Showing posts with label NPY Y2 antibody. Show all posts
Showing posts with label NPY Y2 antibody. Show all posts

Wednesday, October 03, 2012

Neuropeptide Ys-Regulate Food Intake & Body Weight

Role of salivary PYY in the modulation of food intake.

This is a study that comprehensively shows the expression of Neuropeptide Ys  (PYY 3–36 ) are present in saliva and showed the expression of its preferred receptor, Y2R, in the basal layer of the progenitor cells of the tongue epithelia and von Ebner's gland. The researchers used our Y2R antibody (dilution 1:3000) to determine level of expression. This receptor appears to be the main player in mediating hunger and body weight: Hurtado MD, Acosta A, Riveros PP, Baum BJ, Ukhanov K, et al. (2012) Distribution of Y-Receptors in Murine Lingual Epithelia. PLoS ONE 7(9): e46358. doi:10.1371/journal.pone.0046358.


Images: Immunolocalization of Y1, Y2, Y4, and Y5 receptors (Rs) in the dorsal epithelium of murine tongue. Images: Mirror section pairs (Panels A and B, C and D, E and F) were hybridized to the respective YR antibody (green), followed by DAPI counterstain (blue), as indicated in the upper left corner of each panel. For better viewing, the confocal images in B, D, and F were reflected horizontally. Representative areas of the epithelium, positive for either YR (dashed rectangles in the left-sided panels), are shown as close-up images on the right next to each respective panel. The irregular columned structures at the epithelial surface are transversely sectioned filiform papillae. G - Y4R-positive neuronal fibers (green) are located in the subepithelial region underlying the basal laminae. H – co-localization of Y4R and NCAM (red) immunoreactivity within mechanoreceptors of Meissner corpuscles (MC). As a morpho-histological reference of the dorsal lingual epithelium structure, an hematoxylin and eosin stained section is shown in panel I. Panel J shows a hypothetical diagram of a lingual dorsal epithelium layer and the differentiation/migration lineage of cell types expressing respective YR subtypes. K5 – cytokeratin-5 [2]. doi:10.1371/journal.pone.0046358.g006.

Note: this study is further validation of the potency of our NPY Y2 antibody.

Conclusion: NPY family peptides and their cognate receptors in the oral cavity may mediate a wide variety of functions, including proliferation, differentiation, motility, taste perception, as well as satiation. All of these multiple functions and their respective molecular mechanisms are subjects of the ongoing investigations.

Understanding these molecular mechanisms could provide the foundation for discovering less intrusive therapies for obesity. I will keep you posted.

Friday, June 17, 2011

Chronic Type II Diabetes Mellitus and Cardiovascular Disease

Our Neuropeptide and Neuropeptide Receptors and Leptin and Leptin Receptor Antibdodies are frequently used to study pathologies and biology specific to Obesity and Diabetes.

Here's a new publication studying the relationship between diabetic neuropathy and altered neuropeptide Y and its receptor expression levels in myocardium and plasma.

Robina Matyal, Feroze Mahmood, Michael Robich, Hiliary Glazera, Kamal Khabbaza, Philip Hessa, Cesario Bianchia, Robert Hagberga, Shu-Xu Hua, and Frank W. Sellkea. Chronic type II diabetes mellitus leads to changes in neuropeptide Y receptor expression and distribution in human myocardial tissue. European Journal of Pharmacology. Volume 665, Issues 1-3, 31 August 2011, Pages 19-28.

Abstract: Neuropeptide Y is one of the most abundant neurotransmitters in the myocardium, and is known to influence cardiovascular remodeling. We hypothesized that diabetic neuropathy could possibly be associated with altered neuropeptide Y and its receptor expression levels in myocardium and plasma. Plasma neuropeptide Y levels in diabetic (n = 24, HgbA1c 7.9 ± 1.1%) and non-diabetic (n = 27, HgbA1c 5.8 ± 0.5%) patients undergoing cardiac surgery utilizing cardiopulmonary bypass were analyzed. Right atrial tissue of these patients was used to determine the expression of neuropeptide Y, the receptors 1–5, and leptin by immunoblotting, real-time PCR and immunofluorescence. Apoptosis signaling and endostatin and angiostatin were measured to determine the effects of leptin.


Plasma neuropeptide Y levels were significantly increased in patients with Type II diabetes mellitus as compared to non-diabetic patients (P = 0.026). Atrial tissue neuropeptide Y mRNA levels were lower in diabetic patients (P = 0.036). There was a significant up-regulation of myocardial Y2 and Y5 receptors (P = 0.009, P = 0.01 respectively) in the diabetic patients. Leptin, involved with apoptosis and angiogenesis, was down regulated in diabetic patients (P = 0.05). The levels of caspase-3, endostatin and angiostatin were significantly elevated in diabetic patients (P = 0.003, P = 0.008, P = 0.01 respectively). Y1 receptors were more likely to be localized within the nuclei of cardiomyocytes and vascular smooth muscle cells.


Neuropeptide expression is altered differentially in the serum and myocardium by diabetes. Altered regulation of this system in diabetics may be in part responsible for the decreased angiogenesis, increased apoptosis, and increased vascular smooth muscle proliferation leading to coronary artery disease and heart failure in this patient population.