Cloning and Expression of Human Liver Rhodanese cDNA

Aita, Noriko; Ishii, Kazuyuki; Akamatsu, Yousuke; Ogasawara, Yuuki; Tanabe, Shinzo

doi:10.1006/bbrc.1996.6046

Cited by 17 publications

(9 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To construct a fusion protein library, we selected six proteins to comprise the fusion proteins: GFP (27 KDa),29 hCAII (29 KDa),30 hRHO (33 KDa),31 hDHFR (22 KDa),32 eDHFR (18 KDa),33 and eTRPA (28 KDa) 34. All of these proteins exist in monomer.…”

Section: Resultsmentioning

confidence: 99%

Tolerance for random recombination of domains in prokaryotic and eukaryotic translation systems: Limited interdomain misfolding in a eukaryotic translation system

et al. 2006

View full text Add to dashboard Cite

It has been proposed that eukaryotic translation systems have a greater capacity for cotranslational folding of domains than prokaryotic translation systems, which reduces interdomain misfolding in multidomain proteins and, therefore, leads to tolerance for random recombination of domains. However, there has been a controversy as to whether prokaryotic and eukaryotic translation systems differ in the capacity for cotranslational domain folding. Here, to examine whether these systems differ in the tolerance for the random domain recombination, we systematically combined six proteins, out of which four are soluble and two are insoluble when produced in an Escherichia coli and a wheat germ cell-free protein synthesis systems, to construct a fusion protein library. Forty out of 60 two-domain proteins and 114 out of 120 three-domain proteins were more soluble when produced in the wheat system than in the E. coli system. Statistical analyses of the solubilities and the activities indicated that, in the wheat system but not in the E. coli system, the two soluble domains comprised mainly of beta-sheets tend to avoid interdomain misfolding and to fold properly even at the neighbor of the misfolded domains. These results demonstrate that a eukaryotic system permits the concomitance of a wider variety of domains within a single polypeptide chain than a prokaryotic system, which is probably due to the difference in the capacity for cotranslational folding. This difference is likely to be related to the postulated difference in the tolerance for random recombination of domains.

show abstract

Section: Resultsmentioning

confidence: 99%

Tolerance for random recombination of domains in prokaryotic and eukaryotic translation systems: Limited interdomain misfolding in a eukaryotic translation system

et al. 2006

View full text Add to dashboard Cite

show abstract

“…2005), CBR1, a monomeric NADPH‐dependent oxidoreductase with wide substrate specificity for numerous carbonyl compounds (Jarabak & Harvey 1993; Ohara et al. 1995), and TST, a peptide‐modifying enzyme that is also postulated to be capable of detoxifying cyanide ions (Aita et al. 1997).…”

Section: Discussionmentioning

confidence: 99%

“…Consistent with previous observations (Meinl et al 2008), the sulfotransferase SULT1B1, another member of phase II-conjugating enzymes, was also upregulated during Caco-2 differentiation. Additional proteins involved in xenobiotic metabolism have been detected to be upregulated by our proteomic approach; these are CES1, an esterase known to hydrolyze aromatic and aliphatic esters (Quinney et al 2005), CBR1, a monomeric NADPH-dependent oxidoreductase with wide substrate specificity for numerous carbonyl compounds (Jarabak & Harvey 1993;Ohara et al 1995), and TST, a peptide-modifying enzyme that is also postulated to be capable of detoxifying cyanide ions (Aita et al 1997). Finally, AKR1C1 and AKR1C2, both upregulated in differentiated cells, catalyze the conversion of various aldehydes and ketones to their corresponding alcohols by utilizing NADH and ⁄ or NADPH as cofactors.…”

Section: Xenobiotic and Drug Metabolismmentioning

confidence: 99%

Analysis of proteomic changes induced upon cellular differentiation of the human intestinal cell line Caco‐2

