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Noggin binds to and antagonizes bone morphogenetic protein (BMP) ligands of the transforming growth factor beta (TGF-β) family. Noggin supports maintenance of undifferentiated human embryonic stem cells in vitro, and can be used to prevent spontaneous differentiation in the short term (Chaturvedi et al.). Noggin is essential for development of structures derived from ectoderm embryonic somite, skeletal patterning, and neurogenesis in vivo. It also influences chondrogenesis, osteogenesis, and joint formation (Krause et al.), and promotes dopaminergic differentiation of embryonic stem cells and subsequent survival of dopamine neurons (Chiba et al.).

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Epidermal growth factor (EGF) is characterized by high affinity binding to various EGF receptors (EGFRs) and the production of mitogenic responses (Carpenter and Cohen). EGF promotes EGFR dimerization, resulting in activation of downstream pathways including PI3K, ERK1/2, JAK/STAT, β-catenin, and calcium signaling. EGF is secreted by the gut-associated salivary and Brunner’s glands, is found in a variety of body fluids, and stimulates cell proliferation and differentiation in rodent and neonatal human intestine (Wright et al.). Central nervous system stem cells also proliferate in response to the EGF stimulus (Reynolds and Weiss).

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SARS-CoV-2 Recombinant Spike Protein, aa16-685 is expressed in HEK293 cells and is one of four structural proteins encoded by the SARS-CoV-2 genome. The Spike Protein plays a key role in attachment to host cells, allowing invasion through clathrin-mediated endocytosis. The Spike Protein can be cleaved by host cell proteases after aa685 to yield the N-terminal S1 subunit and C-terminal S2 region. The S1 subunit is responsible for interacting with the host cell receptor (angiotensin-converting enzyme II) through a receptor-binding domain that is highly conserved with SARS-CoV. The S1 subunit has two conformations: a ‘down’ conformation in which the receptor is inaccessible, and an ‘up’ conformation in which the receptor is accessible. These conformational changes are key for monoclonal antibody drugs and vaccine development. SARS-CoV-2 Recombinant Spike Protein contains a polyhistidine tag at the amino terminus; it also contains a FLAG tag at the carboxy terminus.

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Vascular endothelial growth factor (VEGF-121) is a naturally-occurring VEGF-A splice variant involved in embryonic vasculogenesis and angiogenesis. VEGF binds to VEGFR-1 and VEGFR-2, and activates Raf/MEK/ERK and PI3K/AKT pathways. VEGF-121 is released as a freely diffusible protein by a variety of normal and transformed cells. It plays an important role in neurogenesis both in vitro and in vivo (Storkebaum et al.). It has neurotrophic effects on neurons of the central nervous system and promotes growth and survival of dopaminergic neurons and astrocytes. VEGF also promotes growth and survival of vascular endothelial cells, monocyte chemotaxis, and colony formation by granulocyte-macrophage progenitor cells (Ferrara et al.).

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Amphiregulin is a member of the epidermal growth factor (EGF) family. It binds to several receptors including EGFR/ErbB1, HER2/ErbB2, HER3/ErbB3, and HER4/ErbB4, which activates Ras/Raf/MAPK and PI3K/AKT pathways. This results in cell proliferation, apoptosis resistance, and invasive behaviour (Normanno et al.). The expression of amphiregulin is induced by tissue injury and inflammation. Amphiregulin promotes mammary development, trophoblast growth, lung and kidney branching morphogenesis, and keratinocyte proliferation. It stimulates the growth of most cell types, including normal and transformed mammary epithelial cells, and malignant cells of the colon, prostate, cervix, and pancreas (Berasain and Avila).

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Insulin-like growth factor 1 (IGF-I) is a polypeptide that belongs to the family of insulin-like growth factors that are similar in molecular structure to proinsulin. IGF-I binds to the IGF-I receptor and is a potent activator of the PI3K/AKT pathway and also activates ERK1/2 signaling. IGF-I is required for embryonic development, and it is produced mainly in the liver in response to a hepatocyte growth hormone. In the absence of insulin, IGF-I is necessary for the maintenance of human pluripotent stem cells (Wang et al.). Together with IL-3, IGF-I stimulates differentiation and proliferation of myeloid cells and has been shown to regulate lymphopoiesis by stimulating proliferation and differentiation of T and B cells in lymphoid organs (Heemskerk et al.).

