1946 syntynyt Tampereella
Ylioppilastutkinto 1964 Lempäälä
Lääketietaan kandidaatti 1966 Turun yliopisto
Lääketieteen lisensiaatti 1972 Turun Yliopisto
Dietetiikan opiskelu 1998 - 2001 Göteborgin Yliopisto
Eläkkeelle 2010
This gene belongs to a family of genes that
function as receptors for tachykinins. Receptor affinities are
specified by variations in the 5'-end of the sequence. The receptors
belonging to this family are characterized by interactions with G
proteins and 7 hydrophobic transmembrane regions. This gene encodes the
receptor for the tachykinin neuropeptide substance K, also referred to as neurokinin A. [provided by RefSeq, Jul 2008]
GeneCards Summary for TACR2 Gene
TACR2 (Tachykinin Receptor 2) is a Protein Coding gene.
Diseases associated with TACR2 include Baritosis and Constipation.
Among its related pathways are RET signaling and Signaling by GPCR.
Gene Ontology (GO) annotations related to this gene include G protein-coupled receptor activity and substance K receptor activity.
An important paralog of this gene is TACR3.
UniProtKB/Swiss-Prot Summary for TACR2 Gene
This is a receptor for the tachykinin
neuropeptide substance K (neurokinin A). It is associated with G
proteins that activate a phosphatidylinositol-calcium second messenger
system. The rank order of affinity of this receptor to tachykinins is:
substance K > neuromedin-K > substance P.
The neurokinin 2 (NK2) receptor is a member of the tachykinin
family of G-protein-coupled receptors which also includes NK1 and NK3
receptors. The NK2 receptor is predominantly expressed in the periphery
(including inflammatory cells and bronchial smooth muscle).
Tachykinin Receptor 1 (Substance P Receptor; Neurokinin-1 Receptor)3
Entrez Gene Summary for TACR1 Gene
This gene belongs to a gene family of tachykinin receptors. These tachykinin
receptors are characterized by interactions with G proteins and contain
seven hydrophobic transmembrane regions. This gene encodes the receptor
for the tachykinin
substance P, also referred to as neurokinin 1. The encoded protein is
also involved in the mediation of phosphatidylinositol metabolism of
substance P. [provided by RefSeq, Sep 2008]
GeneCards Summary for TACR1 Gene
TACR1 (Tachykinin Receptor 1) is a Protein Coding gene.
Diseases associated with TACR1 include Cystitis and Causalgia.
Among its related pathways are RET signaling and Signaling by GPCR.
Gene Ontology (GO) annotations related to this gene include G protein-coupled receptor activity and substance P receptor activity.
An important paralog of this gene is TACR3.
UniProtKB/Swiss-Prot Summary for TACR1 Gene
This is a receptor for the tachykinin
neuropeptide substance P. It is probably associated with G proteins
that activate a phosphatidylinositol-calcium second messenger system.
The rank order of affinity of this receptor to tachykinins is: substance
P > substance K > neuromedin-K.
The neurokinin 1 (NK1) receptor is a member of the tachykinin
family of G-protein-coupled receptors which also includes NK2 and NK3
receptors. The NK1 receptor is localized in high concentrations in the
CNS (particularly the striatum and amygdala) and peripheral tissues.
Kerään tähän arikkeleita ,joita pitää harkiten lukea.
Aivojen plasmalipeideissä on pieni osa fosfatidyylilipidejä, lipositoleja, ja niillä on oma tärkeä modulinsa varsinkin harmaissa hermosoluissa. Niillä on erittäin funktionaalinen modulinsa (, josta tässä fytiiniblogissa olen käsitellyt eri molekyylejä vuosien varrella. Covidin jälkeen on havaittu fosfolipidikirjossa epätasapainoa ja korostuneeksi näyttää jäävän tästä lipositolimodulipuolesta lyso-muotoa, lysofosfolipidiä lysofosfatidyyli-inositolia. Asian taustalla piilee sars-2 viruksen raju soluaineenvaihdunnan manipulointi, joka jättää siten jälkeensä tälle inositolia sisältävälle järjestelmälle mahdollisuuden paisua. Tämä heijastuu kyllä psyykiseen toimitnaan lähinnä mielialaan monivivahteisesti, josmistä pitää saada ajan mitaan tarpeeksi käsitystä . Muuten ei pääse jyvälle siitä, millä tavalla voi johtaa metaboliaa korjaantumiskynnyksen paremmalle puolelle. Itsestään korjaantuvuus kudoksissa ihmisellä on hyvä, muta on jokin kynnys joka pitää ylittää, että päästään sellaisen normaliteetin puolelle. Kyse ei ole vain aivojen inositolimodulista, vaan myös kohdista josa tätä modulia käytetään. Yksi on sokeriaineenvaihdunta. Ilmeisesti vaaraa on keuhkofibroosista ja non-alkoholisesta maksanrasvoittumisestakin jos tämä ei oikene. Viruksen yksi tapa moduloida energia-aineita näyttää olleen ATP, CTP, TTP ja TTP peräisten energioiden purkaminen, fosfaattien irrottaminen ja samalla GTP-peräisen energian suosiminen. En tiedä jos tässä olen asiasta jyvällä. Tällöin on paljon tarjolla esim AMP ja CMP- muotoa, joita oinositoliaineenvaihdunta käyttää. aivojen puolella lysofosfatidylinositoli muodostaa protektiivisuutta erään artikkelin mukaanJos ATP ja CTP ovat purkaantuneita , fosfatidyyli-inositoli ei pysty nousemaan energiarikakisiin muotoihinsa.
