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Decrease in skin collagen glycation with improved glycemic control in patients with insulin-dependent diabetes

T J Lyons1, K E Bailie, D G Dyer

  • 1Department of Medicine, Altnagelvin Hospital, Londonderry, Northern Ireland, United Kingdom.

The Journal of Clinical Investigation
|June 1, 1991
PubMed
Summary
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Improved glycemic control in diabetics reduced protein glycation in skin collagen. However, existing browning and oxidation damage, like pentosidine and CML, remained unchanged, suggesting irreversible collagen damage.

Area of Science:

  • Biochemistry
  • Diabetology
  • Protein Chemistry

Background:

  • Protein glycation, oxidation, and nonenzymatic browning contribute to diabetic complications.
  • Advanced glycation end-products (AGEs) like fructoselysine (FL), pentosidine, N(epsilon)-(carboxymethyl)lysine (CML), and N(epsilon)-(carboxymethyl)hydroxylysine (CMhL) are key markers.

Purpose of the Study:

  • To investigate the impact of intensive glycemic control on glycation and browning/oxidation products in diabetic skin collagen.
  • To determine if improved glycemic control can reverse existing collagen damage.

Main Methods:

  • Measured FL, pentosidine, fluorescence, CML, and CMhL in skin collagen from 14 diabetic patients before and after 4 months of intensive therapy.
  • Monitored changes in home blood glucose and glycated hemoglobin (HbA1) to assess glycemic control.

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Main Results:

  • Intensive therapy significantly reduced blood glucose and HbA1 levels.
  • A significant decrease in skin collagen glycation (FL levels) was observed.
  • Levels of browning and oxidation products (pentosidine, CML, CMhL) and fluorescence remained unchanged.

Conclusions:

  • Improved glycemic control effectively reduces ongoing protein glycation in long-lived proteins like collagen.
  • The study suggests that cumulative damage to collagen from glycation, oxidation, and browning may be irreversible.
  • Early and sustained glycemic control is crucial for preventing long-term protein damage in diabetic patients.