Table 1.

Selected components of the fructosamine proteome

Species	Protein	Hotspot sites	Extent of modification	Functional impairment	Reference
Human	Apolipoprotein A1	K239	4 %	None	[8]
	Apolipoprotein E	K93	Unknown	Impairs heparin binding	[9]
	Bisphosphoglycerate mutase	K158	Unknown	Inactivation	[10]
	CD59	K41	Unknown	Inactivation	[11]
	Complement factor B	K266	Unknown		[12]
	Gastric inhibitory polypeptide	Y1	Unknown	Increased insulin release	[13]
	Glucagon-like peptide-1	1H	Unknown	Decreased insulin release	[14]
	Hemoglobin α2β2	α-K61, β-V1, β-K66	5 % (α:β, 0.6:1)	Increased oxygen binding in T state.	[15–17]
	Insulin	β-F1		Decreased activity.	[18]
	Microglobulin, β2-	I1	Unknown	Aggregation in chronic renal dialysis.	[19]
	Serum albumin	D1, K199, K439, K525	10 %	Decreased drug binding and leakage through the glomerular filter.	[20, 21]
	Superoxide dismutase-1	K122, K128	Unknown	Inactivation	[22]
Bovine	Crystallin, αA	K11, K78	Unknown		[23]
	Crystallin, αB	K90, K92	Unknown		[23]
	Crystallin, γB	G1, K2	Unknown		[24]
	Glutathione peroxidase-1	K117	Unknown	Inactivated.	[25]
	Insulin	α-G1, β-F1, β-K29	Unknown		[26]
	Major intrinsic peptide	K238, K259	Unknown	Affects membrane permeability.	[27]
	Ribonuclease A	K1, K7, K41	Unknown		[28]
	Serum albumin	K12, K136, K211, K232, K377, K524	10 %		[29]
Rat	Collagen-I	α1-K434	50–70 %	Increased susceptibility to cross-linking.	[30]
		α2-K453	27–33 %
		α2-K479	24–29 %
		α2-K924	22–28 %
	Aldoketo reductase 1 A1	K67, K84, K140	18 %	Inactivation.	[31]

Extent of modification: data are for extent of modification in vivo of healthy subjects except for rat collagen which are percentage of total fructosamine adducts on each polypeptide chain (α1 and α2) from rat donors 6–36 months of age