Fondevila MF, Fernandez U,
Gonzalez-Rellan MJ, Da Silva Lima N, Buque X, Gonzalez-Rodriguez A,
Alonso C, Iruarrizaga-Lejarreta M, Delgado TC, Varela-Rey M, Senra A,
Garcia-Outeiral V, Novoa E, Iglesias C, Porteiro B, Beiroa D, Folgueira
C, Tojo M, Torres JL, Hernández-Cosido L, Blanco Ó, Arab JP, Barrera F,
Guallar D, Fidalgo M, López M, Dieguez C, Marcos M, Martinez-Chantar ML,
Arrese M, Garcia-Monzon C, Mato JM, Aspichueta P, Nogueiras R.Hepatology. 2021 Feb;73(2):606-624. doi: 10.1002/hep.31290. Epub 2020 Nov 13.PMID: 32329085Free PMC article.
BACKGROUND AND AIMS: G protein-coupled receptor (GPR) 55 is a putative cannabinoid receptor, and l-alpha-lysophosphatidylinositol (LPI) is its only known endogenous ligand. ...
Irving A, Abdulrazzaq G, Chan SLF, Penman J, Harvey J, Alexander SPH.Adv Pharmacol. 2017;80:223-247. doi: 10.1016/bs.apha.2017.04.004. Epub 2017 Jun 12.PMID: 28826536Review.
GPR18, GPR55, and GPR119 exhibit limited sequence homology with the established CB(1) and CB(2) cannabinoid receptors. However, the pharmacology of these orphan receptors displays overlap with CB(1) and CB(2) receptors, particularly for GPR18 and GPR55. ...Th …
Nevalainen T, Irving AJ.Curr Top Med Chem. 2010;10(8):799-813. doi: 10.2174/156802610791164229.PMID: 20370712Review.
However, to date, the most potent ligand identified for GPR55 is the endogenous phospholipid, lysophosphatidylinositol
(LPI). GPR55 is thought to link predominantly G-protein alpha(13),
where it promotes Rho-dependent signalling. ...This article reviews the
current status …
Lysophosphatidylinositol (LysoPI), an endogenous ligand for G protein-coupled receptor
(GPR) 55, has been known to show various functions in several tissues
and cells; however, its roles in the central nervous system (CNS) are
not well known. ...
Several crystal structures of LPA receptors and
ATX have been solved, which will accelerate development of highly
selective and effective LPA signaling targeting compounds. We also
review additional bioactive lysophospholipid (LPL) signaling molecules
including lysophospha …
Henstridge CM, Balenga NA, Kargl J, Andradas C, Brown AJ, Irving A, Sanchez C, Waldhoer M.Mol Endocrinol. 2011 Nov;25(11):1835-48. doi: 10.1210/me.2011-1197. Epub 2011 Sep 29.PMID: 21964594Free PMC article.Review.
Emerging data suggest that off-target cannabinoid
effects may be mediated via novel seven-transmembrane spanning/G
protein-coupled receptors. Due to its cannabinoid sensitivity, the G protein-coupled receptor 55 (GPR55) was recently proposed as a candidate; however, …
Falasca M, Ferro R.Adv Biol Regul. 2016 Jan;60:88-93. doi: 10.1016/j.jbior.2015.10.003. Epub 2015 Oct 28.PMID: 26588872Review.
