Humanin (20mg – 100mg)

Humanin

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Peptide Partners Manufacturer Id: WF03

Batch Id:  HP20250805

Research Studies

(for educational purposes only)

Study 1: Humanin activates integrin αV–TGFβ axis and leads to glioblastoma progression

Authors: Cuong P. Ha, Tuyen N. M. Hua, Vu. T. A. Vo, Jiyeon Om, Sangwon Han, Seung-Kuy Cha, Kyu-Sang Park & Yangsik Jeong

Source: https://www.nature.com/articles/s41419-024-06790-8

Scientific Findings

The study investigates the role of the mitochondria-derived peptide humanin in glioblastoma progression. It demonstrates that humanin is highly expressed in glioblastoma tissues and can induce glioblastoma stem cell (GSC) attachment, filopodia formation, and migration through direct binding to integrin αVβ8. Humanin activates the integrin αV–TGFβ signaling axis, leading to canonical TGFβ pathway activation, promoting tumor cell invasion, angiogenesis, and overall tumor aggressiveness. The research combines in silico, in vitro, and in vivo approaches, showing that humanin facilitates glioblastoma progression via integrin-mediated cell adhesion and subsequent TGFβ signaling, ultimately contributing to poorer prognosis. Targeting the humanin–integrin–TGFβ axis may offer therapeutic potential.

Plain English Interpretation

This study shows that a small protein called humanin, made inside the mitochondria, helps brain cancer cells stick together and move around more easily, making the cancer more aggressive. Humanin binds directly to a specific receptor on the cancer cells called integrin αVβ8, which then turns on a signaling pathway involving TGFβ that encourages the cancer to invade nearby tissues and grow new blood vessels. These findings suggest that blocking humanin or its interaction with these receptors could be a new way to treat this deadly brain cancer.

Study 2: Humanin variants aggregate to produce different fibril morphologies

Authors: Daniel L. Morris, Sarah B. Nyenhuis, James M. Gruschus, David A. Nyenhuis, Rashmi Puja, Jenny E. Hinshaw, Nico Tjandra

Source: https://www.sciencedirect.com/science/article/pii/S0021925825022537

Scientific Findings

This study investigates the fibrillization of Humanin (HN) and its variants using transmission electron microscopy and other biophysical techniques. The research demonstrates that HN forms amyloid-like β-sheet fibrils and that specific mutations can inhibit this process. These mutations are linked to secretion deficiencies in vitro, emphasizing the role of β-sheet structures in membrane interactions. The study also highlights that these structural transitions are necessary for HN to interact with BCL-2 family proteins and inhibit apoptosis, suggesting that the fibrillization of HN is a key aspect of its cytoprotective function.

Plain English Interpretation

This research explores how the small protein Humanin clumps together to form fibers, similar to those seen in some diseases. By creating different versions of Humanin, the scientists found that the protein’s ability to form these fibers is crucial for its protective effects against cell death. The study suggests that the shape and structure of Humanin are essential for it to work correctly, particularly in how it interacts with cell membranes and other proteins involved in cell survival.

Study 3: The Mitochondrial-Derived Peptide Humanin Protects RPE Cells From Oxidative Stress, Senescence, and Mitochondrial Dysfunction

Authors: Parameswaran G Sreekumar, Keijiro Ishikawa, Chris Spee, Hemal H Mehta, Junxiang Wan, Kelvin Yen, Pinchas Cohen, Ram Kannan, David R Hinton

Source: https://pmc.ncbi.nlm.nih.gov/articles/PMC4811181/

Scientific Findings

The study investigates the expression of humanin (HN) in human retinal pigment epithelial (hRPE) cells and its effects on oxidative stress–induced cell death, mitochondrial bioenergetics, and senescence. Humanin localizes to cytoplasmic and mitochondrial compartments in RPE cells. Exogenous HN is taken up by RPE cells, colocalizing with mitochondria, and inhibits reactive oxygen species formation, restoring mitochondrial bioenergetics. HN increases mitochondrial DNA copy number, upregulates mitochondrial biogenesis regulator mtTFA, and protects RPE cells from oxidative stress–induced apoptosis and senescence. It also maintains transepithelial resistance in polarized RPE monolayers under oxidative stress. The data suggest HN could be a potential therapeutic agent for retinal degeneration including AMD.

Plain English Interpretation

This study shows that a small protein called humanin, produced inside mitochondria, helps protect eye cells responsible for vision from damage caused by oxidative stress. When extra humanin is added, it gets into the cells and helps keep their mitochondria healthy, prevents cell death and aging, and helps maintain the barrier functions of these cells. These findings suggest that humanin might be useful in developing treatments for age-related eye diseases like macular degeneration.