Parvalbumin α (PVALB) is a member of the parvalbumin family. PVALB is a high affinity calcium ion-binding protein, with two EF hand domains. PVALB is structurally and functionally similar to calmodulin and troponin C, it can bind two calcium ions. Parvalbumin is thought to be involved in relaxation after contraction in muscle. Parvalbumin is expressed in a specific population of GABAergic interneurons, which are believed to have a role in maintaining the balance between excitation and inhibition in the cortex as well as the hippocampus.
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4(PIN4) is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and is vital for cell cycle regulation. PIN4 has 2 different isoforms: PAR14 and PAR17. Furthermore, PIN4 protein binds to double-stranded DNA under physiological salt conditions. PIN4 is involved as a ribosomal RNA processing factor in ribosome biogenesis. The PAR14 binds to tightly bent AT-rich stretches of double-stranded DNA, but PAR17 binds to double-stranded DNA.
Nicotinamide phosphoribosyltransferase (NAMPT); also known as pre-B-cell colony-enhancing factor 1 (PBEF1) or visfatin; is an enzyme belonging to the family of glycosyltransferases; to be specific; the pentosyltransferases. This enzyme participates in nicotinate and nicotinamide metabolism. This enzyme catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1- pyrophosphate to yield nicotinamide mononucleotide; one step in the biosynthesis of nicotinamide adenine dinucleotide. NAMPT is also considered as an essential enzyme mediating granulocyte colony-stimulating factor (G-CSF)-triggered granulopoiesis in healthy individuals and in individuals with severe congenital neutropenia. Intracellular NAMPT and NAD+ amounts in myeloid cells; as well as plasma NAMPT and NAD+ levels; were increased by G-CSF treatment of both healthy volunteers and individuals with congenital neutropenia.
Pre-B cell colony enhancing factor (PBEF) was originally identified as a cytokine that potentiated the clonal expansion and differentiation of pre-B cells, but it is also acknowledged to be the ubiquitous intracellular enzyme nicotinamide phosphoribosyltranferase (NAMPT) and the adipokine “visfatin”. PBEF is constitutively expressed in the fetal membranes where its greatest expression is in the amnion. It has intracellular and extracellular forms. Most of the intracellular functions of PBEF are due to its role as a Nampt which can induce angiogenesis through upregulation of VEGF and VEGFR and secretion of MCP-1. Extracellular PBEF has been shown to increase inflammatory cytokines, such as TNF-α, IL-1β, IL-16, and TGF-β1. PBEF also increases the production of IL-6, TNF-α, and IL-1β in CD14+ monocyctes, macrophages, and dendritic cells, enhances the effectiveness of T cells.
Phenazine Biosynthesis-Like Domain-Containing protein (PBLD) belongs to the phenazine biosynthesis-like protein (PhzF) family, which is expressed in most tissues. PBLD takes part in the MAPK signaling pathway, and is involved in multiple basic cellular functions. The expression of PBLD can be increased in several disease processes, including insulin resistance, folate deficiency and hypotension.
Pterin-4-α-Carbinolamine Dehydratase (PCBD1) is the founding member of the Pterin-4-α-Carbinolamine Dehydratase Family. PCBD1 is involved in Tetrahydrobiopterin biosynthesis. It seems to prevent the formation of 7-Pterins and accelerate the formation of Quinonoid-BH2. Furthermore, PCBD1 regulates the homodimerization of the transcription factor Hepatocyte Nuclear Factor 1 (HNF1) and enhances its transcriptional activity. Defects in PCBD1 are the cause of BH4-Deficient Hyperphenylalaninemia Type D (HPABH4D). HPABH4D is characterized by the excretion of 7-substituted Pterins in the urine of affected patients.
Inserisci la tua e-mail e seleziona le aree di interesse per ricevere le ultime novità, approfondimenti e promozioni.
Seleziona uno o più ambiti di interesse per ricevere comunicazioni più utili e mirate.
2025 TEMA Ricerca - All Rights Reserved.
