Methylated lysine in storage body protein of sheep with hereditary ceroid-lipofuscinosis

1992 ◽  
Vol 1138 (2) ◽  
pp. 97-108 ◽  
Author(s):  
Martin L. Katz ◽  
Klaus O. Gerhardt
Keyword(s):  
Body Protein ◽  
Ceroid Lipofuscinosis ◽  
Storage Body ◽  
Methylated Lysine

scholarly journals Mitochondrial ATP synthase subunit c stored in hereditary ceroid-lipofuscinosis contains trimethyl-lysine

1995 ◽  
Vol 310 (3) ◽  
pp. 887-892 ◽  
Author(s):  
M L Katz ◽  
C L Gao ◽  
J A Tompkins ◽  
R T Bronson ◽  
D T Chin
Keyword(s):  
Atp Synthase ◽  
Hereditary Disease ◽  
Lysosomal Storage ◽  
Juvenile Form ◽  
Body Protein ◽  
C Protein ◽  
Subunit C ◽  
Ceroid Lipofuscinosis ◽  
Mitochondrial Atp Synthase ◽  
Storage Body

The subunit c protein of mitochondrial ATP synthase accumulates in lysosomal storage bodies of numerous tissues in human subjects with certain forms of ceroid-lipofuscinosis, a degenerative hereditary disease. Subunit c appears to constitute a major fraction of the total storage-body protein. Lysosomal accumulation of subunit c has also been reported in putative animal models (dogs, sheep and mice) for ceroid-lipofuscinosis. In humans with the juvenile form of the disease, hydrolysates of total storage-body protein have been found to contain significant amounts of epsilon-N-trimethyl-lysine (TML). TML is also abundant in storage-body protein hydrolysates from affected dogs and sheep. These findings suggested that one or both of the two lysine residues of subunit c might be methylated in the stored form of the protein. The normal subunit c protein from mitochondria does not appear to be methylated. In a putative canine model for human juvenile ceroid-lipofuscinosis, residue 43 of the storage-body subunit c was previously found to be TML. In the present study, subunit c was isolated from the storage bodies of humans with juvenile ceroid-lipofuscinosis, and from sheep and mice with apparently analogous diseases. In all three species, partial amino acid sequence analysis of the stored subunit c indicated that the protein contained TML at residue 43. These findings strongly suggest that specific methylation of lysine residue 43 of mitochondrial ATP synthase plays a central role in the lysosomal storage of this protein.

Neuronal Ceroid Lipofuscinosis: The Increasing Spectrum of an Old Disease

2014 ◽  
Vol 14 (8) ◽  
pp. 1043-1051 ◽  
Author(s):  
A. Simonati ◽  
F. Pezzini ◽  
F. Moro ◽  
F.M. Santorelli
Keyword(s):  
Neuronal Ceroid Lipofuscinosis ◽  
Ceroid Lipofuscinosis

scholarly journals Whole-body arginine dimethylation is associated with all-cause mortality in adult renal transplant recipients

Amino Acids ◽  
2021 ◽  
Author(s):  
Adrian Post ◽  
Alexander Bollenbach ◽  
Stephan J. L. Bakker ◽  
Dimitrios Tsikas
Keyword(s):  
Renal Transplant ◽  
Excretion Rate ◽  
Whole Body ◽  
Renal Transplant Recipients ◽  
Transplant Recipients ◽  
Kidney Donors ◽  
Body Protein ◽  
All Cause Mortality ◽  
Arginine Residues ◽  
Excretion Rates

AbstractArginine residues in proteins can be singly or doubly methylated post-translationally. Proteolysis of arginine-methylated proteins provides monomethyl arginine, asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA). ADMA and SDMA are considered cardiovascular risk factors, with the underlying mechanisms being not yet fully understood. SDMA lacks appreciable metabolism and is almost completely eliminated by the kidney, whereas ADMA is extensively metabolized to dimethylamine (DMA), with a minor ADMA fraction of about 10% being excreted unchanged in the urine. Urinary DMA and ADMA are useful measures of whole-body asymmetric arginine-dimethylation, while urinary SDMA serves as a whole-body measure of symmetric arginine-dimethylation. In renal transplant recipients (RTR), we previously found that higher plasma ADMA concentrations and lower urinary ADMA and SDMA concentrations were associated with a higher risk of all-cause mortality. Yet, in this RTR collective, no data were available for urinary DMA. For the present study, we additionally measured the excretion rate of DMA in 24-h collected urine samples of the RTR and of healthy kidney donors in the cohort, with the aim to quantitate whole-body asymmetric (ADMA, DMA) and symmetric (SDMA) arginine-dimethylation. We found that lower DMA excretion rates were associated with higher all-cause mortality, yet not with cardiovascular mortality. In the healthy donors, kidney donation was associated with considerable decreases in ADMA (by − 39%, P < 0.0001) and SDMA (by − 21%, P < 0.0001) excretion rates, yet there was no significant change in DMA (by − 9%, P = 0.226) excretion rate. Our results suggest that protein-arginine dimethylation is altered in RTR compared to healthy kidney donors and that it is pronouncedly shifted from symmetric to asymmetric arginine-dimethylation, with whole-body protein-arginine dimethylation being almost unaffected.

scholarly journals 224 A method for estimating the target for protein energy retention in sheep

2020 ◽  
Vol 98 (Supplement_4) ◽  
pp. 143-143
Author(s):  
Holland C Dougherty ◽  
Hutton Oddy ◽  
Mark Evered ◽  
James W Oltjen
Keyword(s):  
Body Composition ◽  
Protein Content ◽  
Heat Production ◽  
Crude Protein ◽  
Muscle Protein ◽  
Energy Utilization ◽  
Body Protein ◽  
Protein Mass ◽  
Reference Weight ◽  
Animal Growth

Abstract Target protein mass at maturity is a common “attractor” used in animal models to derive components of animal growth. This target muscle protein at maturity, M*, is used as a driver of a model of animal growth and body composition with pools representing muscle and visceral protein; where viscera is heart, lungs, liver, kidneys, reticulorumen and gastrointestinal tract; and muscle is non-visceral protein. This M* term then drives changes in protein mass and heat production, based on literature data stating that heat production scales linearly with protein mass but not liveweight. This led us to adopt a modelling approach where energy utilization is directly related to protein content of the animal, and energy not lost as heat or deposited as protein is fat. To maintain continuity with existing feeding systems we estimate M* from Standard Reference Weight (SRW) as follows: M* (kJ) = SRW * SHRINK * (1-FMAT) * (MUSC) * (CPM)* 23800. Where SRW is standard reference weight (kg), SHRINK is the ratio of empty body to live weight (0.86), FMAT is proportion of fat in the empty body at maturity (0.30), MUSC is the proportion of empty body protein that is in muscle (0.85), CPM is the crude protein content of fat-free muscle at maturity (0.21), and 23800 is the energetic content (kJ) of a kilogram of crude protein. Values for SHRINK, FMAT, MUSC and CPM were derived from a synthesis of our own experimental data and the literature. For sheep, these values show M* to be: M* (kJ) = SRW * 0.86* (1-0.3) * 0.85 * 0.21 *23800 = SRW * 2557. This method allows for use of existing knowledge regarding standard reference weight and other parameters in estimating target muscle mass at maturity, as part of a model of body composition and performance in ruminants.

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