ORGANIC CATION TRANSPORTERS OF THE SLC22 FAMILY. MOLECULAR DIVERSITY, STRUCTURE, FUNCTION, PARTNERSHIP IN THE FUNCTIONING OF THE INTERORGAN COMMUNICATION SYSTEM OF ANIMALS (A REWIEW)

<p align="left">Organic cation/zwitterions transporters (OCT-OCTN) of the SLC22 family share many structural characteristics with other MFS proteins and have received a great deal of attention because of their role in the handling of common drugs, toxins, and endogenic substances(neu...

Full description

Bibliographic Details
Main Author: Lev Smirnov
Format: Article
Language:English
Published: Karelian Research Centre of the Russian Academy of Sciences 2018-12-01
Series:Transactions of the Karelian Research Centre of the Russian Academy of Sciences
Subjects:
Online Access:http://journals.krc.karelia.ru/index.php/biology/article/view/866
id doaj-709987fd3cab4086937707bdca6b7f04
record_format Article
spelling doaj-709987fd3cab4086937707bdca6b7f042020-11-25T02:48:49ZengKarelian Research Centre of the Russian Academy of SciencesTransactions of the Karelian Research Centre of the Russian Academy of Sciences1997-32172312-45042018-12-011210.17076/eb866662ORGANIC CATION TRANSPORTERS OF THE SLC22 FAMILY. MOLECULAR DIVERSITY, STRUCTURE, FUNCTION, PARTNERSHIP IN THE FUNCTIONING OF THE INTERORGAN COMMUNICATION SYSTEM OF ANIMALS (A REWIEW)Lev Smirnov0Institute of Biology, Karelian Research Centre, Russian Academy of Sciences<p align="left">Organic cation/zwitterions transporters (OCT-OCTN) of the SLC22 family share many structural characteristics with other MFS proteins and have received a great deal of attention because of their role in the handling of common drugs, toxins, and endogenic substances(neurotransmitters, polyamines). OCTs are expressing in many tissues, including kidney, liver, olfactory mucosa, brain, retina, and placenta. At present, 3 OCTs and 3 OCTNs are known. OCTs may be a part of the evolutionary conservative system that protects higher organisms against potentially toxic compounds in the environment. The polypeptide chain consists of 543–557 amino acid residues. The secondary structure of the molecule is characterized by 12 transmembrane helices and intracellular localization of N- and C-termini of the molecule. The large extracellular loop (110 amino acid residues) between helices 1 and 2 contains 3 sites for N-linked glycosylation and 6 conservative cysteine residues. The second large intracellular loop located between helices 6 and 7 contains consensus sites for protein kinase A, C, G and casein kinase 2. The specific sequence [-Ser/Thr]-Ile-Val-Thr-Glu-[Phe/Trp]-[Asp/Asn]-Leu-Val-Cys- before helix 2 is unique for the SLC family. OCT1 and OCT2 have 70 % similarity in the amino acid composition, and 50 % similarity to OCT3. According to the “Remote Sensing and Signaling Hypothesis”, OCTs (especially OCTNs) may function in remote interorgan communication by regulating the levels of signaling molecules and key metabolites between organs and organ-body fluids.</p>http://journals.krc.karelia.ru/index.php/biology/article/view/866остoctnorganic cation transporterssubstrate specificityremote sensing and communication.
collection DOAJ
language English
format Article
sources DOAJ
author Lev Smirnov
spellingShingle Lev Smirnov
ORGANIC CATION TRANSPORTERS OF THE SLC22 FAMILY. MOLECULAR DIVERSITY, STRUCTURE, FUNCTION, PARTNERSHIP IN THE FUNCTIONING OF THE INTERORGAN COMMUNICATION SYSTEM OF ANIMALS (A REWIEW)
Transactions of the Karelian Research Centre of the Russian Academy of Sciences
