Spexin Peptide

Modern bioinformatics search techniques identified a peptide in rat tissues known as spexin. The peptide is most pronounced in rodents as it helps in weight loss for such rodents with diet-induced obesity. In human beings, the peptide forms as a result of a gene known as Ch12orf39. In mature form sexing contains 14 strands of amino acids. There is no evidence of the expression spexin protein or mRNA in human tissue as it is expressed in most rodents. The functions of spexin in the human body are less known. NWTPQAMLYLKGAQ-amide, a synthetic amidated peptide, has shown the ability to induce contraction of muscles in the evaluation of how stomach explants contract.

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Spexin lower the level of adrenocortical cell production and at times induce a rise in the secretion of glucocorticoid and aldosterone among other functions in rodents. This paper will identify cells or tissues that express the presence of spexin in humans. This identification can help evaluate the physiological function of spexin, more specifically in T2DM. This kind of diabetes is responsible for altering the metabolism of lipids and glucose which result from high food consumption and an inactive lifestyle. Studies have shown the effectiveness of spexin in weight loss reduction. The peptide gene is especially utilised in obese human fat. Spexin is thus, suggested to help in the metabolism of both lipds and glucose homeostasis in type 2 diabetes mellitus. The study focused on examining the presence of spexin in tissues and their circulation after glucose injection in patients with type 2 diabetes mellitus.

The study revealed the presence of spexin gene in most endocrine tissues under consideration. The genes were highly expressed in the adrenal gland than in the skeletal muscles. The gene was especially high in visceral fat, pancreas, and thyroid. Spexin was found to be primarily located in the cytoplasm of the tissues under consideration. Follicular epithelial cells of other tissues like the thyroid expressed a heterogeneous staining. The research also revealed that cytoplasmic staining was present in some follicles and totally lacked in others. Immunostaining was, however, highly expressed in the medullary and adrenal cortex cells. Other cells like the islets of Langerhans indicated spexin immunoreactivity at high levels while others like visceral fats like indicated moderate immunoreactivity of spexin.

Some organs in the human body such as the liver, small intestines, stomach, skin, lungs, kidney and colon indicated a high presence of spexin gene than the skeletal muscles. Most of these organs also showed cytoplasmic immunohistochemical localization of spexin in their glands and epithelia. Nevertheless, other connective tissue structures like the submucosal layer and lamina propia gave negative results on staining while layers of muscles indicated moderate or weak immunostaining. In the small intestines, epithelial cells indicated high cytoplasmic staining than crypt cells. Epithelial cells found in the colon, however, showed temperate immunostaining while the goblet cells had no staining. In general, it can be seen that spexin is more expressed in epithelial cells than in connective cells and human muscles.

According to this research, there is intense immunoreactivity of spexin in the epithelial cells of skin, respiratory conducting airwaves and the entire digestive system. This high expression suggests the involvement of spexin in the transepithelial transfer. The same can also be related to epithelial cell renewal regulation rate. Spexin has also been seen to control the rate of differentiation, proliferation and death of cells in both glandular and surface epithelial. The study has furthermore; found that spexin regulates proliferation of adrenocortical. It can thus, be deduced that the peptide is a novel hormone that is aids in weight regulation, favoring its proposed use in obesity therapy. Spexin is notably majorly found in the islets of the pancreas of a healthy person and is a natural ligand for galanin. Galanin and type 2 diabetes mellitus have a positive relationship as it lowers insulin resistance by raising the levels of GLUT4 and enhancing its transportation. Test results have shown that spexin levels are low in type 2 DM in relation to the lean controls. An OGTT time scale, on the other, showed negative results for a spexin-glucose relationship. The notable relationships between serum spexin, glucose and peptides indicate that the peptide can be vital in the metabolism of T2DM.

This study does not show correlations with different cardiometabolic risk factors like leptin. Spexin rates inversely relate to the growth rate of insulin in patients with T2DM. The study strength included large samples and ethnic homogeneity of participants. The studys short comings, on the other, hand include lack of longitudinal data and its cross-sectional nature. The study did not verify whether spexin levels were influenced by pubertal status, fat distribution, obesity duration or patterns of physical activity. The study, however, does not give pathophysiological or physiological importance of spexin peptides in the metabolism of lipids and glucose. From the study, we can learn that spexin relates inversely with glucose in T2DM. the peptide also has importance in the activity of various cells and tissues. Spexine regulates the rate of differentiation, proliferation and death of cells in glandular and surface epithelial. We also learn that spexin can regulate weight loss in obese patients giving it chances for use in obesity therapy.

Bibliographies

Gu, Liping, , Mingyu G., Ying Zhang, Shuai Yan, Yufan Wang, Xiaoying Ding, Na Li, Jiajing Yin, Nengguang Fan, Yongde Peng and Yuhang Ma. "Spexin Peptide Is Expressed in Human Endocrine and Epithelial Tissues and Reduced after Glucose Load in Type 2 Diabetes." Peptides 71 (2015): 232-39.

Guo, Lili, Mingyi Shi, Guangzhi Li, Lingxiang Zhang, Hu Shao, Ling Zhang, Penghua Fang, Yingping Ma, Qiaojia Shi, Jian Li, and Yumei Sui. "Galanin Antagonist Increases Insulin Resistance by Reducing Glucose Transporter 4 Effect in Adipocytes of Rats." General and Comparative Endocrinology 173, no. 1 (2011): 159-63.

Gu, Liping, Yuhang Ma, , Shuai Yan, Na Li, Yufan Wang, Xiaoying Ding, Mingyu Gu, Jiajing Yin, Nengguang Fan, Yongde Peng and Ying Zhang. "Spexin Peptide Is Expressed in Human Endocrine and Epithelial Tissues and Reduced after Glucose Load in Type 2 Diabetes." Peptides 71 (2015): 232-39.

Mirabeau, O., E. Perlas, C. Severini, E. Audero, O. Gascuel, R. Possenti, E. Birney, N. Rosenthal, and C. Gross. "Identification of Novel Peptide Hormones in the Human Proteome by Hidden Markov Model Screening." Genome Research 17, no. 3 (2007): 320-27.

Porzionato, A., M. Rucinski, V. Macchi, C. Stecco, L. K. Malendowicz, and R. De Caro. "Spexin Expression in Normal Rat Tissues." Journal of Histochemistry & Cytochemistry 58, no. 9 (2010): 825-37.

Walewski, Jose L., Fengxia Ge, Harrison Lobdell, Nancy Levin, Gary J. Schwartz, Joseph R. Vasselli, Afons Pomp, Gregory Dakin, and Paul D. Berk. "Spexin Is a Novel Human Peptide That Reduces Adipocyte Uptake of Long Chain Fatty Acids and Causes Weight Loss in Rodents with Diet-induced Obesity." Obesity 22, no. 7 (2014): 1643-652.

Wong, M. Sze, T. Chen, C. Cho, H. Law, I. K. Chu, & Wong, A. "Goldfish Spexin: Solution Structure and Novel Function as a Satiety Factor in Feeding Control." AJP: Endocrinology and Metabolism 305, no. 3 (2013)..