PHYTIN, Fytiini (IP6) An interesting molecule in human food and the human biochemistry.
Rescher U, Ruhe D, Ludwig C, Zobiack N, Gerke V (2004) Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes. J Cell Sci 117: 3473–3480CrossrefCASPubMedWeb of Science®Google Scholar
Janetopoulos C, Devreotes P (2006) Phosphoinositide signaling plays a key role in cytokinesis. J Cell Biol 174: 485–490CrossrefCASPubMedWeb of Science®Google Scholar
Reaktion merkitys: Katabolinen inositolipolyfosfaattien purkaminen fosfaateista takaisin siihen inositolimuotoon, muotoon, josta voi jälleen alkaa fosfolipidien synteesi ( kuten myoinositolin fosfatidihapon ja CTP-energian avulla de novo) solussa kohti PI, PIP, PIP2 muotoja).
https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/annexin
Theodora S. Ross, in Cellular and Molecular Mechanisms of Inflammation: Signal Transduction in Inflammatory Cells, Part A, 1992
The primary sequence of the cyclic hydrolase is identical to that of lipocortin III, a member of a large family of homologous calcium- and phospholipid-binding proteins without defined biological functions (88). Some of these proteins have been shown to be phosphorylated in response to growth factors. The purified enzyme (33 kDa) is inhibited by inositol 2-phosphate [Ins(2)P], Zn2+, and glycerophosphoinositol (GroPIns) and stimulated by acidic phospholipids (87, 89). The pattern of interaction with particular phospholipids is the same as that previously observed for lipocortins (88, 90). The mechanism of inhibition by GroPIns is due to its ability to act as a substrate for this enzyme (89). The regulatory significance of this reaction is unclear, as the level of GroPIns-hydrolyzing activity measured in cellular extracts does not inversely correlate with the cellular levels of GroPIns (T. S. Ross and P. W. Majerus, unpublished observations). The presence of significant amounts of Ins(2)P and GroPIns in cells has been well documented (89, 91) and suggests that they may function as regulators of cellular cIns(1:2)P levels.
Measurement of the cyclic hydrolase activity in cellular extracts has unveiled a very interesting pattern. Cells with relatively low to nondetectable activity were either completely transformed or partially transformed (92). When levels of cyclic inositol phosphates were measured in these cells, it was found that cIns(1:2)P increased in proportion to the decreased cyclic hydrolase activity. The enzyme activity is also increased within one cell type when it is in a confluent state as compared to a logarithmically growing state. Overexpression of cyclic hydrolase in cells decreases the cIns(1:2)P levels as well as the final saturation density. In addition, high endogenous expression of cyclic hydrolase in cells tends to correlate with the differentiated state (e.g., high levels in platelets, brain, and neutrophils and low levels in several immortalized tissue culture cell lines of fibroblasts and T cells). The finding that this correlation exists both in nature and during heterologous expression of the enzyme makes the discovery of a cellular function for cIns(1:2)P likely to be successful. Further studies of the regulation of the cyclic hydrolase activity and cIns(1:2)P cellular levels will yield valuable information as to how to continue the quest for the function(s) of the cyclic bond.
https://www.jlr.org/article/S0022-2275(20)34570-3/fulltext
https://www.nature.com/articles/ncomms9505
Jälkimmäisessä artikkelsisa näkyy se Ins-1 fosfaattimuoto, oka rikastuu PIP muotoon eli muuttuu samalla vesiliukoisten poly ja monofosfaattein puolelta rasvaliukoisiin, fosfolipidien puolelle, jolloin siitä tulee annexiinijärjestelmälle molekyyli, johon jokin ANX voi sitoutua. Ainakin ANXA2 tumankalvon modifioinneissa solunjaossa sytokineesin alussa. PI(4,5)P2 muoto on tuma-alueelle tunnusomainen PL-muoto. ( salvage tie, ei: de novo tie)
Normaalisti verisuonistossa kiertävästä Glu-plasminogeenistä muodstuu - sen havaittua hyytymää ja kiinnityttyä siihen suonen sisäpinnalla- plasminogeeniä. Normaalisti kuitenkin muodostuu myös angiostatiinia 3%:sti plasminogeenistä. Onpohdittu, miten se muodostuu.
tiedetään ainkin, että matrixmetalloproteiineista käsin- niiden aktivoiduttua plasmiinista preMMP-muodosta MMP-muotoon, usea MMP pystyy pilkkomaan Glu-PLG- muodsta angiotensiinia esiin. Näistä on mainittu elastaasi tässä alla olevassa linkissä. Elastaasi voi tuottaa kahta eri kokoa angiostatiinia: toisessa on 4 rinkulaa jäljellä ja toisessa vain 3 rinkulaa, niitä rinkuloita , joita plasminogeenillä ja plasmiinilla on 5 kpl.
