Amylin in Insulin Deficiency

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Insulin-deficient animals showed reduction or absence of amylin, whether insulin deficiency was invoked chemically with streptozotocin (Bretherton-Watt et al., 1989; Inman et al., 1990; Jamal et al., 1990; Mulder et al., 1995b, 1996c; Ogawa et al., 1990) or by autoimmune b-cell destruction, as with BB rats (Bretherton-Watt et al., 1991; Huang et al., 1991a,b). That is, loss of insulin secretion was associated with loss of amylin secretion. This indicates that any source of amylin that is outside of b-cells (for example, pancreatic d-cells or the gastric antrum) must contribute comparatively little to overall circulating concentrations, or else the disappearance of amylin and insulin following b-cell destruction would be dissimilar.

In human type 1 diabetes, pancreatic amylin content was low (Tasaka et al., 1995). Plasma amylin concentrations were described as low (e.g., 0.7 pM, Hartter et al., 1991; 1.6 pM, Manley and Hales, 1997) or undetectable (van Hulst et al., 1994), and nutrient-stimulated increments in plasma concentration were either low (Hanabusa et al., 1992) or unmeasurable (Koda et al., 1992). Absence of amylin secretion was similarly observed in children with type 1 diabetes (Akimoto et al., 1993) (Fig. 4).

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FIGURE 4 Changes in plasma concentration of insulin and amylin secretion following a 75 g oral glucose load in five non-diabetic subjects, five subjects with type 1 diabetes, and six subjects with impaired glucose tolerance. Symbols are means ± SEM. Data from Koda et al. (1992).

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