Lysophosphatidylinositol (LPI) is a
well-known bioactive lipid that is able to activate signalling cascades
relevant to cell proliferation, migration, survival and tumourigenesis.
It is well-established that the G protein-coupled receptor 55 (GPR55) is the specific …
Arifin SA, Falasca M.Metabolites. 2016 Jan 15;6(1):6. doi: 10.3390/metabo6010006.PMID: 26784247Free PMC article.Review.
In this review, we will focus on the physiological and
pathophysiological roles of the lysophospholipid mediator lysophosphatidylinositol (LPI) and its receptor G-protein coupled receptor 55 (GPR55) in metabolic diseases. ...
Hurst K, Badgley C,
Ellsworth T, Bell S, Friend L, Prince B, Welch J, Cowan Z, Williamson R,
Lyon C, Anderson B, Poole B, Christensen M, McNeil M, Call J, Edwards
JG.Hippocampus. 2017 Sep;27(9):985-998. doi: 10.1002/hipo.22747. Epub 2017 Jun 27.PMID: 28653801Free PMC article.
GPR55, an orphan G-protein coupled receptor, is activated by lysophosphatidylinositol (LPI) and the endocannabinoid anandamide, as well as by other compounds including THC. ..
"Pleckstrin homology domain (PH domain) or (PHIP) is a protein domain of approximately 120 amino acids that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton.[1][2][3][4][5][6][7]
Individual PH domains possess specificities for phosphoinositides phosphorylated at different sites within the inositol ring, e.g., some bind phosphatidylinositol (4,5)-bisphosphate but not phosphatidylinositol (3,4,5)-trisphosphate or phosphatidylinositol (3,4)-bisphosphate,
while others may possess the requisite affinity. This is important
because it makes the recruitment of different PH domain containing
proteins sensitive to the activities of enzymes that either
phosphorylate or dephosphorylate these sites on the inositol ring, such
as phosphoinositide 3-kinase or PTEN,
respectively. Thus, such enzymes exert a part of their effect on cell
function by modulating the localization of downstream signaling proteins
that possess PH domains that are capable of binding their phospholipid
products.
Structure
The 3D structure of several PH domains has been determined.[11] All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets, followed by a C-terminalamphipathic
helix. The loops connecting the beta-strands differ greatly in length,
making the PH domain relatively difficult to detect while providing the
source of the domain's specificity. The only conserved residue among PH
domains is a single tryptophan (W) located within the alpha helix that serves to nucleate the core of the domain.
Proteins containing PH domain
PH domains can be found in many different proteins, such as OSBP or ARF. Recruitment to the Golgi apparatus
in this case is dependent on both PtdIns and ARF. A large number of PH
domains have poor affinity for phosphoinositides and are hypothesized to
function as protein binding domains. A Genome-wide look in Saccharomyces cerevisiae
showed that most of the 33 yeast PH domains are indeed promiscuous in
binding to phosphoinositides, while only one (Num1-PH) behaved highly
specific .[12] Proteins reported to contain PH domains belong to the following families:
Pleckstrin,
the protein where this domain was first detected, is the major
substrate of protein kinase C (PKC) in platelets. Pleckstrin contains two PH
domains. ARAP proteins contain five PH domains.
PLEKHF2 (Pleckstrin Homology And FYVE Domain Containing 2) is a Protein Coding gene.
An important paralog of this gene is PLEKHF1.
UniProtKB/Swiss-Prot Summary for PLEKHF2 Gene
May play a role in early endosome fusion
upstream of RAB5, hence regulating receptor trafficking and fluid-phase
transport. Enhances cellular sensitivity to TNF-induced apoptosis
(PubMed:18288467).
This gene encodes a serine/threonine-protein
kinase that functions in cell division. Together with the kinesin KIF14,
this protein localizes to the central spindle and midbody, and
functions to promote efficient cytokinesis. This protein is involved in
central nervous system development. Polymorphisms in this gene are
associated with bipolar disorder and risk for schizophrenia. Alternative
splicing results in multiple transcript variants. [provided by RefSeq,
Aug 2011]
Plays a role in cytokinesis. Required for
KIF14 localization to the central spindle and midbody. Putative RHO/RAC
effector that binds to the GTP-bound forms of RHO and RAC1. It probably
binds p21 with a tighter specificity in vivo. Displays serine/threonine
protein kinase activity. Plays an important role in the regulation of
cytokinesis and the development of the central nervous system.
Phosphorylates MYL9/MLC2.