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TRAIL (TNF-related apoptosis-inducing ligand) belongs to the tumor necrosis factor (TNF) superfamily and is associated with initiating apoptosis. TRAIL has four major receptors: two death receptors DR4 and DR5, and two decoy receptors DcR1 and DcR2. TRAIL binds to the death receptors, which recruits the Fas-associated death domain (FADD) and activates caspases 8 and 10, which eventually leads to apoptosis (Pitti et al.; Wiley et al.; Zauli and Secchiero). It has been shown that mice lacking the expression of TRAIL have defects in thymocyte apoptosis and negative selection, and these mice had increased susceptibility to autoimmune diseases (Lamhamedi-Cherradi et al.).

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GRO (growth-regulated oncogene)-beta or CXCL2 is a member of the CXC family, which plays an integral role in recruitment and activation of neutrophils and basophils in response to tissue injury and microbial infection. GRO-beta and GRO-gamma are closely related to GRO-alpha and share 90% and 86% amino acid sequence homology, respectively, with GRO-alpha. Receptor-binding studies have demonstrated that GRO-alpha, -beta, and -gamma signal mainly through G protein-coupled receptors CXCR1 and CXCR2 (Ahuja and Murphy). GRO-beta is expressed in epithelial cells, monocytes, fibroblasts, and melanocytes and is further induced during inflammatory, epithelialization, and angiogenic processes, for example during the wound healing process of human burn wounds (Zaja-Milatovic and Richmond). GRO-beta also stimulates mitogenesis in certain human melanoma cells (Unemori et al.).

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Receptor activator of nuclear factor kappa-B ligand (RANKL) is a member of the tumor necrosis factor (TNF) superfamily (Anderson et al.). Cytokines in the TNF superfamily are involved in a variety of long-term cellular activities such as differentiation, proliferation, and cell death (MacEwan). RANKL is a type II homotrimeric transmembrane protein expressed in both a membrane-bound and secreted form (Ikeda et al.). RANKL binds to the receptor activator of nuclear factor kappa-B (RANK). Upon binding to its receptor, RANKL activates the AKT signaling pathway (Moon et al.). Osteoprotegerin (OPG) may also bind RANKL, and this binding competes with RANKL-RANK binding (Lacey et al.). RANKL is involved in osteoclastogenesis (Lacey et al.; Yasuda et al.) and T cell activation (Wong et al.).

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Use angiopoietin-like protein 2 (ANGPTL2) to regulate tissue remodeling through integrin α5β signaling and activation of p38 mitogen-activated protein kinases (MAPK) (Odagiri et al.; Tabata et al.). Highly expressed in the heart, small intestine, and stomach, ANGPTL2 is a glycosylated secretory protein that contains a coiled domain and a fibrinogen-like domain (Kim et al.). Studies have shown that the coiled-coil domain of ANGPTL2 functions as a growth factor, enhancing the survival of hematopoietic stem cells (HSCs) ex vivo (Broxmeyer et al.). ANGPTL2 is also known to play a role in obesity and metabolic diseases, promoting local inflammation in adipose tissue and systemic insulin resistance in mice models (Tabata et al.). By activating an inflammatory cascade in endothelial cells and increasing macrophage infiltration, ANGPTL2 accelerates vascular inflammation which may lead to endothelial dysfunction and atherosclerosis progression (Horio et al.). This protein product contains a His-residue tag at the amino end of the polypeptide chain. For consistency and reproducibility across your applications, sclerostin from STEMCELL comes lyophilised with ≥92% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

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Fibroblast growth factor 18 (FGF-18) is a growth factor and member of the FGF subfamily. FGF-18 is most similar to FGF-8 and FGF-17, and is secreted in adult lung and developing tissues (Ohbayashi et al.). FGF-18 signals through FGF receptor 3 (FGFR3) to regulate proliferation, differentiation, and matrix production of articular and growth plate chondrocytes in vivo and in vitro (Davidson et al.). FGF-18 has skeletal functions and protects articular cartilage by gene expression profiling and regulates proliferation and differentiation of midline cerebellar structures (Mori et al.). Also, recombinant human FGF-18 has been shown to effectively regulate hair growth (Song et al.).

