Kinetensin and Fragments
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Introduction
Kinetensin, a nonapeptide originally isolated from pepsin-treated plasma, and its amino acids 1-8 fragments [des-Leu9] belongs to the neurotensin family of peptides and are known to stimulate the growth of human tumors. Its sequence is H-Ile-Ala-Arg-Arg-His-Pro-Tyr-Phe-Leu-OH and with molecular weight 1172.40, which is similar to neurotensin and angiotensin I. Kinetensin increases vascular permeability when injected intradermally into rats and releases histamine from rat mast cells in vitro. Kinetensin, neuromedin N, and xenopsin share a certain structural homology with the C-terminal end of neurotensin. neurotensin is an endogenous tridecapeptide that, in the central nervous system and gastrointestinal tract, fulfills a broad spectrum of biological functions, which includes the proliferation of normal and neoplastic cells through its interaction with a subtype-1 NT, a single G protein-coupled seven-transmembrane receptor (NTR1).
Mechanism of action
As previous literature reported, kinetensin exhibits a structure that similar to the C-terminal end of neurotensin that is important because the neurotensin C-terminal fragments are biologically active but unstable in circulation. For this reasons, kinetensin has been classified as neurotensin-family peptides that can bind with different affinities to the same receptors. Kinetensin was rapidly metabolized approximately 200-fold more than neurotensim in living organisms. Its metabolism mainly takes placed in the circulation which confirmed both in vivo and in vitro. Kinetensin also cleared in lung and gut. The converting of enzyme is inhibited and the lung clearance is abolished at the highest concentration in the lungs but it has no effect on the metabolism of actin in the intestinal tract or the general circulation. Arterial infusion of kinetensin could achieve high blood kinetensin levels at the pancreas while not increase plasma pancreatic polypeptide. Therefore, the lack of biological activity and together with the extremely rapid degradation of exogenous kinetensin, makes it unlikely that kinetensin plays a role as a circulating regulatory peptide.
Application of kinetensin and fragments
Compared to commonly used drugs for disease treatment, the peptide is less toxic and less side effects, which can be used for long term disease treatment. The peptide under physiological condition forms no toxic or noxious degradation product. In medicine, Kinetensin peptide having specific amino acid sequence was used for treating such as cancer, autoimmune diseases, fibrotic diseases, inflammatory diseases, neurodegenerative diseases, infectious diseases, and lung diseases.
References
- Read, D., Shulkes, A., Fletcher, D., & Hardy, K. (1993). Pharmacokinetics and biological activity of kinetensin in conscious sheep. Agents and actions, 38(1-2), 231-239.
- Podstawka‐Proniewicz, E., Kudelski, A., Kim, Y., & Proniewicz, L. M. (2012). Adsorption of neurotensin‐family peptides on SERS‐active Ag substrates. Journal of Raman Spectroscopy, 43(9), 1196-1203.
- Keegan, K. D., Woodruff, G. N., & Pinnock, R. D. (1994). The pharmacology of neurotensin analogues on neurones in the rat substantia nigra, pars compacta in vitro. European journal of pharmacology, 253(1-2), 131-137.
