https://www.genecards.org/card/DHDDS
pidentää cis-prenyyliketjuja tuottan polyprenyyli runkoa
https://www.genecards.org/card/NUS1
Kondensoivat yhdessä IPP ja FPP muodostaen
erittäin pitkiä C90-C100 polypreenipyrofosfaatteja.
Sitten kolmannessa vaiheessa on uusia havaiittuja entsyymejäkin ja kolmen vaiheen askeleet. tapahtumia.
GeneCards Summary
DHRSX encodes a polyprenol dehydrogenase that supports dolichol biosynthesis and positive regulation of autophagy. It has dolichal reductase [NAD(P)+] activity and polyprenol dehydrogenase activity, placing it at the intersection of lipid metabolism and membrane-associated redox chemistry. The protein is active in the lipid droplet and is found in the extracellular region, endoplasmic reticulum membrane, and cytosol.
Through its catalytic activity, DHRSX participates in the dolichol biosynthetic process and dolichyl monophosphate biosynthetic process, both of which are linked to protein metabolism pathways. Expression measurements show notable levels in the endocrine system, proximal digestive tract, and female reproductive system, providing tissue context for its metabolic role. The combination of localization in the endoplasmic reticulum membrane and lipid droplet with activity in the cytosol and extracellular region aligns with a function in cellular lipid handling and redox-linked biosynthesis.
Pathogenic variants in DHRSX are reported in congenital disorder of glycosylation, type 1Dd. This disorder is the principal clinical association for the gene and connects DHRSX to a glycosylation defect syndrome.
https://www.genecards.org/card/ZBED1
ZBED1 encodes a DNA-binding transcriptional activator located in the pseudoautosomal region 1 of the X and Y chromosomes. It was first identified for similarity to Ac transposable elements, but it lacks transposase activity and instead functions in the nucleus. As a zinc finger BED-type factor, it is part of the transcriptional machinery that links promoter recognition to gene activation.
ZBED1 binds promoter elements in ribosomal protein genes, including RPS6 and RPL10A, and also binds promoter regions of genes related to cell proliferation such as histone H1. It functions as an E3 SUMO ligase that sumoylates CHD3, causing its dissociation from chromatin. This alleviates transcriptional repression, enhances RNA polymerase II recruitment, and drives expression of growth-related genes. The protein localizes to the nucleus, PML body, nucleoplasm, and centrosome, and expression is high in the female reproductive system with substantial RNA and protein expression in muscle, adipose, endocrine, hematopoietic, and male reproductive tissues.
Clinical links for ZBED1 are limited in the provided evidence, but its activity is tied to transcriptional control of growth-related genes and cell proliferation. No specific diseases or named therapeutic agents are described here.
Commun Biol
https://pubmed.ncbi.nlm.nih.gov/14770295/
Serpins are unique among the various types of active site proteinase inhibitors because they covalently trap their targets by undergoing an irreversible conformational rearrangement. Members of the serpin superfamily are present in the three major domains of life (Bacteria, Archaea and Eukarya) as well as several eukaryotic viruses. The human genome encodes for at least 35 members that segregate evolutionarily into nine (A-I) distinct clades. Most of the human serpins are secreted and circulate in the bloodstream where they reside at critical checkpoints intersecting self-perpetuating proteolytic cascades such as those of the clotting, thrombolytic and complement systems. Unlike these circulating serpins, the clade B serpins (ov-serpins) lack signal peptides and reside primarily within cells. Most of the human clade B serpins inhibit serine and/or papain-like cysteine proteinases and protect cells from exogenous and endogenous proteinase-mediated injury. Moreover, as sequencing projects expand to the genomes of other species, it has become apparent that intracellular serpins belonging to distinct phylogenic clades are also present in the three major domains of life. As some of these serpins also guard cells against the deleterious effects of promiscuous proteolytic activity, we propose that this cytoprotective function, along with similarities in structure are common features of a cohort of intracellular serpin clades from a wide variety of species.
Geeni HDAC11
https://www.genecards.org/card/HDAC11?search=HDAC,9-
Tämän artikkelin yhteydessä kerrotaan NOTCH- HLH signaalitiestä tarkasti,i
sillä tämä tumaan sijoittunut HDAC -geeni ja sen koodaama proteiini säätäa epigenetiikkaa ja kromatiinin organisaatiota NOTCH - THL signaalitiessäkin. eli T-lymfosyyttien kehitystä.
Sirtuiini-inhibiittorien kehittely on monimutkaisemoaa ja niitä ei esiinnyt kliinisessö käytössä vielä. HDAC inhibiittoteita on jo käytössä ja kombinoidussa kemoterapiassa.
NYKYVAIHE uusinta tietoa SIRT ja HDAC tutkimuksistq