Ainakin lyhemmällä angiostatiinilla on havaittu aivan tuumorin kasvua vastustavaa vaikutusta. Suoniston sisällä hyytymässä alkavaa neovaskularisaatiotaipumusta tietysti vastustaa heti jo angiostatiinin pitempikin muoto. tuumorfeista on identifioitu angiostatiinin kaltainen molekyyli, joka oli hieman päistään lyhempi kuin normaalit angiostatiinimuodot. Lääketehdas taas on kehittänyt angiostatiinimuodon, joka kattaa angiostatiinin molempien päiden rakenteet ja on tehty verisuoistossa kiertävästä plasminogeenistä. Sillä on todettu eläinkokeissa antiproleratiivista vaikutusta, tosin sen käyttäminen tai testaaminen lääkkeenä ei ole helppoa,sillä rakenneta täytyy säilyttää alle 70 celsiusasteen pakkasessa.
https://www.haemtech.com/products/protease-inhibitors/human-angiostatin
https://diapharma.com/plasminogen-plg/
Plasmin is released as a zymogen called plasminogen (PLG) from the liver into the factor IX systemic circulation. Two major glycoforms of plasminogen are present in humans – type I plasminogen contains two glycosylation moieties (N-linked to N289 and O-linked to T346), whereas type II plasminogen contains only a single O-linked sugar (O-linked to T346). Type II plasminogen is preferentially recruited to the cell surface over the type I glycoform. Conversely, type I plasminogen appears more readily recruited to blood clots."
(Tässä lähteessä kaavat Plasminogeeni, sen aktivaattorit t-PA kudosaktivaattori ja munuaisperäinen u-PA) .
Tämän kaltaista funktiota on usealla fosfohydrolaasilla, mutta tälle geenille ei löytynyt paikan lisäksi muuta erityistietoa. (Tällä ryhmällä
| NUDT3 | Nudix Hydrolase 3 | Protein Coding | 38 | GC06M069334 | 38.75 | ||
| 2 | NUDT4 | Nudix Hydrolase 4 | Protein Coding | 40 | GC12P093412 | 37.54 | |
| 3 | NUDT11 | Nudix Hydrolase 11 | Protein Coding | 37 | GC0XM051490 | 36.56 | |
| 4 | NUDT10 | Nudix Hydrolase 10 | Protein Coding | 35 | GC0XP051332 | 33.10 | |
| 5 | ENSG00000267689 | Diphosphoinositol Polyphosphate Phosphohydrolase 2, Pseudogene |
ENSG00000267689 (Diphosphoinositol Polyphosphate Phosphohydrolase 2, Pseudogene) is a Pseudogene.
https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P12429
ANXA3
Organism:
Homo sapiens (Human)
Synonyms:
ANX3
Uniprot:
P12429go to UniProt
Biological function:
Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate go to UniProt
Aliases for ANXA3 Gene
https://www.genecards.org/cgi-bin/carddisp.plgene=ANXA3&keywords=ANXA3
GeneCards Symbol: ANXA3
Annexin A3
ANX3
Inositol 1,2-Cyclic Phosphate 2-Phosphohydrolase
Placental Anticoagulant Protein III
35-Alpha Calcimedin
Lipocortin III
Annexin-3
PAP-III
Annexin III (Lipocortin III, 1,2-Cyclic-Inositol-Phosphate Phosphodiesterase, Placental Anticoagulant Protein III, Calcimedin 35-Alpha)
Annexin III (Lipocortin III)
Calcimedin 35-Alpha
Annexin III
External Ids for ANXA3 Gene
Entrez Gene Summary for ANXA3 GeneThis gene encodes a member of the annexin family. Members of this calcium-dependent phospholipid-binding protein family play a role in the regulation of cellular growth and in signal transduction pathways. This protein functions in the inhibition of phopholipase A2 and cleavage of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. This protein may also play a role in anti-coagulation. [provided by RefSeq, Jul 2008]
GeneCards Summary for ANXA3 Gene
ANXA3 (Annexin A3) is a Protein Coding gene. Diseases associated with ANXA3 include Ovarian Cancer and Prostate Cancer. Among its related pathways are Prostaglandin synthesis and regulation. Gene Ontology (GO) annotations related to this gene include calcium ion binding and calcium-dependent phospholipid binding. An important paralog of this gene is ANXA4.
UniProtKB/Swiss-Prot Summary for ANXA3 Gene
Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. ( ANXA3_HUMAN,P12429 )
