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Article: Remembering Birgit Vennesland (1913-2001), a great biochemist.

Conn, Eric E / Pistorius, Elfriede K / Solomonson, Larry P

2005 Volume 83, Issue 1, Page(s) 11–16

MeSH term(s)	Biochemistry/history ; Carbon Dioxide/metabolism ; Germany ; History, 20th Century ; Norway ; Photosynthesis ; United States
Chemical Substances	Carbon Dioxide (142M471B3J)
Language	English
Publishing date	2005-09-02
Publishing country	Netherlands
Document type	Biography ; Historical Article ; Journal Article ; Portrait
ZDB-ID	1475688-2
ISSN	1573-5079 ; 0166-8595
ISSN (online)	1573-5079
ISSN	0166-8595
DOI	10.1007/s11120-004-5456-y
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Article: Endothelial nitric oxide production is tightly coupled to the citrulline-NO cycle.

Flam, Brenda R / Eichler, Duane C / Solomonson, Larry P

Nitric oxide : biology and chemistry

2007 Volume 17, Issue 3-4, Page(s) 115–121

Abstract: Nitric oxide (NO) is an important vasorelaxant produced along with L-citrulline from L-arginine in a reaction catalyzed by endothelial nitric oxide synthase (eNOS). Previous studies suggested that the recycling of L-citrulline to L-arginine is essential ... ...

Abstract	Nitric oxide (NO) is an important vasorelaxant produced along with L-citrulline from L-arginine in a reaction catalyzed by endothelial nitric oxide synthase (eNOS). Previous studies suggested that the recycling of L-citrulline to L-arginine is essential for NO production in endothelial cells. However, there is no direct evidence demonstrating the degree to which the recycling of L-citrulline to L-arginine is coupled to NO production. We hypothesized that the amount of NO formed would be significantly higher than the amount of L-citrulline formed due to the efficiency of L-citrulline recycling via the citrulline-NO cycle. To test this hypothesis, endothelial cells were incubated with [14C]-L-arginine and stimulated by various agents to produce NO. The extent of NO and [14C]-L-citrulline formation were simultaneously determined. NO production exceeded apparent L-citrulline formation of the order of 8 to 1, under both basal and stimulated conditions. As further support, alpha-methyl-DL-aspartate, an inhibitor of argininosuccinate synthase (AS), a component of the citrulline-NO cycle, inhibited NO production in a dose-dependent manner. The results of this study provide evidence for the essential and efficient coupling of L-citrulline recycling, via the citrulline-NO cycle, to endothelial NO production.
MeSH term(s)	Animals ; Aorta/cytology ; Arginine/metabolism ; Argininosuccinate Synthase/antagonists & inhibitors ; Bradykinin/pharmacology ; Cattle ; Cell Survival/drug effects ; Cells, Cultured ; Citrulline/metabolism ; Dose-Response Relationship, Drug ; Endothelial Cells/cytology ; Endothelial Cells/drug effects ; Endothelial Cells/metabolism ; Enzyme Inhibitors/pharmacology ; Models, Biological ; N-Methylaspartate/analogs & derivatives ; N-Methylaspartate/pharmacology ; Nitric Oxide/metabolism ; Nitric Oxide Synthase Type III/metabolism ; Vanadates/pharmacology
Chemical Substances	Enzyme Inhibitors ; Citrulline (29VT07BGDA) ; Nitric Oxide (31C4KY9ESH) ; Vanadates (3WHH0066W5) ; N-Methylaspartate (6384-92-5) ; 2-methylaspartic acid (866-73-9) ; Arginine (94ZLA3W45F) ; Nitric Oxide Synthase Type III (EC 1.14.13.39) ; Argininosuccinate Synthase (EC 6.3.4.5) ; Bradykinin (S8TIM42R2W)
Language	English
Publishing date	2007-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1362794-6
ISSN	1089-8611 ; 1089-8603
ISSN (online)	1089-8611
ISSN	1089-8603
DOI	10.1016/j.niox.2007.07.001
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Article ; Online: Phosphorylation of argininosuccinate synthase by protein kinase A.

