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Literature summary for 3.1.3.4 extracted from

  • Reue, K.; Dwyer, J.R.
    Lipin proteins and metabolic homeostasis (2009), J. Lipid Res., 50 Suppl, S109-S114.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
lipin-1 adenovirus overexpression Mus musculus

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
adipocyte
-
Homo sapiens
-
adipose tissue lipin-1 Mus musculus
-
brain lipin-1 Mus musculus
-
heart lipin-1 Mus musculus
-
hepatocyte
-
Rattus norvegicus
-
kidney lipin-1 Mus musculus
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liver lipin-1 Mus musculus
-
skeletal muscle lipin-1 Mus musculus
-

Synonyms

Synonyms Comment Organism
lipin-1
-
Mus musculus
lipin-1
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Homo sapiens
lipin-1
-
Rattus norvegicus
lipin-2
-
Mus musculus
lipin-2
-
Homo sapiens
lipin-3
-
Mus musculus

Expression

Organism Comment Expression
Mus musculus hepatic lipin-1 expression levels and VLDL secretion both increase in obese individuals following gastric bypass surgery up
Homo sapiens positive correlation between lipin-1 expression levels in adipose tissue and insulin sensitivity in obese subjects with normal or impaired glucose tolerance and in healthy young men. Lipin-1 expression is induced in adipocytes by insulin-sensitizing drugs such as thiazolidinediones and harmine. Lipin-2 expression in human adipose tissue up

General Information

General Information Comment Organism
malfunction knockdown of endogenous lipin-1 expression decreases the secretion of newly synthesized triglycerides Rattus norvegicus
malfunction lipin-1 deficiency produces lipodystrophy. In fatty liver dystrophy mice, occurrence of fatty liver and hypertriglyceridemia during the neonatal period, and peripheral neuropathy, which progresses throughout adulthood. Fatty liver dystrophy mice are lipodystrophic, develop insulin resistance, and have increased susceptibility to atherosclerosis. Lipin-2 cannot compensate for lipin-1 function in adipose tissue of fatty liver dystrophy mice Mus musculus
malfunction mutations affecting lipin-1 and lipin-2 cause human disease. Human lipodystrophic subjects do not show causative mutations in the LPIN1 gene. Mutations in LPIN1 in patients with recurrent acute myoglobinuria in childhood. Distinct inactivating mutations in patients from several ethnic backgrounds and at dispersed locations throughout the lipin-1 protein structure. LPIN1 polymorphisms are associated with numerous metabolic traits, like insulin and/or glucose levels, resting metabolic rate, and systolic blood pressure. LPIN1 polymorphisms associated with response of type 2 diabetic patients to rosiglitazone. LPIN1 polymorphism can cause an amino acid substitution within the C-LIP domain, which is associated with statin-induced myopathy Homo sapiens
physiological function enhanced expression of lipin-1 in a hepatocyte cell line leads to stimulation of triglyceride synthesis and secretion Rattus norvegicus
physiological function lipin-1 accounts for all of the PAP activity in adipose tissue and skeletal muscle, but only part of the activity in liver, heart, kidney, and brain. Enhanced lipin-1 expression in adipose tissue or skeletal muscle promotes obesity. Lipin-2 and/or lipin-3 are capable of promoting VLDL synthesis and secretion Mus musculus
physiological function lipin-2 expression in adipose tissue may compensate for lack of lipin-1 Homo sapiens