  contributor:
    fullname: Dontsov
– volume: 230
  start-page: 307
  year: 1958
  ident: 10.1016/S0021-9258(17)32402-X_bib45
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)70565-6
  contributor:
    fullname: Brin
– volume: 211
  start-page: 10
  year: 1970
  ident: 10.1016/S0021-9258(17)32402-X_bib28
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0005-2736(70)90118-5
  contributor:
    fullname: Nielsen
– volume: 83
  start-page: 3816
  year: 1986
  ident: 10.1016/S0021-9258(17)32402-X_bib8
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.83.11.3816
  contributor:
    fullname: Wallimann
– volume: 238
  start-page: 1145
  year: 1963
  ident: 10.1016/S0021-9258(17)32402-X_bib1
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)81273-X
  contributor:
    fullname: Futterman
– volume: 28
  start-page: 50
  year: 1987
  ident: 10.1016/S0021-9258(17)32402-X_bib15
  publication-title: Invest. Ophthalmol. Vis. Sci.
  contributor:
    fullname: Molday
– start-page: 36
  year: 1983
  ident: 10.1016/S0021-9258(17)32402-X_bib44
  contributor:
    fullname: Shichi
– volume: 350
  start-page: 151
  year: 1974
  ident: 10.1016/S0021-9258(17)32402-X_bib34
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0005-2744(74)90213-7
  contributor:
    fullname: Ii
– volume: 53
  start-page: 105
  year: 1989
  ident: 10.1016/S0021-9258(17)32402-X_bib49
  publication-title: Prog. Biophys. Mol. Biol.
  doi: 10.1016/0079-6107(89)90016-3
  contributor:
    fullname: Keleti
– volume: 672
  start-page: 307
  year: 1981
  ident: 10.1016/S0021-9258(17)32402-X_bib4
  publication-title: Biochim. Biophys. Acta.
  doi: 10.1016/0304-4165(81)90298-1
  contributor:
    fullname: Schnetkamp
– volume: 41
  start-page: 325
  year: 1985
  ident: 10.1016/S0021-9258(17)32402-X_bib9
  publication-title: Cell
  doi: 10.1016/0092-8674(85)90085-6
  contributor:
    fullname: Tombes
– start-page: 301
  year: 1961
  ident: 10.1016/S0021-9258(17)32402-X_bib26
  contributor:
    fullname: Gregersen
– volume: 238
  start-page: 3928
  year: 1963
  ident: 10.1016/S0021-9258(17)32402-X_bib32
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)51808-1
  contributor:
    fullname: Scott
– volume: 5
  start-page: 253
  year: 1960
  ident: 10.1016/S0021-9258(17)32402-X_bib30
  publication-title: J. Neurochem.
  doi: 10.1111/j.1471-4159.1960.tb13363.x
  contributor:
    fullname: Cohen
– volume: 55
  start-page: 286
  year: 1960
  ident: 10.1016/S0021-9258(17)32402-X_bib46
  publication-title: J. Lab. Clin. Med.
  contributor:
    fullname: Murphy
– volume: 15
  start-page: 643
  year: 1968
  ident: 10.1016/S0021-9258(17)32402-X_bib27
  publication-title: J. Neurochem.
  doi: 10.1111/j.1471-4159.1968.tb08963.x
  contributor:
    fullname: Matchinsky
– volume: 220
  start-page: 879
  year: 1956
  ident: 10.1016/S0021-9258(17)32402-X_bib5
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)65313-X
  contributor:
    fullname: Lowry
– volume: 37
  start-page: 189
  year: 1953
  ident: 10.1016/S0021-9258(17)32402-X_bib24
  publication-title: J. Gen. Physiol.
  doi: 10.1085/jgp.37.2.189
  contributor:
    fullname: Wald
– volume: 20
  start-page: 44
  year: 1971
  ident: 10.1016/S0021-9258(17)32402-X_bib47
  publication-title: Eur. J. Biochem.
  doi: 10.1111/j.1432-1033.1971.tb01360.x
  contributor:
    fullname: Albrecht
– volume: 4
  start-page: 335
  year: 1972
  ident: 10.1016/S0021-9258(17)32402-X_bib37
  publication-title: Microvasc. Res.
  doi: 10.1016/0026-2862(72)90069-6
  contributor:
    fullname: Evans
– volume: 90
  start-page: 45
  year: 1982
  ident: 10.1016/S0021-9258(17)32402-X_bib20
  publication-title: Methods Enzymol.
  contributor:
    fullname: Harris
– volume: 443
  start-page: 556
  year: 1976
  ident: 10.1016/S0021-9258(17)32402-X_bib43
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0005-2787(76)90517-7
  contributor:
    fullname: Farnsworth
– volume: 268
  start-page: 360
  year: 1990
  ident: 10.1016/S0021-9258(17)32402-X_bib50
  publication-title: FEBS Lett
  doi: 10.1016/0014-5793(90)81286-W
  contributor:
    fullname: Srere
– volume: 265
  start-page: 13308
  year: 1990
  ident: 10.1016/S0021-9258(17)32402-X_bib12
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)38299-7
  contributor:
    fullname: Hsu
– volume: 184
  start-page: 11
  year: 1969
  ident: 10.1016/S0021-9258(17)32402-X_bib2
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0304-4165(69)90093-2
  contributor:
    fullname: McConnell
– volume: 257
  start-page: 11836
  year: 1982
  ident: 10.1016/S0021-9258(17)32402-X_bib31
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(18)33840-7
  contributor:
    fullname: Nicotra
– volume: 22
  start-page: 335
  year: 1977
  ident: 10.1016/S0021-9258(17)32402-X_bib17
  publication-title: Life Sci.