Corbin, Karen D / Pendleton, Laura C / Solomonson, Larry P / Eichler, Duane C

Biochemical and biophysical research communications

2008 Volume 377, Issue 4, Page(s) 1042–1046

Abstract: Argininosuccinate synthase (AS) is essential for endothelial nitric oxide (NO) production and its regulation in this capacity has been studied primarily at the transcriptional level. The dynamics of vascular function suggest that an acute regulation ... ...

Abstract	Argininosuccinate synthase (AS) is essential for endothelial nitric oxide (NO) production and its regulation in this capacity has been studied primarily at the transcriptional level. The dynamics of vascular function suggest that an acute regulation system may mediate AS function. This premise underlies our hypothesis that AS is phosphorylated in vascular endothelium. Immunoprecipitation and immobilized metal affinity chromatography demonstrated that AS is an endogenous phosphoprotein. An in vitro kinase screen revealed that protein kinase A (PKA), a kinase that enhances NO production via eNOS activation, phosphorylated AS. Vascular endothelial growth factor (VEGF) was identified as a candidate pathway for regulating AS phosphorylation since it enhanced NO production and activated PKA and eNOS. MDLA, an AS inhibitor, diminished maximal VEGF-mediated NO production. In addition, immunoprecipitation studies suggested that VEGF enhanced AS phosphorylation. Overall, these results represent the first demonstration that vascular endothelial NO production can be regulated by dynamic AS phosphorylation.
MeSH term(s)	Amino Acid Sequence ; Animals ; Argininosuccinate Synthase/metabolism ; Cattle ; Cells, Cultured ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Endothelium, Vascular/enzymology ; Nitric Oxide/biosynthesis ; Phosphorylation ; Vascular Endothelial Growth Factor A/metabolism
Chemical Substances	Vascular Endothelial Growth Factor A ; Nitric Oxide (31C4KY9ESH) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; Argininosuccinate Synthase (EC 6.3.4.5)
Language	English
Publishing date	2008-12-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2008.10.056
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Article: Argininosuccinate synthase expression is required to maintain nitric oxide production and cell viability in aortic endothelial cells.

Goodwin, Bonnie L / Solomonson, Larry P / Eichler, Duane C

The Journal of biological chemistry

2004 Volume 279, Issue 18, Page(s) 18353–18360

Abstract: Although cellular levels of arginine greatly exceed the apparent K(m) for endothelial nitric-oxide synthase, current evidence suggests that the bulk of this arginine may not be available for nitric oxide (NO) production. We propose that arginine ... ...

Abstract	Although cellular levels of arginine greatly exceed the apparent K(m) for endothelial nitric-oxide synthase, current evidence suggests that the bulk of this arginine may not be available for nitric oxide (NO) production. We propose that arginine regeneration, that is the recycling of citrulline back to arginine, defines the essential source of arginine for NO production. To support this proposal, RNA interference analysis was used to selectively reduce the expression of argininosuccinate synthase (AS), because the only known metabolic role for AS in endothelial cells is in the regeneration of l-arginine from l-citrulline. Western blot analysis demonstrated a significant and dose-dependent reduction of AS protein as a result of AS small interfering RNA treatment with a corresponding diminished capacity to produce basal or stimulated levels of NO, despite saturating levels of arginine in the medium. Unanticipated, however, was the finding that the viability of AS small interfering RNA-treated endothelial cells was significantly decreased when compared with control cells. Trypan blue exclusion analysis suggested that the loss of viability was not because of necrosis. Two indicators, reduced expression of Bcl-2 and an increase in caspase activity, which correlated directly with reduced expression of AS, suggested that the loss of viability was because of apoptosis. The exposure of cells to an NO donor prevented apoptosis associated with reduced AS expression. Overall, these results demonstrate the essential role of AS for endothelial NO production and cell viability.
MeSH term(s)	Animals ; Aorta ; Apoptosis ; Arginine/metabolism ; Argininosuccinate Synthase/biosynthesis ; Argininosuccinate Synthase/physiology ; Cattle ; Cell Survival ; Citrulline/metabolism ; Endothelium, Vascular/cytology ; Gene Silencing ; Nitric Oxide/biosynthesis ; Proto-Oncogene Proteins c-bcl-2/analysis ; RNA, Small Interfering/pharmacology
Chemical Substances	Proto-Oncogene Proteins c-bcl-2 ; RNA, Small Interfering ; Citrulline (29VT07BGDA) ; Nitric Oxide (31C4KY9ESH) ; Arginine (94ZLA3W45F) ; Argininosuccinate Synthase (EC 6.3.4.5)
Language	English
Publishing date	2004-02-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M308160200
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Article: Regulation of endothelial argininosuccinate synthase expression and NO production by an upstream open reading frame.

