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Glycosylation and Cross‐linkage of Cardiac Myosin in Diabetic Subjects: A Post‐mortem Study
Author(s) -
Yudkin J. S.,
Cooper M. B.,
Gould B. J.,
Oughton J.
Publication year - 1988
Publication title -
diabetic medicine
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.474
H-Index - 145
eISSN - 1464-5491
pISSN - 0742-3071
DOI - 10.1111/j.1464-5491.1988.tb01001.x
Subject(s) - medicine , myosin , glycosylation , sephadex , endocrinology , cardiology , biochemistry , chemistry , enzyme
We have investigated the possibility that post‐translational modification of myosin by protein glycosylation and cross‐linking occurs in cardiac myosin. Left ventricular muscle was obtained at post‐mortem from 6 diabetic and 7 non‐diabetic subjects. Myosin was extracted from muscle and purified using Sephadex chromatography followed by protein concentration. Glycosylation was estimated using boronate affinity chromatography with the myosin dissolved in a pyrophosphate buffer, the glycosylated myosin being displaced with sorbitol. Cross‐linkage was assessed by fluorescence at 440 nm upon excitation at 370 nm. Diabetic subjects had significantly higher levels ( p <0.02) of glycosylated myosin (median 6.0% (range 3.8–6.6%)) than non‐diabetic subjects (median 2.4% (range 0.3–4.2%)) but there was no difference in the degree of cross‐linkage as assessed by fluorescence (diabetic median 9.8 (range 6.5–17.0) arbitrary units; non‐diabetic median 9.7 (range 6.0–11.4) arbitrary units). Glycosylation of left ventricular myosin may be of relevance to the excess risk of congestive cardiac failure in diabetic patients.