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Beta cell failure, stress and dm2
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An overview of beta cell failure an its genetics. Fine for chat.
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Beta cell failure, stress and dm2
1.
The
n e w e ng l a n d j o u r na l of m e dic i n e clinical implications of basic research Beta-Cell Failure, Stress, and Type 2 Diabetes Randal J. Kaufman, Ph.D. Type 2 diabetes mellitus is caused by a combina- ate improvement in our understanding of disease tion of genetic and environmental factors that re- mechanisms, partly because genomewide associa- sult in decreased insulin function at sites of insu- tion studies often implicate genes (or nongenic lin action and a reduced ability of pancreatic beta regions) of unknown function, such as CDKAL1. cells to elevate insulin secretion in response to in- Occasionally, discoveries from disparate fields creased blood glucose levels. The variant genes merge to provide new conceptual frameworks that cause susceptibility to diabetes were virtually that improve our mechanistic understanding of unknown until the advent of genomewide associa- disease. A recent example is provided in two stud- tion studies. In 2007, one such study identified ies, by Arragain et al.3 and Wei et al.,4 that link associations between type 2 diabetes and six dif- CDKAL1 with protein translation and show how ferent chromosomal loci.1 The company deCODE this link may be relevant to type 2 diabetes. Genetics subsequently confirmed these associa- It was previously established that some bacte- tions and identified an association with variant rial and eukaryotic transfer RNAs have a specific CDKAL1.2 Subsequent studies increased the num- moiety (the methyl–thio group ms2t6) attached to ber of implicated loci to about 40. Unfortunately, the adenosine residue that is adjacent to the anti- this plethora of loci has not yielded a proportion- codon (Fig. 1). The presence of this moiety on Figure 1. Tinkering with Transfer RNA. Type 2 diabetes is associated with variant CDKAL1. Wei et al.4 recently ascribed a function to this gene: it critically modifies a specific transfer RNA (tRNA) by catalyzing the addition of a methyl–thio moiety (ms2t6) to a residue adjacent to the anticodon (in pink). Mice deficient in beta-cell Cdkal1 incorporate fewer lysine residues into proinsulin, which may contribute to the susceptibility of these mice to type 2 diabetes. n engl j med 365;20 nejm.org november 17, 2011 1931 The New England Journal of Medicine Downloaded from nejm.org by RUY PANTOJA on November 17, 2011. For personal use only. No other uses without permission. Copyright © 2011 Massachusetts Medical Society. All rights reserved.
2.
The
n e w e ng l a n d j o u r na l of m e dic i n e Figure 2. Interfering with Insulin Production. The production of mature insulin takes place within the beta cell and depends on the cleavage of the preproinsulin and proinsulin molecules. The cleavage site at the junction of the A chain and the C-peptide contains a lysine residue, which is critical for cleavage. transfer RNAs is essential for faithful transla- the adenosine residue. In the research group’s tion from messenger RNA to protein. Arragain et most recent study, Wei et al. report that CDKAL1 al. report that CDKAL1 is an enzyme (a methyl- targets a specific transfer RNA — tRNALys(UUU) thiotransferase) and that it adds the moiety to (Fig. 1) — which adds a lysine residue during pro- 1932 n engl j med 365;20 nejm.org november 17, 2011 The New England Journal of Medicine Downloaded from nejm.org by RUY PANTOJA on November 17, 2011. For personal use only. No other uses without permission. Copyright © 2011 Massachusetts Medical Society. All rights reserved.
