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Human Monoclonal PPP1R3A Primary Antibody für ELISA, WB - ABIN537103
Gao, Zhou, Xie, Zhang, Rahmeh, Huang, Lee, Lee: Protein phosphatase-1 is targeted to DNA polymerase delta via an interaction with the p68 subunit. in Biochemistry 2008
Show all 2 Pubmed References
results show that dysfunction of subunit PPP1R3A of protein phosphatase 1 leads to weight gain, increased fat deposition and insulin resistance
Mice in which human PPP1R3A C1984DeltaAG replaced mouse PP1R3A had decreased muscle glycogen levels because failure of the truncated mutant to bind glycogen & colocalize with glycogen synthase (GS) decreased GS & increased glycogen phosphorylase activity.
Backcrossing of G(M)-/- mice onto two different genetic backgrounds gave rise to lean, glucose-tolerant, insulin-sensitive G(M)-/- mice indicating that at least one variant gene,is required for the development of the prediabetic phenotype of obese mice.
Disruption of the Ppp1r3a gene does not result in either fat deposition or insulin resistance, but PPP1r3a is essential for control of glycogen metabolism by exercise.
Variant in PPP1R3A is associated with type 2 diabetes.
In the univariate analyses, TP53, PPP1R3A, and KMT2B were significantly more frequently mutated in interval cancers than in screen-detected cancers.
results demonstrate that hScrib acts as a scaffold to integrate the control of the PP1gamma and ERK signaling pathways and explains how disruption of hScrib localisation can contribute towards the development of human malignancy
A joint effect between the Asp905 and BMI increases the risk of type 2 diabetes, and Asp905Tyr and ARE polymorphism of PPP1R3 gene are not the major diabetogenic gene variants in Chinese population.
We describe a family in which five individuals with severe insulin resistance, but no unaffected family members, were compound heterozygous with respect to frameshift/premature stop mutations in two unlinked genes, PPARG and PPP1R3A
G(M) promotes glycogen storage and inversely regulates glycogen synthase and glycogen phosphorylase activities, while, specifically, synthase phosphatase activity of G(M)-PP1 is inhibited by glycogen.
Among the largest cohort of nondiabetic subjects (Caucasian, n = 112), the presence of the deletion allele (ARE-2) was associated with insulin resistance and hyperandrogenemia.
Inactivation of PPP1R3 gene is associated with tumor progression and metastasis of colorectal cancers
PPP1R3A C1984DeltaAG (stop codon 668) isthe 1st prevalent mutation that directly impairs glycogen synthesis & decreases glycogen levels in human skeletal muscle. It is present in approximately 1 in 70 UK whites.
The glycogen-associated form of protein phosphatase-1 (PP1) derived from skeletal muscle is a heterodimer composed of a 37-kD catalytic subunit and a 124-kD targeting and regulatory subunit. This gene encodes the regulatory subunit which binds to muscle glycogen with high affinity, thereby enhancing dephosphorylation of glycogen-bound substrates for PP1 such as glycogen synthase and glycogen phosphorylase kinase.
protein phosphatase 1 glycogen-associated regulatory subunit
, protein phosphatase 1 regulatory subunit 3A
, protein phosphatase type-1 glycogen targeting subunit
, glycogen and sarcoplasmic reticulum binding subunit, skeletal muscle
, glycogen-associated regulatory subunit of protein phosphatase-1
, protein phosphatase 1 glycogen- associated regulatory subunit
, protein phosphatase 1 regulatory subunit GM
, protein phosphatase 1, regulatory (inhibitor) subunit 3A
, serine /threonine specific protein phosphatase
, type-1 protein phosphatase skeletal muscle glycogen targeting subunit