  contributor:
    fullname: Thomson
– volume: 552
  start-page: 379
  year: 1979
  ident: 10.1016/S0021-9258(17)32402-X_bib29
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0005-2736(79)90182-2
  contributor:
    fullname: Schnetkamp
– volume: 330
  start-page: 76
  year: 1973
  ident: 10.1016/S0021-9258(17)32402-X_bib42
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0005-2736(73)90285-X
  contributor:
    fullname: Kagan
– volume: 17
  start-page: 149
  year: 1970
  ident: 10.1016/S0021-9258(17)32402-X_bib3
  publication-title: J. Neurochem.
  doi: 10.1111/j.1471-4159.1970.tb02195.x
  contributor:
    fullname: Futterman
– volume: 280
  start-page: 398
  year: 1979
  ident: 10.1016/S0021-9258(17)32402-X_bib25
  publication-title: Nature
  doi: 10.1038/280398a0
  contributor:
    fullname: Robinson
– volume: 30
  start-page: 8970
  year: 1991
  ident: 10.1016/S0021-9258(17)32402-X_bib14
  publication-title: Biochemsitry.
  doi: 10.1021/bi00101a009
  contributor:
    fullname: Lopez-Escalera
SSID ssj0000491
Score 1.8004302
Snippet Glucose metabolism in the photoreceptor rod outer segment produces both ATP (GTP) and NADPH to support phototransduction and NADPH-requiring processes in this...
Glucose metabolism in the photoreceptor rod outer segment produces both ATP (GTP) and NADPH to support phototransduction and NADPH-requiring processes in this...
SourceID proquest
crossref
pubmed
pascalfrancis
highwire
SourceType Aggregation Database
Index Database
Publisher
StartPage 17954
SubjectTerms Adenosine Triphosphate - biosynthesis
Anaerobiosis
Animals
Biological and medical sciences
Cattle
Cell metabolism, cell oxidation
Cell physiology
Fundamental and applied biological sciences. Psychology
Glucose - metabolism
Glutathione Reductase - metabolism
Glycolysis
Guanosine Triphosphate - biosynthesis
Light
Molecular and cellular biology
NADP - metabolism
Oxidation-Reduction
Rod Cell Outer Segment - metabolism
Signal Transduction
Vision, photoreception
Title Glucose metabolism in photoreceptor outer segments. Its role in phototransduction and in NADPH-requiring reactions
URI http://www.jbc.org/content/269/27/17954.abstract
https://www.ncbi.nlm.nih.gov/pubmed/8027053
https://search.proquest.com/docview/16933165
https://search.proquest.com/docview/76572494
Volume 269
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1db9MwFLXKEGIvCDYmCgz8gBAoSpekTp08lvFRQEygbVLfLCexYWhNpjZ9gD_HX-Ne2_noYOLjJaqS1LFyTuxr-_hcQp7wNMiDgkU-fEeBzwoYoGTpJPF5LuNEhZkuNG4U_nA0mZ2yd_N4Phj86KmW1nU2yr__dl_J_6AK5wBX3CX7D8i2hcIJ-A34whEQhuNfYfzG6c0XqgYszzHfBYrCv1QwkFaoV6mWXoU5G7yV-mz2so28t7hQgJLC5s4ae6ti7VKGGy8m72j68uPMXyqUCeNcAkSWeTez97VjWC-etXZO1nCkySLXzt940MHZFCtmdcc7hsbkvBHwFG4XHjMC1aSjSbOa1JeWvjir2uKtSqRJ8OvyavbbNqMMiaxr-0jZtheiQdxYMO83zpFN5OJYaG0EXFsLTYn1n_6lF7ATEsftQ9DyCmdW0Hww8uf9_wCgFwtDjwQG6IE1Lt605b7UXbYiRqiaiLgw1bhGrqMTIyZveP-ps6uH4ZdN2egq0m0hO-hq9yzkz13NtskNV43NMKmxrkblrlwBkNpmXbl6WGTCo5Pb5JbjAZ1akt4hA1XukN1pKetq8Y0-pUZpbODZITcPGwB3ydJxmHYcpmcl3eAwNRymLYcpcJgih9s7-xymQAq8cInDtOXwXXL6-tXJ4cx3eUD8nLGg9lUsCwmBswolh_FvHGWBKlIZc3Qv1HrCAw6BOwxFmNIJU2YxPtQ5zwLNdBLp8R7ZKqtS3SM0z9Ixy0KFcgMWp7FkhdJwJpZBKmUxHpJR89rFhbV7EZ0OEhATiBhgLgxiYj4k-w04IrMfgOgTA65vINaWCsMY6DvDIXncICjgzeNqnSxVtV4JdEkah5P46jv4JOYRS-EZexb6tnBHovt_qNwDst193A_JVr1cq32IsevskeHxT3g80GA
link.rule.ids 314,780,784,27924,27925
linkProvider Colorado Alliance of Research Libraries
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Glucose+metabolism+in+photoreceptor+outer+segments.+Its+role+in+phototransduction+and+in+NADPH-requiring+reactions&rft.jtitle=The+Journal+of+biological+chemistry&rft.au=S+C+Hsu&rft.au=R+S+Molday&rft.date=1994-07-08&rft.pub=American+Society+for+Biochemistry+and+Molecular+Biology&rft.issn=0021-9258&rft.eissn=1083-351X&rft.volume=269&rft.issue=27&rft.spage=17954&rft_id=info:doi/10.1016%2FS0021-9258%2817%2932402-X&rft_id=info%3Apmid%2F8027053&rft.externalDBID=n%2Fa&rft.externalDocID=269_27_17954
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0021-9258&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0021-9258&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0021-9258&client=summon