3.
clinical implications of
basic research tein synthesis (i.e., during translation from mes- sight into how variant CDKAL1 may cause sus- senger RNA to protein) (Fig. 2). In other words, ceptibility to type 2 diabetes. Several questions CDKAL1 seems to have a global effect on pro- may be addressed through future study. The au- tein production by ensuring faithful translation thors propose that a failure to incorporate lysine of the AAA codon (encoding lysine) through its results in the misfolding of proinsulin and pre- mediation of a highly specific event (the modi- vents proteolytic processing. Is this indeed the fication of a specific amino acid residue of case, and if it is, what amino acids (if any) re- tRNALys[UUU]). The investigators went on to ab- place lysine? If a general deficiency of lysine in- rogate Cdkal1 in the beta cells of mice and ob- corporation into protein causes protein misfold- served a diminished insulin response to an intra- ing, perhaps the cellular response to protein peritoneal injection of glucose. These events misfolding affects the production of insulin. were exacerbated in mice that were fed a high- There are now a number of examples in which fat diet for several weeks. protein misfolding in the beta cell prevents pro- How does an abrogation of Cdkal1 in the beta insulin processing and appropriate trafficking cell result in a feeble insulin response? One of between the endoplasmic reticulum and the the most attractive hypotheses is the apparent Golgi apparatus, thus causing stress and a dis- failure of the mutant beta cell to process the ruption in mitochondrial structure. Because proinsulin protein into insulin. The authors CDKAL1 is strongly expressed in the endoplas- found that proinsulin in the mutant cells had a mic reticulum, its own misfolding (assuming lower lysine content than proinsulin in wild-type that such occurs) may affect other folding, pro- cells. They also found that levels of C-peptide (a cessing, or quality-control events that may cause by-product of proinsulin processing) were low- an accumulation of unfolded protein and beta- er in the islets and serum of the mutant mice. cell death. In a broader aspect, there are now Linking these two observations is the fact that many associations between oxidative stress and lysine makes up the cleavage site between C-pep- beta-cell failure. It is interesting to consider that tide and the A chain of insulin (Fig. 2). Thus, a CDKAL1, owing to its composition, may be ex- deficiency of lysine content in proinsulin would quisitely sensitive to oxidation. As the molecular be predicted to result in a molecule that is re- mechanisms of CDKAL1 are revealed, researchers sistant to cleavage at the junction between the may consider small-molecule mediators to pre- C-peptide and the A chain. vent the progression of type 2 diabetes in pa- However, it is clear that the general health of tients who carry CDKAL1 risk variants. the mutant beta cell is also compromised. For ex- Disclosure forms provided by the author are available with the full text of this article at NEJM.org. ample, the authors observed an increase in expres- sion of stress molecules in the endoplasmic re- From the Center for Neuroscience, Aging, and Stem Cell Research, ticulum. Such stress is likely to be caused by an Sanford-Burnham Medical Research Institute, La Jolla, CA. increased number of proteins (including insulin) 1. Sladek R, Rocheleau G, Rung J, et al. A genome-wide asso- that are misfolded because they are deficient in ciation study identifies novel risk loci for type 2 diabetes. Nature lysine. Moreover, there is scanty cell-surface ex- 2007;445:881-5. 2. Steinthorsdottir V, Thorleifsson G, Reynisdottir I, et al. pression of the Glut2 receptor on the mutant A variant in CDKAL1 influences insulin response and risk of beta cell. (Glut2 transports extracellular glucose type 2 diabetes. Nat Genet 2007;39:770-5. into the cell, which sets off a chain of events 3. Arragain S, Handelman SK, Forouhar F, et al. Identification of eukaryotic and prokaryotic methylthiotransferase for biosyn- that culminate in the mobilization of insulin- thesis of 2-methylthio-N6-threonylcarbamoyladenosine in tRNA. containing granules.) All, some, or none of these J Biol Chem 2010;285:28425-33. events may be pivotal to the diabetic phenotype 4. Wei FY, Suzuki T, Watanabe S, et al. Deficit of tRNA(Lys) modification by Cdkal1 causes the development of type 2 diabe- of the mutant mice. tes in mice. J Clin Invest 2011;121:3598-608. The authors have provided much-needed in- Copyright © 2011 Massachusetts Medical Society. n engl j med 365;20 nejm.org november 17, 2011 1933 The New England Journal of Medicine Downloaded from nejm.org by RUY PANTOJA on November 17, 2011. For personal use only. No other uses without permission. Copyright © 2011 Massachusetts Medical Society. All rights reserved.
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