ANGPTL8 Antibodies

Angiopoietin-like protein 8 (ANGPTL8)

Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels (PubMed:22569073, PubMed:22809513, PubMed:23150577). May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state (By similarity).

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Gene Information

Human
Gene Name:	ANGPTL8
Uniprot:	Q6UXH0
Entrez:	55908

Family

Belongs to:
ANGPTL8 family

Alternative Names

Angiopoietin like Protein 8; Angiopoietin-like Protein 8; ANGPTL8; Betatrophin; C19orf80; chromosome 19 open reading frame 80; Gm6484; hepatocellular carcinoma-associated gene TD26; hepatocellular carcinoma-associated protein TD26; Lipasin; PRO1185; PVPA599; RIFL; TD26; UNQ599

Molecular Weight

Mass (kDA):
22.105 kDA

Genomic Context

Human
Location:	19p13.2
Sequence:	19; NC_000019.10 (11239619..11241943)

Tissue Specificity

Predominantly expressed in liver. Also expressed in adipose tissues.

Subcellular Localizations

Secreted.

Diseases

• Diabetes mellitus, insulin-dependent (IDDM)

Interacting Proteins

• RCHY1

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/ANGPTL8

What Are the Best Uses of the ANGPTL8 Marker?

What Are the Best Uses Of The ANGPTL1 Marker? This article will explore the benefits of ANGPTL1, including the fact that it inhibits the antiapoptotic protein Bcl-2. Angptl8 is also known to promote cell proliferation. As such, it has numerous applications in research, from cancer screening to cell differentiation. Read on to learn more.

ANGPTL1 inhibits antiapoptotic protein Bcl-2

ANGPTL1 is a novel inhibitor of the antiapoptotic protein Bcl2. This protein is responsible for the translocation of apoptosis-inducing proteins inside the cell nucleus. It is thought to form part of a multiprotein complex that includes CDK1, PP1 and Nucleolin. Although the exact mechanisms of nuclear translocation remain unclear, Bcl-2 is believed to exhibit subcellular localizations.

ANGPTL1 acts as an inhibitor of the antiapoptotic protein Bcl 2. Bax is a 26-kDa protein found in mitochondria. It also appears on the ER membrane and nuclear envelope. Although it shares structural similarities with BCL-XL, the structure of Bcl-2 differs. While BCL-XL has been shown to sequester both BAX and BAK, BCL-2 only constrains BAX. This means that Bcl-2 cannot prevent the activation of BAK.

Biologists Petros AM and Andrews DW have shown that the Bcl-2 family members interact with membranes to promote apoptosis. Using crystal structures of Bcl-2 and BAX, they have identified BH3 domains as the dominant interactions between these proteins. Further, Angptl1 inhibits antiapoptotic protein Bcl-2 by binding to its BH3 domain.

The BCL-2 family contains members that are both pro-apoptotic and anti-apoptotic. These two subgroups contain anti-apoptotic BCL-2, pro-apoptotic pore-forming proteins BAX, BAK, and BAK/Boo, and pro-apoptotic BH3-only proteins.

The mechanisms responsible for increased levels of BCL-2 include gene amplification and chromosome translocations. In addition, gene-repressive miRNAs are downregulated or deleted. Overexpression of BCL-2 originates from the loss of repression of miRNA 15/16. The increased BCL-2 levels result from apoptosis in a leukemic cell line model.

BCL-2 is expressed in leukemic and non-leukemic cells, as well as in many types of normal hematopoietic cells. Its expression varies according to cell type and stage of maturation. In pre-B cells, BCL-2 levels increase; as the cells progress toward mature B-cell stages, the levels decrease.

The BCL-2 family of proteins regulate the integrity of mitochondrial outer membranes. The vast majority of members of this family localize in several subcellular compartments and participate in non-apoptotic functions. Though Bcl-2 family proteins are structurally similar, they have significant differences in subcellular distribution. The latter was initially attributed to subtle intramolecular variations in TM amino acid composition. The findings suggest that BCL-2 is a target for therapy of many diseases.

ANGPTL1 inhibits antiappoptotic protein Bcl-2 by inducing the BH4 domain. Bcl-2 family members are important in cancer therapy. They have been shown to be useful in treating various types of cancer. Some of the known interactions between Bcl-2 and transcription factors are detailed below. In addition to Lewis A, Ruvolo PP and Bcl-XL also have other important roles in cancer.

The Bax and Bcl-2 family proteins regulate mitochondrial permeabilization through post-translational modifications. Bax homodimers are associated with apoptosis. Bax homodimers are located in the mitochondrial apoptosis pore, whereas Bax monomers bind Bcl-2 homodimers.

It promotes cell proliferation

One study showed that the ANGPTL8 marker promotes cell growth in beta cells. In this study, scientists found that aged mice had higher levels of Angptl8 than young ones, but the beta cells were not as active as those of the control group. These results challenge the betatrophin hypothesis that the ANGPTL8 marker induces beta cell proliferation. However, it is not yet known whether this effect occurs in humans.

Although more studies are needed, preliminary findings suggest that ANGPTL8 has a potential role in MetS. Its expression increases along with HsCRP levels and may be used as a biomarker for the disease. Further, Eisenberg MJ, et al., have published a systematic review of the association between ANGPTL8 and cardiovascular risk. These results suggest that ANGPTL8 may be a useful predictor for MetS and CVD.

Aside from the role in cell proliferation, the ANGPTL8 marker is also associated with angiogenesis, a process in which blood vessels become inflamed and expand. The markers ANGPTL8 and ANGPL-2 exert a promoting effect on angiogenesis and tumor growth. Angptl2 is overexpressed in many types of cancer, including gastric cancer. ANGPTL2 promotes EMT and cell migration, but downregulation reverses this process and inhibits cell migration. They may participate in an ERK/MAPK cascade that activates ANGPTL2 and thereby promotes tumour growth.

Recently, the role of ANGPTL8 in glucose homeostasis has been called into question. A recent study showed that mice with Gm6484-knockout were able to maintain normal glucose levels even when exposed to S961, a compound that promotes beta cell replication. However, the failure of this experiment to induce beta cell replication in humans could have resulted from the heterologous species used in the study.

Besides being associated with diabetes and obesity, ANGPTL8 does not control pancreatic beta cell expansion. In fact, there are no human studies that indicate that ANGPTL8 is not a beta cell expansion factor. The expression of betatropin in humans is associated with type 2 diabetes and obesity. The authors of the study have found that ANGPTL8 overexpression induces a seventeen-fold increase in beta cell replication in insulin-resistant (ICR) mice. Not only did they find an increase in beta cell area, but the mice had improved glucose tolerance and insulin sensitivity.

Betatrophin is a protein produced by the liver. The proteins in the liver may contribute to the increased b-cell proliferation in an insulin-resistant state. Some researchers suggested that betatrophin may be a factor in this process. In response to this, Yi et al9. suggested that mice lacking betatrophin/ANGPTL8 had normal b-cell expansion in insulin-resistant mice.

It inhibits antiapoptotic protein Bcl-xl

Boster Bio ANGPTL8 inhibitor blocks the activity of the antiapoptotic protein Bclxl in a variety of cancers. It is produced by a highly specific gene called BAX. BAX is a member of the BCL2 family of proteins that function as homo or heterodimers and play a variety of roles within cellular processes. Specifically, BAX functions as an apoptotic activator.

Boster Bio develops research antibodies and ELISA kits for the detection of various biomarkers in cancer, developmental biology, neurosciences, and inflammation. The antibodies are validated against panels of over 250 tissues and are picogram-level sensitive. The company's immunological reagents are available through its subsidiary tebu-bio.