ост
octn
organic cation transporters
substrate specificity
remote sensing and communication.
author_facet Lev Smirnov
author_sort Lev Smirnov
title ORGANIC CATION TRANSPORTERS OF THE SLC22 FAMILY. MOLECULAR DIVERSITY, STRUCTURE, FUNCTION, PARTNERSHIP IN THE FUNCTIONING OF THE INTERORGAN COMMUNICATION SYSTEM OF ANIMALS (A REWIEW)
title_short ORGANIC CATION TRANSPORTERS OF THE SLC22 FAMILY. MOLECULAR DIVERSITY, STRUCTURE, FUNCTION, PARTNERSHIP IN THE FUNCTIONING OF THE INTERORGAN COMMUNICATION SYSTEM OF ANIMALS (A REWIEW)
title_full ORGANIC CATION TRANSPORTERS OF THE SLC22 FAMILY. MOLECULAR DIVERSITY, STRUCTURE, FUNCTION, PARTNERSHIP IN THE FUNCTIONING OF THE INTERORGAN COMMUNICATION SYSTEM OF ANIMALS (A REWIEW)
title_fullStr ORGANIC CATION TRANSPORTERS OF THE SLC22 FAMILY. MOLECULAR DIVERSITY, STRUCTURE, FUNCTION, PARTNERSHIP IN THE FUNCTIONING OF THE INTERORGAN COMMUNICATION SYSTEM OF ANIMALS (A REWIEW)
title_full_unstemmed ORGANIC CATION TRANSPORTERS OF THE SLC22 FAMILY. MOLECULAR DIVERSITY, STRUCTURE, FUNCTION, PARTNERSHIP IN THE FUNCTIONING OF THE INTERORGAN COMMUNICATION SYSTEM OF ANIMALS (A REWIEW)
title_sort organic cation transporters of the slc22 family. molecular diversity, structure, function, partnership in the functioning of the interorgan communication system of animals (a rewiew)
publisher Karelian Research Centre of the Russian Academy of Sciences
series Transactions of the Karelian Research Centre of the Russian Academy of Sciences
issn 1997-3217
2312-4504
publishDate 2018-12-01
description <p align="left">Organic cation/zwitterions transporters (OCT-OCTN) of the SLC22 family share many structural characteristics with other MFS proteins and have received a great deal of attention because of their role in the handling of common drugs, toxins, and endogenic substances(neurotransmitters, polyamines). OCTs are expressing in many tissues, including kidney, liver, olfactory mucosa, brain, retina, and placenta. At present, 3 OCTs and 3 OCTNs are known. OCTs may be a part of the evolutionary conservative system that protects higher organisms against potentially toxic compounds in the environment. The polypeptide chain consists of 543–557 amino acid residues. The secondary structure of the molecule is characterized by 12 transmembrane helices and intracellular localization of N- and C-termini of the molecule. The large extracellular loop (110 amino acid residues) between helices 1 and 2 contains 3 sites for N-linked glycosylation and 6 conservative cysteine residues. The second large intracellular loop located between helices 6 and 7 contains consensus sites for protein kinase A, C, G and casein kinase 2. The specific sequence [-Ser/Thr]-Ile-Val-Thr-Glu-[Phe/Trp]-[Asp/Asn]-Leu-Val-Cys- before helix 2 is unique for the SLC family. OCT1 and OCT2 have 70 % similarity in the amino acid composition, and 50 % similarity to OCT3. According to the “Remote Sensing and Signaling Hypothesis”, OCTs (especially OCTNs) may function in remote interorgan communication by regulating the levels of signaling molecules and key metabolites between organs and organ-body fluids.</p>
topic ост
octn
organic cation transporters
substrate specificity
remote sensing and communication.
url http://journals.krc.karelia.ru/index.php/biology/article/view/866
work_keys_str_mv AT levsmirnov organiccationtransportersoftheslc22familymoleculardiversitystructurefunctionpartnershipinthefunctioningoftheinterorgancommunicationsystemofanimalsarewiew
_version_ 1724746484877885440