Pendleton, Laura C / Goodwin, Bonnie L / Solomonson, Larry P / Eichler, Duane C

The Journal of biological chemistry

2005 Volume 280, Issue 25, Page(s) 24252–24260

Abstract: Argininosuccinate synthase (AS) catalyzes the rate-limiting step in the recycling of citrulline to arginine, which in endothelial cells, is tightly coupled to the production of nitric oxide (NO). In previous work, we established that endothelial AS mRNA ... ...

Abstract	Argininosuccinate synthase (AS) catalyzes the rate-limiting step in the recycling of citrulline to arginine, which in endothelial cells, is tightly coupled to the production of nitric oxide (NO). In previous work, we established that endothelial AS mRNA can be initiated from multiple start sites, generating co-expressed mRNA variants with different 5'-untranslated regions (5'-UTRs). One of the 5'-UTRs, the shortest form, represents greater than 90% of the total AS mRNA. Two other extended 5'-UTR forms of AS mRNA, resulting from upstream initiations, contain an out-of-frame, upstream open reading frame (uORF). In this study, the function of the extended 5'-UTRs of AS mRNA was investigated. Single base insertions to place the uORF in-frame, and mutations to extend the uORF, demonstrated functionality, both in vitro with AS constructs and in vivo with luciferase constructs. Overexpression of the uORF suppressed endothelial AS protein expression, whereas specific silencing of the uORF AS mRNAs resulted in the coordinate up-regulation of AS protein and NO production. Expression of the full-length of the uORF was necessary to mediate a trans-suppressive effect on endothelial AS expression, demonstrating that the translation product itself affects regulation. In conclusion, the uORF found in the extended, overlapping 5'-UTR AS mRNA species suppresses endothelial AS expression, providing a novel mechanism for regulating endothelial NO production by limiting the availability of arginine.
MeSH term(s)	5' Untranslated Regions ; Animals ; Argininosuccinate Synthase/genetics ; Argininosuccinate Synthase/metabolism ; Base Sequence ; Cattle ; Cells, Cultured ; Endothelium, Vascular/cytology ; Endothelium, Vascular/enzymology ; Luciferases/genetics ; Molecular Sequence Data ; Mutagenesis ; Nitric Oxide/biosynthesis ; Open Reading Frames ; Protein Biosynthesis ; RNA, Messenger/genetics ; Transcription, Genetic
Chemical Substances	5' Untranslated Regions ; RNA, Messenger ; Nitric Oxide (31C4KY9ESH) ; Luciferases (EC 1.13.12.-) ; Argininosuccinate Synthase (EC 6.3.4.5)
Language	English
Publishing date	2005-04-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M500106200
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Article: Tumor necrosis factor-alpha reduces argininosuccinate synthase expression and nitric oxide production in aortic endothelial cells.

Goodwin, Bonnie L / Pendleton, Laura C / Levy, Monique M / Solomonson, Larry P / Eichler, Duane C

American journal of physiology. Heart and circulatory physiology

2007 Volume 293, Issue 2, Page(s) H1115–21

Abstract: Endothelial dysfunction associated with elevated serum levels of TNF-alpha observed in diabetes, obesity, and congenital heart disease results, in part, from the impaired production of endothelial nitric oxide (NO). Cellular NO production depends ... ...

