Icariin is a prenylflavonoid with anti-cancer properties and is studied for its diverse signaling effects observed in vivo. It has been documented to stimulate pathways that induce osteogenesis, decrease inflammation and promote angiogenesis.

Icariin has been shown in vivo to induce mice bone formation through upregulating runt-related transcription factor 2 (Runx2) genes and increasing bone morphogenic protein expression. These prompt osteogenic differentiation and bone development. Also, icariin invokes marrow stromal cell proliferation via increased alkaline phosphatase activity.

In vitro, icariin has been used to induce apoptosis by generating reactive oxygen species (ROS) and stimulating c-Jun N-terminal kinase (JNK) activity. Both of these apoptosis inducing processes compromise mitochondrial membranes to release cytochrome c. The generation of ROS causes direct damage to the membrane while JNK prompts downstream molecules to form pores in mitochondrial membranes.

Icariin has also been shown to inhibit nuclear factor-κB (NF-κB) expression, decreasing cytokine production. Additionally, icariin innervates phosphoinositide 3-kinase/protein kinase B (PI3K/AKT) cell cycle pathways. The PI3K/AKT pathway has been demonstrated in vitro to induce angiogenesis, following the addition of icariin.

Icaritin is a prenylflavonoid derivative of icariin (Goldbio # I-215) and has been used for oncology research, to influence bone formation and displays neuroprotective effects. Applications in oncology and neurology research have been related to the activity of icaritin on estrogen receptors.

Within the field of cancer research, icaritin has been shown to act as an agonist and antagonist on estrogen receptors in vivo which was based upon concentration in different cancer lines. Icaritin was shown in vitro to sustain extracellular signal–regulated kinase (ERK) activity through stimulating estrogen receptors. Prolonged ERK activation arrested the cell cycle in the G2 stage and subsequently triggered apoptosis. Anti-cancer activity of icaritin has also been observed to occur in estrogen receptor negative cancer cells, showing an estrogen receptor independent pathway.

For Alzheimer’s research, icaritin has been investigated for attenuating cytotoxic effects caused by β-Amyloid proteins. While the mechanism for neuroprotection has not been elucidated, icaritin was shown to possibly exert these effects through mitogen-protein kinase (MAPK)/ERK cell signaling pathways.

Icaritin exerts an osteogenic effect in vivo by forming a bioactive scaffold that promotes bone growth while also increasing alkaline phosphatase (ALP) activity. It is also used to inhibit osteoclast differentiation and activity through suppression of receptor activator of nuclear factor kappa-B ligand (RANKL).

Icotinib hydrochloride or icotinib HCl, is a first generation inhibitor of tyrosine kinase epidermal growth factor receptor (EGFR-TK). It has been used in measuring the efficacy of novel anti-cancer compounds in vivo against non-small-cell lung cancers that formed advanced solid tumors. Icotinib reversibly inhibits EGFR-TK competitively by blocking the ATP-binding site on tyrosine kinase.

Idebenone is a synthetic analog of ubiquinone (CoQ10). It scavenges free radicals and acts as an antioxidant. Idebenone differs from ubiquinone by having a shorter, less lipophilic tail and thus can function in multiple cellular environments. In contrast to ubiquinone, idebenone acts as a competitive inhibitor of complex I in the electron transport chain and is capable of facilitating cellular respiration that is independent of a functioning complex I. It can accept electrons from the glycerophosphate shuttle, NADH-quinone oxidoreductase, and complex II of the electron transport chain. Idebenone was originally developed to treat cognitive disorders such as Alzheimer’s disease, but was not found to be effective so other uses are being explored.

Interferon alpha1 belongs to the type I interferon family and is encoded by the IFNA1 gene in humans. It is expressed in peripheral blood leukocytes and lymphoblastoid cells. It plays an important role in inducing non-specific resistance against a broad range of viral infections, and also affects cell proliferation and modulates immune responses. Interferon alpha proteins represent a group of related but distinct proteins that share over 95 % amino acid sequence homology. IFNA1 contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity. IFNalpha1A differs from IFNalpha1B by having one alanine residue in a position where IFNalpha1B has a valine.

Interferon alpha1 belongs to the type I interferon family and is encoded by the IFNA1 gene in humans. It is expressed in peripheral blood leukocytes and lymphoblastoid cells. It plays an important role in inducing non-specific resistance against a broad range of viral infections. It also affects cell proliferation and modulates immune responses. Interferon alpha proteins represent a group of related but distinct proteins that share over 95 % amino acid sequence homology. IFNA1 contains four highly conserved cysteine residues which form two disulfide bonds, one of which is necessary for biological activity. IFNalpha1B differs from IFNalpha1A by having one valine residue in a position where IFNalpha1A has an alanine.

