Management of painful diabetic neuropathy.

Type 2 diabetes mellitus is a prevalent disease in the US which affects more than 15 million people. As the disease progresses over time, neuropathic pain can become a common complication; it is present in more than 50% of individuals with diabetes mellitus aged >60 years. The pathogenesis of diabetic neuropathy is theorized to be multifactorial. Numerous medications, some with different mechanisms of action, have been examined regarding their effects on the symptoms associated with diabetic neuropathy such as pain, paraesthesia and numbness. However, the majority of the studies have included small patient populations. Tricyclic antidepressants, amitriptyline and desipramine in particular, have been relatively well studied and shown to be effective. However, anticholinergic adverse effects may limit their usefulness and may preclude use in the elderly. Studies have also shown gabapentin to be effective and well tolerated in the treatment of diabetic neuropathy. Capsaicin cream provides another treatment option with a favourable adverse effect profile. Many other medications have been evaluated in diabetic neuropathy; however, more placebo-controlled studies with adequate patient populations need to be performed to solidify their role in treatment.

Milk lipoprotein lipases: a review.

Lipoprotein lipase activity has been found in the milks from severals species where it is assumed to result from leakage from the mammary gland into milk. The function of the enzyme in the gland is apparently to assist in the transfer of blood lipoprotein triacylglycerol fatty acids into milk triacylglycerols. Bovine skim milk is one of the richest sources of lipoprotein lipase and this enzyme has been purified extensively (7000 fold) by affinity chromatography. The lipase has a molecular weight of about 62000, is inhibited by protamine sulfate, 1.0 M sodium chloride, apolipoprotein C-I (apolipoprotein-serine), and apolipoprotein C-III (apolipoprotein-alanine). The enzyme is activated by apolipoprotein C-II (apolipoprotein-glutamic acid), serum, and by heparin to which it also binds. The lipase is highly specific for the primary esters of acylglycerols and exhibits a slight stereospecificity for the sn-1 ester in preference to the sn-3-ester. Bovine milk also has separate activity toward 1-monoacylglycerols. Human milk contains a serum stimulated lipoprotein lipase with many of the characteristics of the enzyme in bovine milk, as well as an enzyme stimulated by bile salts which resembles the sterol ester hydrolase of rat pancreatic juice. The assay, function, purification, characteristics, and substrate specificities of these enzyme are discussed.