Beta cell

Beta cell
The photo above shows a mouse pancreatic islet as seen by light microscopy. Beta cells can be recognised by the green insulin staining. Glucagon is labelled in red and the nuclei in blue.
A porcine islet of Langerhans. The left image is a brightfield image created using hematoxylin stain; nuclei are dark circles and the acinar pancreatic tissue is darker than the islet tissue. The right image is the same section stained by immunofluorescence against insulin, indicating beta cells.
Latin endocrinocytus B; insulinocytus
Code TH H3.04.02.0.00026

Beta cells (beta-cells, β-cells) are a type of cell in the pancreas located in the so-called islets of Langerhans. They make up 65-80% of the cells in the islets.

Contents

Function

Beta cells store and release insulin, a hormone that controls the level of glucose in the blood. The liver maintains the base-line glucose level, but the beta cells can respond quickly to spikes in blood glucose by releasing stored insulin while simultaneously producing more. The response time is fairly quick, taking approximately 10 minutes.

Apart from insulin, beta cells release C-peptide, a byproduct of insulin production, into the bloodstream in equimolar quantities. C-peptide helps to prevent neuropathy and other symptoms of diabetes related to vascular deterioration.[1] Measuring the levels of C-peptide can give a practitioner an idea of the viable beta cell mass.[2]

Beta-cells also produce amylin,[3] also known as IAPP, islet amyloid polypeptide. Amylin functions as part of the endocrine pancreas and contributes to glycemic control. Amylin's metabolic function is now somewhat well characterized as an inhibitor of the appearance of nutrient [especially glucose] in the plasma. Thus, it functions as a synergistic partner to insulin. Whereas insulin regulates long-term food intake, increased amylin decreases food intake in the short term.

Pathology

Diabetes can experimentally be induced in beta cells for research purposes by streptozotocin or alloxan, which are specifically toxic to beta cells.

See also

References

  1. ^ Ido Y, Vindigni A, Chang K, Stramm L, Chance R, Heath WF et al. (1997). "Prevention of vascular and neural dysfunction in diabetic rats by C-peptide". Science 277 (5325): 563–6. doi:10.1126/science.277.5325.563. PMID 9228006. 
  2. ^ Hoogwerf B, Goetz F (1983). "Urinary C-peptide: a simple measure of integrated insulin production with emphasis on the effects of body size, diet, and corticosteroids". J Clin Endocrinol Metab 56 (1): 60–7. doi:10.1210/jcem-56-1-60. PMID 6336620. 
  3. ^ Moore C, Cooper G (1991). "Co-secretion of amylin and insulin from cultured islet beta-cells: modulation by nutrient secretagogues, islet hormones and hypoglycemic agents". Biochem Biophys Res Commun 179 (1): 1–9. doi:10.1016/0006-291X(91)91325-7. PMID 1679326. 
  4. ^ "U.K. prospective diabetes study 16. Overview of 6 years' therapy of type II diabetes: a progressive disease. U.K. Prospective Diabetes Study Group". Diabetes 44 (11): 1249–58. 1995. doi:10.2337/diabetes.44.11.1249. PMID 7589820. 
  5. ^ Rudenski A, Matthews D, Levy J, Turner R (1991). "Understanding "insulin resistance": both glucose resistance and insulin resistance are required to model human diabetes". Metabolism 40 (9): 908–17. doi:10.1016/0026-0495(91)90065-5. PMID 1895955. 

External links