Abstract	Endothelial dysfunction associated with elevated serum levels of TNF-alpha observed in diabetes, obesity, and congenital heart disease results, in part, from the impaired production of endothelial nitric oxide (NO). Cellular NO production depends absolutely on the availability of arginine, substrate of endothelial nitric oxide synthase (eNOS). In this report, evidence is provided demonstrating that treatment with TNF-alpha (10 ng/ml) suppresses not only eNOS expression but also the availability of arginine via the coordinate suppression of argininosuccinate synthase (AS) expression in aortic endothelial cells. Western blot and real-time RT-PCR demonstrated a significant and dose-dependent reduction of AS protein and mRNA when treated with TNF-alpha with a corresponding decrease in NO production. Reporter gene analysis demonstrated that TNF-alpha suppresses the AS proximal promoter, and EMSA analysis showed reduced binding to three essential Sp1 elements. Inhibitor studies suggested that the repression of AS expression by TNF-alpha may be mediated, in part, via the NF-kappaB signaling pathway. These findings demonstrate that TNF-alpha coordinately downregulates eNOS and AS expression, resulting in a severely impaired citrulline-NO cycle. The downregulation of AS by TNF-alpha is an added insult to endothelial function because of its important role in NO production and in endothelial viability.
MeSH term(s)	Animals ; Aorta/cytology ; Aorta/drug effects ; Aorta/enzymology ; Aorta/metabolism ; Arginine/metabolism ; Argininosuccinate Synthase/biosynthesis ; Argininosuccinate Synthase/genetics ; Cattle ; Cell Nucleus/metabolism ; Cells, Cultured ; Citrulline/metabolism ; Dose-Response Relationship, Drug ; Down-Regulation ; Endothelial Cells/drug effects ; Endothelial Cells/enzymology ; Endothelial Cells/metabolism ; Enzyme Repression ; Genes, Reporter ; Luciferases ; NF-kappa B/metabolism ; Nitric Oxide/metabolism ; Nitric Oxide Synthase Type III/biosynthesis ; Nitric Oxide Synthase Type III/genetics ; Promoter Regions, Genetic ; RNA, Messenger/metabolism ; Signal Transduction/drug effects ; Sp1 Transcription Factor/metabolism ; Sp3 Transcription Factor/metabolism ; Transcription, Genetic ; Transfection ; Tumor Necrosis Factor-alpha/metabolism ; Tumor Necrosis Factor-alpha/pharmacology
Chemical Substances	NF-kappa B ; RNA, Messenger ; Sp1 Transcription Factor ; Tumor Necrosis Factor-alpha ; Sp3 Transcription Factor (148710-94-5) ; Citrulline (29VT07BGDA) ; Nitric Oxide (31C4KY9ESH) ; Arginine (94ZLA3W45F) ; Luciferases (EC 1.13.12.-) ; Nitric Oxide Synthase Type III (EC 1.14.13.39) ; Argininosuccinate Synthase (EC 6.3.4.5)
Language	English
Publishing date	2007-05-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603838-4
ISSN	1522-1539 ; 0363-6135
ISSN (online)	1522-1539
ISSN	0363-6135
DOI	10.1152/ajpheart.01100.2006
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Article ; Online: Troglitazone up-regulates vascular endothelial argininosuccinate synthase.

Goodwin, Bonnie L / Corbin, Karen D / Pendleton, Laura C / Levy, Monique M / Solomonson, Larry P / Eichler, Duane C

Biochemical and biophysical research communications

2008 Volume 370, Issue 2, Page(s) 254–258

Abstract: Vascular endothelial nitric oxide (NO) production via the citrulline-NO cycle not only involves the regulation of endothelial nitric oxide synthase (eNOS), but also regulation of caveolar-localized endothelial argininosuccinate synthase (AS), which ... ...

