Scinovex
article Open AccessTop 10% cited

A Novel Serum Protein Similar to C1q, Produced Exclusively in Adipocytes

Journal of Biological Chemistry · 1995 · Vol. 270(45) · pp. 26746–26749
Philipp E. SchererSuzanne WilliamsM FoglianoGiulia BaldiniHarvey F. Lodish

Abstract

We describe a novel 30-kDa secretory protein, Acrp30 (adipocyte complement-related protein of 30 kDa), that is made exclusively in adipocytes and whose mRNA is induced over 100-fold during adipocyte differentiation. Acrp30 is structurally similar to complement factor C1q and to a hibernation-specific protein isolated from the plasma of Siberian chipmunks; it forms large homo-oligomers that undergo a series of post-translational modifications. Like adipsin, secretion of Acrp30 is enhanced by insulin, and Acrp30 is an abundant serum protein. Acrp30 may be a factor that participates in the delicately balanced system of energy homeostasis involving food intake and carbohydrate and lipid catabolism. Our experiments also further corroborate the existence of an insulin-regulated secretory pathway in adipocytes.

MeSH terms

Adipose TissueAmino Acid SequenceAnimalsBlood ProteinsCloning, MolecularInsulinMolecular Sequence DataMolecular WeightProteinsRepetitive Sequences, Nucleic AcidMolecular StructureComplement C1q3T3 CellsIntercellular Signaling Peptides and ProteinsMice
Citations
3,219
FWCI
3.08
field-weighted impact
References
30
Percentile
92%
vs. same field & year
Citations per year
Cited by
Understanding Adipocyte Differentiation
Physiological Reviews · 1998 · 2,384 citations
Adipose Tissue
Diabetes · 2006 · 1,059 citations
Adiponectin, a Therapeutic Target for Obesity, Diabetes, and Endothelial Dysfunction
International Journal of Molecular Sciences · 2017 · 1,137 citations
Insulin resistance: Review of the underlying molecular mechanisms
Journal of Cellular Physiology · 2018 · 916 citations
Adiponectin and Metabolic Syndrome
Arteriosclerosis Thrombosis and Vascular Biology · 2003 · 1,204 citations
Citation Network

How this paper connects to the literature. Drag to explore, click any node to open that paper.