Regulation Of Amylase Secretion Research Articles

Regulation and Characterization of Amylase Enzyme Secretion In the Digestive Tract of <i>Antheraea Assamensis</i> Helfer

Antheraea assamensis Helfer is an endemic non-mulberry lepidopteran species of North East India with high commercial demand for its golden hued silk. Antheraea assamensis suffers from a protozoan disease pebrine which lead to death of the silkworm. In this study, the effect of various factors (starvation, feeding, temperature, pH, Ca ion and larval stage) in the regulation of amylase secretion is compared in healthy and diseased muga silkworm. Moreover, enzyme zymography and purification of amylase from the midgut is also performed. Result shows that, the secretion of amylase in Antheraea assamensis in starved condition, significantly decreases. Refeeding experiments (after 2 days of starvation) suggest that amylase secretion sharply increases due to feeding stimulus. The purified enzyme molecular weight is confirmed as 56 kDa by SDS PAGE. The purification fold of purified enzyme is 34 times higher than the crude enzyme extract.

The islet-acinar axis of the pancreas: more than just insulin

Although the role of the islets in the regulation of acinar cell function seemed a mystery to investigators who observed their dispersion among pancreatic acini, over time an appreciation for this intricate and unique structural arrangement has developed. The last three decades have witnessed a steadily growing understanding of the interrelationship of the endocrine and the exocrine pancreas. The islet innervation and vascular anatomy have been more fully characterized and provide an appropriate background for our current understanding. The interrelationship between the endocrine and exocrine pancreas is mediated by islet-derived hormones such as insulin and somatostatin, other humoral factors including pancreastatin and ghrelin, and also neurotransmitters (nitric oxide, peptide YY, substance P, and galanin) released by the nerves innervating the pancreas. Although considerable progress has been achieved, further work is required to fully delineate the complex interplay of the numerous mechanisms involved. This review aims to provide a comprehensive update of the current literature available, bringing together data gleaned from studies addressing the actions of individual hormones, humoral factors, and neurotransmitters on the regulation of amylase secretion from the acinar cell. This comprehensive view of the islet-acinar axis of the pancreas while acknowledging the dominant role played by insulin and somatostatin on exocrine secretion sheds light on the influence of the various neuropeptides on amylase secretion.

Rap1 Activation Plays a Regulatory Role in Pancreatic Amylase Secretion

Rap1 is a member of the Ras superfamily of small GTP-binding proteins and is localized on pancreatic zymogen granules. The current study was designed to determine whether GTP-Rap1 is involved in the regulation of amylase secretion. Rap1A/B and the two Rap1 guanine nucleotide exchange factors, Epac1 and CalDAG-GEF III, were identified in mouse pancreatic acini. A fraction of both Rap1 and Epac1 colocalized with amylase in zymogen granules, but only Rap1 was integral to the zymogen granule membranes. Stimulation with cholecystokinin (CCK), carbachol, and vasoactive intestinal peptide all induced Rap1 activation, as did calcium ionophore A23187, phorbol ester, forskolin, 8-bromo-cyclic AMP, and the Epac-specific cAMP analog 8-pCPT-2'-O-Me-cAMP. The phospholipase C inhibitor U-73122 abolished carbachol- but not forskolin-induced Rap1 activation. Co-stimulation with carbachol and 8-pCPT-2'-O-Me-cAMP led to an additive effect on Rap1 activation, whereas a synergistic effect was seen on amylase release. Although the protein kinase A inhibitor H-89 abolished forskolin-stimulated CREB phosphorylation, it did not modify forskolin-induced GTP-Rap1 levels, excluding PKA participation. Overexpression of Rap1 GTPase-activating protein, which blocked Rap1 activation, reduced the effect of 8-bromo-cyclic AMP, 8-pCPT-2'-O-Me-cAMP, and vasoactive intestinal peptide on amylase release by 60% and reduced CCK- as well as carbachol-stimulated pancreatic amylase release by 40%. These findings indicate that GTP-Rap1 is required for pancreatic amylase release. Rap1 activation not only mediates the cAMP-evoked response via Epac1 but is also involved in CCK- and carbachol-induced amylase release, with their action most likely mediated by CalDAG-GEF III.

Origin and mediation of secretion induced by oral phytohaemagglutinin (PHA) in rats

After oral administration several gut-binding lectins induce accumulation of liquor and amylase in the proximal small intestine. Orally administered Phaseolus vulgaris phytohaemagglutinin (PHA) was used to study the mediation of these effects in rats. The regulation of amylase secretion clearly differed from that of the liquor. The amylase activity was of pancreatic origin, in agreement with the known cholecystokinin-releasing effect of PHA. It appears that CCK exerts its effect both directly and by facilitating neural stimulatory pathways. Intestinal secretion was identified as the source of the liquor, without a contribution by other secretions. It was mediated by a local cholinergic reflex with the involvement of both muscarinic and nicotinic acetylcholine receptors. It is speculated that the observed enteric reflex may enable the gut to transport secreted antibacterial peptides or secretory antibodies from the crypts to adherent bacteria on adjacent villi.

Lack of nitric oxide-mediated regulation of amylase secretion stimulated by VIP in parotid glands of NOD mice

The non-obese diabetic (NOD) mouse is chosen among other experimental models to study autoimmune sialadenitis resembling Sjögren's syndrome (SS), because of its unique characteristic of developing salivary dysfunction. Based on the deep loss of nitric oxide synthase (NOS) activity in parotid glands of NOD mice observed from early stages of disease and the inhibitory effect of nitric oxide (NO) donors on amylase secretion in normal salivary glands, our goal was to investigate whether parotid glands from NOD mice lacking NOS activity presented this regulatory mechanism of amylase secretion. We found that parotid glands from NOD mice lack nitric oxide-mediated regulation of amylase secretion in response to VIP stimulation. The lack of regulation might be assigned to the loss of NOS activity as derived from the results with NOS inhibitors and increasing concentrations of VIP. These functional differences observed in NOD vs. BALB/c parotid glands occur in the absence of immune infiltrates in exocrine tissue, and it is not related to cAMP accumulation. NO-mediated regulation of amylase secretion was not observed in BALB/c submandibular glands to the same extent as described in parotid glands and was absent in submandibular glands of NOD mice.

Understanding salivary fluid and protein secretion.

Understanding salivary fluid and protein secretion.

Dispersed rat parotid cells: role of calcium and cAMP in the regulation of amylase secretion.

The inter-relationship between cellular calcium and cAMP in the regulation of amylase secretion in dispersed rat parotid cells was evaluated. α- adrenergic stimulation augmented β-adrenergic receptor-mediated amylase release. Cellular calcium depletion was unable to completely block amylase secretion.

Effect of Serotonin, Glucagon and Other Hormones on Amylase Secretion from Rabbit Parotid Gland

It was reported that in the sympathetic nervous system, catecholamines, played an important role in regulation of amylase secretion and that the β-receptors were involved in this mechanism (1–3). The possibility that amylase secretion mediated by β-receptors is intermediated by cyclic AMP has been indicated by Babad et al. (4) and other reports (5). The present experiments were undertaken to clarify the effects of various hormones which stimulate adenyl cyclase activity on amylase secretion in some tissues from rabbit parotid glands.