Abstract	Vascular endothelial nitric oxide (NO) production via the citrulline-NO cycle not only involves the regulation of endothelial nitric oxide synthase (eNOS), but also regulation of caveolar-localized endothelial argininosuccinate synthase (AS), which catalyzes the rate-limiting step of the cycle. In the present study, we demonstrated that exposure of endothelial cells to troglitazone coordinately induced AS expression and NO production. Western blot analysis demonstrated an increase in AS protein expression. This increased expression was due to transcriptional upregulation of AS mRNA, as determined by quantitative real time RT-PCR and inhibition by 1-d-ribofuranosylbenzimidazole (DRB), a transcriptional inhibitor. Reporter gene assays and EMSA analyses identified a distal PPARgamma response element (PPRE) (-2471 to -2458) that mediated the troglitazone increase in AS expression. Overall, this study defines a novel molecular mechanism through which a thiazolidinedione (TZD) like troglitazone supports endothelial function via the transcriptional up-regulation of AS expression.
MeSH term(s)	Animals ; Argininosuccinate Synthase/genetics ; Argininosuccinate Synthase/metabolism ; Base Sequence ; Cattle ; Cell Line ; Chromans/pharmacology ; Endothelium, Vascular/drug effects ; Endothelium, Vascular/enzymology ; Gene Expression Regulation/drug effects ; Ligands ; Nitric Oxide/metabolism ; PPAR gamma/agonists ; PPAR gamma/metabolism ; Response Elements/drug effects ; Thiazolidinediones/pharmacology ; Transcription, Genetic/drug effects ; Up-Regulation
Chemical Substances	Chromans ; Ligands ; PPAR gamma ; Thiazolidinediones ; Nitric Oxide (31C4KY9ESH) ; Argininosuccinate Synthase (EC 6.3.4.5) ; troglitazone (I66ZZ0ZN0E)
Language	English
Publishing date	2008-05-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2008.03.089
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Article: The caveolar nitric oxide synthase/arginine regeneration system for NO production in endothelial cells.

Solomonson, Larry P / Flam, Brenda R / Pendleton, Laura C / Goodwin, Bonnie L / Eichler, Duane C

The Journal of experimental biology

2003 Volume 206, Issue Pt 12, Page(s) 2083–2087

Abstract: The enzyme endothelial nitric oxide synthase (eNOS) catalyzes the conversion of arginine, oxygen and NADPH to NO and citrulline. Previous results suggest an efficient, compartmentalized system for recycling of citrulline to arginine utilized for NO ... ...

Abstract	The enzyme endothelial nitric oxide synthase (eNOS) catalyzes the conversion of arginine, oxygen and NADPH to NO and citrulline. Previous results suggest an efficient, compartmentalized system for recycling of citrulline to arginine utilized for NO production. In support of this hypothesis, the recycling enzymes, argininosuccinate synthase (AS) and argininosuccinate lyase (AL), have been shown to colocalize with eNOS in caveolae, a subcompartment of the plasma membrane. Under unstimulated conditions, the degree of recycling is minimal. Upon stimulation of NO production by bradykinin, however, recycling is co-stimulated to the extent that more than 80% of the citrulline produced is recycled to arginine. These results suggest an efficient caveolar recycling complex that supports the receptor-mediated stimulation of endothelial NO production. To investigate the molecular basis for the unique location and function of endothelial AS and AL, endothelial AS mRNA was compared with liver AS mRNA. No differences were found in the coding region of the mRNA species, but significant differences were found in the 5'-untranslated region (5'-UTR). The results of these studies suggest that sequence in the endothelial AS-encoding gene, represented by position -92 nt to -43 nt from the translation start site in the extended AS mRNA 5'-UTRs, plays an important role in differential and tissue-specific expression. Overall, a strong evidential case has been developed supporting the proposal that arginine availability, governed by a caveolar-localized arginine regeneration system, plays a key role in receptor-mediated endothelial NO production.
MeSH term(s)	Arginine/biosynthesis ; Argininosuccinate Lyase/metabolism ; Argininosuccinate Synthase/genetics ; Argininosuccinate Synthase/metabolism ; Base Sequence ; Cell Membrane/metabolism ; Endothelium, Vascular/enzymology ; Endothelium, Vascular/ultrastructure ; Molecular Sequence Data ; Nitric Oxide/metabolism ; Nitric Oxide Synthase/metabolism
Chemical Substances	Nitric Oxide (31C4KY9ESH) ; Arginine (94ZLA3W45F) ; Nitric Oxide Synthase (EC 1.14.13.39) ; Argininosuccinate Lyase (EC 4.3.2.1) ; Argininosuccinate Synthase (EC 6.3.4.5)
Language	English
Publishing date	2003-05-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	218085-6
ISSN	1477-9145 ; 0022-0949
ISSN (online)	1477-9145
ISSN	0022-0949
DOI	10.1242/jeb.00361
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Article: Endothelial argininosuccinate synthase mRNA 5'-untranslated region diversity. Infrastructure for tissue-specific expression.

