Aims/hypothesis Based on mouse study findings, pancreatic islet cells are supposed to lack basement membrane (BM) and interact directly with vascular endothelial BM. Until now, the BM composition of human islets has remained elusive. Methods Immunohistochemistry with specific monoclonal and polyclonal antibodies as well as electron microscopy were used to study BM organisation and composition in human adult islets. Isolated islet cells and function-blocking monoclonal antibodies and recombinant soluble Lutheran peptide were further used to study islet cell adhesion to laminin (Lm)-511. Short-term cultures of islets were used to study Lutheran and integrin distribution. Results Immunohistochemistry revealed a unique organisation for human Lm-511/521 as a peri-islet BM, which coinvaginated into islets with vessels, forming an outer endocrine BM of the intra-islet vascular channels, and was distinct from the vascular BM that additionally contained Lm-411/421. These findings were verified by electron microscopy. Lutheran glycoprotein, a receptor for the Lm α5 chain, was found prominently on endocrine cells, as identified by immunohistochemistry and RT-PCR,

Basement membranes (BMs) are an important part of the physiological microenvironment of pancreatic islet cells. In mouse islets, b-cells interact directly with BMs of capillary endothelial cells. We have shown that in the human islets, the capillaries are surrounded by a double BM both in foetal and adult tissues. The endocrine islet cells are facing a BM that is separate from the endothelia. Laminins are the functionally most important component of BMs. The only laminin isoform present in the human endocrine islet BM is laminin-511 (previously known as laminin 10). The islet cells facing this BM have a strong and polarized expression of Lutheran glycoprotein, which is a well-known receptor for the laminin a5 chain. Dispersed human islet cells adhere to purified human laminin-511 and the binding is equally effectively blocked by a soluble form of Lutheran as by antibody against integrin b1. Our results reveal unique features of the BM structure of human islets, different from rodents. This information has potentially important implications for the generation of an optimal microenvironment for b-cell function, proliferation and differentiation.

Turmeric (Curcuma longa) has been used in Indian cooking, and in herbal remedies. Its possible mechanism of action was examined in terms of antioxidant availability during actual cooking conditions and in therapeutic applications using standardized extracts. The assays involve different levels of antioxidant action such as oxygen radical absorbance capacity (ORAC), radical scavenging abilities using 1,1-diphenyl-2-picryl hydrazyl (DPPH), 2,2'-azobis-3-ethylbenzthiazoline-6-sulfonic acid (ABTS), ferric reducing antioxidant power (FRAP) and protection of membranes examined by inhibition of lipid peroxidation besides the content of phenols and total flavonoids. The aqueous and ethanol extracts of two major preparations of turmeric, corresponding to its use in cooking and medicine, showed significant antioxidant abilities. In conclusion, the studies reveal that the ability of turmeric to scavenge radicals, reduce iron complex and inhibit peroxidation may explain the possible mechanisms by which turmeric exhibits its beneficial effects in relation to its use in cooking and medicine.

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Pancreatic islet development is impaired in mice lacking EGFRs (epidermal growth factor receptors). Even partial tissue-specific attenuation of EGFR signalling in the islets leads to markedly reduced beta-cell proliferation and development of diabetes during the first weeks after birth. Out of the many EGFR ligands, betacellulin has been specifically associated with positive effects on beta-cell growth, through both increased proliferation and neogenesis. EGFR action is also necessary for the beta-cell mitogenic activity of the gut hormone GLP-1 (glucagon-like peptide 1). Finally, in vitro models demonstrate a central role for EGFR in transdifferentiation of pancreatic acinar and ductal cells into endocrine islet cells. EGFR thus plays an essential role in beta-cell mass regulation, but its mechanisms of action remain poorly understood.