Buhrke¹,

Lengler

Lampen

2011

Dev Growth Differ

View full text Add to dashboard Cite

The human intestinal cell line Caco-2 is a well-established model system to study cellular differentiation of human enterocytes of intestinal origin, because these cells have the capability to differentiate spontaneously into polarized cells with morphological and biochemical features of small intestinal enterocytes. Therefore, the cells are widely used as an in vitro model for the human intestinal barrier. In this study, a proteomic approach was used to identify the molecular marker of intestinal cellular differentiation. The proteome of proliferating Caco-2 cells was compared with that of fully differentiated cells. Two-dimensional gel analysis yielded 53 proteins that were differently regulated during the differentiation process. Pathway analysis conducted with those 34 proteins that were identified by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis revealed subsets of proteins with common molecular and cellular function. It was shown that proteins involved in xenobiotic and drug metabolism as well as in lipid metabolism were upregulated upon cellular differentiation. In parallel, proteins associated with proliferation, cell growth and cancer were downregulated, reflecting the loss of the tumorigenic phenotype of the cells. Thus, the proteomic approach in combination with a literature-based pathway analysis yielded valuable information about the differentiation process of Caco-2 cells on the molecular level that contributes to the understanding of the development of colon cancer or inflammatory diseases such as ulcerative colitis -diseases associated with an imbalanced differentiation process of intestinal cells.

show abstract

“…The gene that encodes human 3MST (MPST), also known as liver rhodanese and thiosulfate sulfurtransferase 2 (TST2), is located on chromosome 22 (22q11.2) and encodes at least three splice variants (6,50). This gene should not be confused with thiosulfate sulfurtransferase (TST) or rhodanese, which is immediately adjacent on chromosome 22 (22q13.1) but encodes a distinct enzyme (2). Polymorphisms in 3MST may underlie mercaptolactate-cysteine disulfiduria (6).…”

Section: The First Criterion: H 2 S Is a Gasmentioning

confidence: 99%

Endogenous Production of H₂S in the Gastrointestinal Tract: Still in Search of a Physiologic Function

Linden

Levitt

Farrugia

et al. 2010

Antioxidants & Redox Signaling

102

View full text Add to dashboard Cite

Hydrogen sulfide (H 2 S) has long been associated with the gastrointestinal tract, especially the bacteria-derived H 2 S present in flatus. Along with evidence from other organ systems, the finding that gastrointestinal tissues are capable of endogenous production of H 2 S has led to the hypothesis that H 2 S is an endogenous gaseous signaling molecule. In this review, the criteria of gasotransmitters are reexamined, and evidence from the literature regarding H 2 S as a gaseous signaling molecule is discussed. H 2 S is produced enzymatically by gastrointestinal tissues, but evidence is lacking on whether H 2 S production is regulated. H 2 S causes well-defined physiologic effects in gastrointestinal tissues, but evidence for a receptor for H 2 S is lacking. H 2 S is inactivated through enzymatic oxidation, but evidence is lacking on whether manipulating H 2 S oxidation alters endogenous cell signaling. Remaining questions regarding the role of H 2 S as a gaseous signaling molecule in the gastrointestinal tract suggest that H 2 S currently remains a molecule in search of a physiologic function. Antioxid. Redox Signal. 12, 1135-1146.

show abstract

Cloning and Expression of Human Liver Rhodanese cDNA

Cited by 17 publications

References 14 publications

Tolerance for random recombination of domains in prokaryotic and eukaryotic translation systems: Limited interdomain misfolding in a eukaryotic translation system

Tolerance for random recombination of domains in prokaryotic and eukaryotic translation systems: Limited interdomain misfolding in a eukaryotic translation system

Analysis of proteomic changes induced upon cellular differentiation of the human intestinal cell line Caco‐2

Endogenous Production of H₂S in the Gastrointestinal Tract: Still in Search of a Physiologic Function

Contact Info

Product

Resources

About

Cloning and Expression of Human Liver Rhodanese cDNA

Cited by 17 publications

References 14 publications

Tolerance for random recombination of domains in prokaryotic and eukaryotic translation systems: Limited interdomain misfolding in a eukaryotic translation system

Tolerance for random recombination of domains in prokaryotic and eukaryotic translation systems: Limited interdomain misfolding in a eukaryotic translation system

Analysis of proteomic changes induced upon cellular differentiation of the human intestinal cell line Caco‐2

Endogenous Production of H2S in the Gastrointestinal Tract: Still in Search of a Physiologic Function

Contact Info

Product

Resources

About

Endogenous Production of H₂S in the Gastrointestinal Tract: Still in Search of a Physiologic Function