Pendleton, Laura C / Goodwin, Bonnie L / Flam, Brenda R / Solomonson, Larry P / Eichler, Duane C

The Journal of biological chemistry

2002 Volume 277, Issue 28, Page(s) 25363–25369

Abstract: Based on the integral role that argininosuccinate synthase (AS) plays in the production of nitric oxide in vascular endothelial cells and urea in liver, an analysis was carried out to determine whether signals reside in the AS mRNA to account for tissue ... ...

Abstract	Based on the integral role that argininosuccinate synthase (AS) plays in the production of nitric oxide in vascular endothelial cells and urea in liver, an analysis was carried out to determine whether signals reside in the AS mRNA to account for tissue differences in AS function and location. Reverse transcriptase-PCR and sequence analysis showed that the AS mRNA coding region was the same for both endothelial cells and liver; however, 5'-RACE analysis (rapid amplification of cDNA ends) identified AS mRNA species in endothelial cells in addition to a major 43-nucleotide (nt) 5'-untranslated region (UTR) AS mRNA with overlapping extended 5'-UTRs of 66 and 92 nt. Comparison to the genomic sequence immediately upstream of the reported transcription start site for the human and mouse AS gene suggested that expression of all three species of bovine endothelial AS mRNA are driven by a common promoter and that 5'-UTR diversity in endothelial cells results from three transcriptional initiation sites within exon 1. RNase protection analysis and real-time reverse transcriptase-PCR verified and quantitated the differential expression of the extended 5'-UTR species relative to the major 43-nt 5'-UTR AS mRNA. In vitro translation studies showed a less pronounced but similar discordant expression. Sequential deletions starting from the 5' terminus of the 92-nt 5'-UTR construct resulted in a corresponding increase in translational efficiency, but the most pronounced effect resulted from mutation of an upstream open reading frame, which restored translational efficiency of the 92-nt 5'-UTR AS mRNA. When the different AS mRNA 5'-UTRs, cloned in front of a luciferase reporter gene, were transfected into endothelial cells, the pattern of luciferase expression was nearly identical to that observed for the different 5'-UTR AS mRNAs in endothelial cells. Given the different roles ascribed for argininosuccinate synthase, urea versus NO production, these results suggest that sequence in the AS gene represented by position -92 to -43 nt from the translation start site in the extended AS mRNA 5'-UTRs plays an important role in differential and tissue-specific expression.
MeSH term(s)	5' Untranslated Regions ; Animals ; Argininosuccinate Synthase/genetics ; Base Sequence ; Cattle ; DNA Primers ; Endothelium, Vascular/cytology ; Endothelium, Vascular/enzymology ; Liver/enzymology ; RNA, Messenger/genetics ; Reverse Transcriptase Polymerase Chain Reaction
Chemical Substances	5' Untranslated Regions ; DNA Primers ; RNA, Messenger ; Argininosuccinate Synthase (EC 6.3.4.5)
Language	English
Publishing date	2002-04-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111677200
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