HYOU1

Official Full Name

hypoxia up-regulated 1

Organism

Homo sapiens

GeneID

10525

Background

The protein encoded by this gene belongs to the heat shock protein 70 family. This gene uses alternative transcription start sites. A cis-acting segment found in the 5' UTR is involved in stress-dependent induction, resulting in the accumulation of this protein in the endoplasmic reticulum (ER) under hypoxic conditions. The protein encoded by this gene is thought to play an important role in protein folding and secretion in the ER. Since suppression of the protein is associated with accelerated apoptosis, it is also suggested to have an important cytoprotective role in hypoxia-induced cellular perturbation. This protein has been shown to be up-regulated in tumors, especially in breast tumors, and thus it is associated with tumor invasiveness. This gene also has an alternative translation initiation site, resulting in a protein that lacks the N-terminal signal peptide. This signal peptide-lacking protein, which is only 3 amino acids shorter than the mature protein in the ER, is thought to have a housekeeping function in the cytosol. In rat, this protein localizes to both the ER by a carboxy-terminal peptide sequence and to mitochondria by an amino-terminal targeting signal. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2014]

Synonyms

IMD59; Grp170; HSP12A; ORP150; GRP-170; ORP-150;

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Detailed Information

Recent Research Progress

HYOU1, hypoxia up-regulated 1 protein, also known as oxygen-regulated protein 150 (ORP150), encoded by HYOU1 gene, belongs to heat shock protein 70 (HSP70) family. Under hypoxia, HYOU1 protein can be accumulated in the endoplasmic reticulum (ER) to protect cells from hypoxia interference, which can come to a conclusion that HYOU1 protein is thought to play an important role in protein folding and secretion in the ER, while inhibition of HYOU1 expression can accelerate cell apoptosis. As inhibition of HYOU1 protein is closely related to the acceleration of apoptosis, it suggests that the protein has important cytoprotective effects in hypoxia-induced cellular uptake.

HYOU1 and tumorigenesis

It is reported that HYOU1 protein was up-regulated in a variety of cancers, such as prostate cancer, bladder cancer, breast cancer, colorectal cancer, and other tumors, and high expression of HYOU1 was positively correlated with high invasion and poor diagnosis. Over-expressed HYOU1 protein can significantly inhibit the tumor cell apoptosis induced by anti-tumor drugs, and promote the resistance of tumor cells to chemotherapy. In the study of malignant tumors caused by Kaposi's sarcoma-associated herpesvirus (KSHV) which promotes tumorigenesis and inflammation mainly by expressing vIL-6, the results performed that HYOU1 increases endogenous vIL-6 protein levels and HYOU1 facilitates vIL-6-induced JAK/STAT signaling, migration, and survival in endothelial cells. Furthermore, the research suggested that HYOU1 can also modulate vIL-6's ability to induce CCL2, a chemokine involved in cell migration. Collectively, HYOU1 is important for vIL-6 function and may play a role in the pathogenesis of KSHV-associated cancers. What’s more, Yujuan Zhou et al. found that the expression of HYOU1 both at mRNA level and protein level was up-regulated significantly in nasopharyngeal carcinoma (NPC) tissues, and HYOU1 protein expression was positively correlated with clinical staging and metastasis of NPC. Therefore, HYOU1 can be regarded as potential molecular biomarker for progression and prognosis of NPC.

HYOU1 and immune-metabolic diseases

Interestingly, HYOU1 also appears to be associated with immune-metabolic diseases. Haapaniemi E M et al. described a novel immune-metabolic syndrome, features hypoglycemia and severe bacterial and herpetic infections, caused by recessive HYOU1 mutations. They found that the binding characteristics of the mutant HYOU1 protein appeared to have changed, leading to heterotopic protein binding, and significant enrichment of redox proteins was also noted in the HYOU1 binding couples of affinity purified mass spectrometry (AP-MS). And changes in metabolites involved in the redox balance lead to increased mitochondrial count and production of highly reactive oxygen species in patients' neutrophils. HYOU1 is a chaperone that localizes to endoplasmic reticulum (ER) and mitochondria, and participates in cell stress responses, including oxidative stress and unfolded protein response. Because most genes that cause congenital neutropenia perform similar functions, HYOU1 was considered a good candidate.

References:

Zhou Y, et al. HYOU1, Regulated by LPLUNC1, Is Up-Regulated in Nasopharyngeal Carcinoma and Associated with Poor Prognosis. Journal of Cancer, 2016, 7(4):367.
Giffin L, et al. Modulation of Kaposi's Sarcoma-Associated Herpesvirus Interleukin-6 Function by Hypoxia-Upregulated Protein 1. Journal of Virology, 2014, 88(16):9429-9441.
Haapaniemi E M, et al. Combined immunodeficiency and hypoglycemia associated with mutations in hypoxia upregulated 1. Journal of Allergy & Clinical Immunology, 2017, 139(4):1391.

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