Interferon alpha2 belongs to the type I interferon family and is encoded by the IFNA2 gene in humans. Like the other IFN-alpha proteins, it is expressed in leukocytes and plays an important role in inducing non-specific resistance against a broad range of viral infections. Recombinant IFN-alpha2A has been used to induce regression of corticosteroid-resistant hemangiomas in infancy. IFNA2 is one of 13 subtypes of interferon alpha found in humans, clustered on chromosome 9. It contains four highly conserved cysteine residues forming two disulfide bonds, one of which is necessary for biological activity.

Interferon alpha2 belongs to the type I interferon family and is encoded by the IFNA2 gene in humans. Like the other IFN-alpha proteins, it is expressed in leukocytes and plays an important role in inducing non-specific resistance against a broad range of viral infections. Studies have shown the ability of recombinant IFN-alpha2B to decrease hepatic metastases from intraocular melanoma. It used to treat high-risk cutaneous melanomas, but is associated with many contraindications. IFNA2 is one of 13 subtypes of interferon alpha found in humans, clustered on chromosome 9. It contains four highly conserved cysteine residues forming two disulfide bonds, one of which is necessary for biological activity.

Interferon alpha2 belongs to the type I interferon family and is encoded by the IFNA2 gene in humans. Like the other IFN-alpha proteins, it is expressed in leukocytes and plays an important role in inducing non-specific resistance against a broad range of viral infections. Studies have shown the ability of recombinant IFN-alpha2B to decrease hepatic metastases from intraocular melanoma. It used to treat high-risk cutaneous melanomas, but is associated with many contraindications. IFNA2 is one of 13 subtypes of interferon alpha found in humans, clustered on chromosome 9. It contains four highly conserved cysteine residues forming two disulfide bonds, one of which is necessary for biological activity.

Interferon gamma is the only type II interferon and binds to the heterodimeric IFNGR that consists of two chains, IFNGR1 and IFNGR2. This interaction activates the JAK-STAT pathway. IFNG is produced primarily by T-lymphocytes and natural killer (NK) cells. It is critical for innate and adaptive immunity against viral and intracellular bacterial infections. This is due partly to its ability to inhibit viral replication directly, but also due to its immunostimulatory and immunomodulatory effects. IFNG induces the production of cytokines and upregulates the expression of class I and II MHC antigens, Fc receptors, and leukocyte adhesion molecules. It modulates macrophage effector functions, influences isotype switching, and potentiates the secretion of immunoglobulins by B cells. Additionally, IFNG augments TH1 cell expansion and may be required for TH1 cell differentiation.

Interferon gamma is the only type II interferon and binds to the heterodimeric IFNGR that consists of two chains, IFNGR1 and IFNGR2. This interaction activates the JAK-STAT pathway. IFNG is produced primarily by T-lymphocytes and natural killer (NK) cells. It is critical for innate and adaptive immunity against viral and intracellular bacterial infections. This is due partly to its ability to inhibit viral replication directly, but also due to its immunostimulatory and immunomodulatory effects. IFNG induces the production of cytokines and upregulates the expression of class I and II MHC antigens, Fc receptors, and leukocyte adhesion molecules. It modulates macrophage effector functions, influences isotype switching, and potentiates the secretion of immunoglobulins by B cells. Additionally, IFNG augments TH1 cell expansion and may be required for TH1 cell differentiation.

Interferon gamma is the only type II interferon found in humans and binds to the heterodimeric IFNGR that consists of two chains, IFNGR1 and IFNGR2. This interaction activates the JAK-STAT pathway. IFNG is produced primarily by T-lymphocytes and natural killer (NK) cells. It is critical for innate and adaptive immunity against viral and intracellular bacterial infections. This is partly due to its ability to inhibit viral replication directly, but also due to its immunostimulatory and immunomodulatory effects. IFNG induces the production of cytokines and upregulates the expression of class I and II MHC antigens, Fc receptors, and leukocyte adhesion molecules. It modulates macrophage effector functions, influences isotype switching, and potentiates the secretion of immunoglobulins by B cells. Additionally, IFNG augments TH1 cell expansion and may be required for TH1 cell differentiation.