Literature DB >> 24194049

Influence ofL-arginine on glucose mediated collagen cross link precursors in patients with diabetes mellitus.

G Lubec1, H Vierhapper, A J Bailey, P Damjancic, P Fasching, T J Sims, D Kampel, C Popow, B Bartosch.   

Abstract

Long term complications of diabetes mellitus are largely due to chemical, structural and mechanical changes of connective tissue proteins involving glucose mediated collagen cross links (GMCC). To date there are only experimental therapeutic approaches for preventing long term complications of diabetes mellitus using the toxic substance aminoguanidine.L-arginine, a nontoxic substance, has been shown to reduce GMCC in animal models of diabetes mellitus. We have now performed a blind placebo controlled study with crossing over of two treatment periods of three months each in 29 patients with diabetes mellitus in order to examine the effect of treatment withL-arginine (2 × 1g daily) on glucose mediated collagen cross links (GMCC). GMCC was evaluated by determining glycosyl lysine (hexosyl lysine) levels in skin punch biopsies. Patients treated byL-arginine showed significantly lower GMCC precursors of skin collagen compared with the placebo treated group (difference of hexosyl lysine as counts/mL/ug hydroxyproline between the first and second skin biopsy 0.11 ± 4.44 vs. 4.03 ± 5.27,t = 2.17,p < 0.05). The only side effects ofL-arginine were gastric pain occurring only in patients who did not follow the instructions to takeL-arginine at meals. We conclude thatL-arginine could be useful for treating long term complications of diabetes mellitus.

Entities:  

Year:  1991        PMID: 24194049     DOI: 10.1007/BF00808093

Source DB:  PubMed          Journal:  Amino Acids        ISSN: 0939-4451            Impact factor:   3.520


  14 in total

1.  Collagen crosslinks: isolation of reduced N -hexosylhydroxylysine from borohydride-reduced calf skin insoluble collagen.

Authors:  M L Tanzer; R Fairweather; P M Gallop
Journal:  Arch Biochem Biophys       Date:  1972-07       Impact factor: 4.013

2.  Reduced susceptibility of nonenzymatically glucosylated glomerular basement membrane to proteases: is thickening of diabetic glomerular basement membranes due to reduced proteolytic degradation?

Authors:  G Lubec; A Pollak
Journal:  Ren Physiol       Date:  1980

Review 3.  Search for a biochemical basis of diabetic microangiopathy.

Authors:  R G Spiro
Journal:  Diabetologia       Date:  1976-03       Impact factor: 10.122

4.  Accelerated age-related browning of human collagen in diabetes mellitus.

Authors:  V M Monnier; R R Kohn; A Cerami
Journal:  Proc Natl Acad Sci U S A       Date:  1984-01       Impact factor: 11.205

5.  Arginine-responsive asymptomatic hyperammonemia in the premature infant.

Authors:  M L Batshaw; R C Wachtel; G H Thomas; A Starrett; S W Brusilow
Journal:  J Pediatr       Date:  1984-07       Impact factor: 4.406

6.  Relation between complications of type I diabetes mellitus and collagen-linked fluorescence.

Authors:  V M Monnier; V Vishwanath; K E Frank; C A Elmets; P Dauchot; R R Kohn
Journal:  N Engl J Med       Date:  1986-02-13       Impact factor: 91.245

7.  Thermal stability, mechanical properties and reducible cross-links of rat tail tendon in experimental diabetes.

Authors:  T T Andreassen; K Seyer-Hansen; A J Bailey
Journal:  Biochim Biophys Acta       Date:  1981-10-12

8.  Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking.

Authors:  M Brownlee; H Vlassara; A Kooney; P Ulrich; A Cerami
Journal:  Science       Date:  1986-06-27       Impact factor: 47.728

9.  Effects of age and diabetes mellitus on the solubility and nonenzymatic glucosylation of human skin collagen.

Authors:  S L Schnider; R R Kohn
Journal:  J Clin Invest       Date:  1981-06       Impact factor: 14.808

10.  Evidence for glucose-mediated covalent cross-linking of collagen after glycosylation in vitro.

Authors:  M J Kent; N D Light; A J Bailey
Journal:  Biochem J       Date:  1985-02-01       Impact factor: 3.857

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  3 in total

1.  L-Arginine inhibits in vitro nonenzymatic glycation and advanced glycosylated end product formation of human serum albumin.

Authors:  D A Servetnick; D Bryant; K J Wells-Knecht; P L Wiesenfeld
Journal:  Amino Acids       Date:  1996-03       Impact factor: 3.520

2.  Methylglyoxal, glyoxalases and the development of diabetic complications.

Authors:  P J Thornalley
Journal:  Amino Acids       Date:  1994-02       Impact factor: 3.520

3.  In vivo monitoring of serum protein cross linking in patients with diabetes mellitus. Evidence for pharmacological modification of immunoglobulin G cross links.

Authors:  B Lubec; M Weninger; C Popow; H Vierhapper; J Lunec; G Lubec
Journal:  Amino Acids       Date:  1993-02       Impact factor: 3.520

  3 in total

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