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Tumor necrosis factor-α (TNF-α) is a pro-inflammatory cytokine that activates NF-κB, MAPK, and PI3K/AKT pathways. Activated T cells and macrophages are the primary producers of TNF-α in response to inflammation and infectious conditions. Many other cell types have been shown to produce TNF-α, among them B cells, NK cells, mast cells, neutrophils, dendritic cells, microglia, endothelial cells, smooth muscle cells, cardiomyocytes, and fibroblasts. TNF-α has cytotoxic effects on cancer cells in vitro by stimulating anti-tumor immunosuppressive responses. TNF-α stimulates expression of E- and P-selectins, thus facilitating adhesion of neutrophils, monocytes, and memory T cells to activated platelets and endothelial cells (Zelová andamp; Hosek). Other effects of TNF-α include vasodilatation and edema formation.

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Commonly known as vaspin, Serpin A12 is an adipokine that is thought to perform insulin-sensitizing functions, such as the regulation of kallikrein 7 (KLK7), an insulin-inhibiting protease (Heiker et al.). The Serpin A12 glycoprotein belongs to the serine protease inhibitor family (serpin), and is mainly associated with obesity, insulin resistance, and glucose metabolism, but may also protect against high fat-induced bone loss (Wang et al.). Serpins share a highly conserved core structure with multiple α-helices, β-strands, and a reactive site loop (RCL) to interact with the target protease (Huntington). It is expressed predominantly in visceral adipose tissue and at significantly higher amounts in obese individuals (Kurowska et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, Serpin A12 from STEMCELL comes lyophilised with ≥94% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤1,0 EU/μg protein.

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Interleukin 33 (IL-33) is a pro-inflammatory cytokine from the IL-1 family. It binds to ST2 receptor and activates NF-κB and MAPK pathways. IL-33 is expressed by epithelial cells, smooth muscle cells, and fibroblasts in various tissues and organs, as well as resting basophils, mast cells, eosinophils, natural helper cells, group 2 innate lymphoid cells, dendritic cells, and activated macrophages (Schmitz et al.; Yasuda et al.). It contributes to allergic inflammation by stimulating production of the cytokines IL-4, IL-5, and IL-13, and stimulates host defense against microbial and viral infections (Liew; Yasuda et al.). In the central nervous system, IL-33 is produced by endothelial cells and astrocytes. It induces proliferation of microglia and mediates production of pro-inflammatory cytokines (Yasuoka et al.).

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Interleukin 12 (IL-12p70) is a heterodimeric cytokine composed of p35 and p40 subunits. IL-12 is produced by monocytes, macrophages, dendritic cells, neutrophils, and B cells in response to bacterial products and cytokines such as IFN-γ. The IL-12 receptor is expressed on T, NK, and dendritic cells. Upon binding, IL-12 initiates signaling via the JAK/STAT signaling pathway and stimulates NK, B, and T cells to produce IFN-γ (Watford et al.). It also regulates cytokine synthesis, proliferation of T and NK cells, and stimulates differentiation of CD4+ and CD8+ T cells (Germann and Rüde). Mice that are deficient in IL-12 are susceptible to many intracellular pathogens and have impaired IFN-γ secretion, Th1 differentiation, and NK cytolytic activity; however, Th2 development and IL-4 production are enhanced (Watford et al.).

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Fibroblast growth factor 16 (FGF-16) is a heparin-binding member of the FGF family. FGFs possess broad mitogenic and cell survival activities and are expressed during embryonic development. FGFs act primarily on cells of mesodermal and neuroectodermal origin to regulate diverse physiological functions including angiogenesis, cell growth, pattern formation, embryonic development, metabolic regulation, cell migration, and tissue repair (Goldfarb; Green et al.). In vitro, FGF-16 has been shown to promote the proliferation of brown adipocytes and in rat embryos it is predominantly expressed in these cells. FGF-16 has also been shown to play a critical role in embryonic heart development and is thought to play a cardioprotective role after birth (Hotta et al.; Lu et al.; Wang et al.).

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Use resistin to modulate various cellular responses, such as promoting neutrophil extracellular trap (NET) formation (Jiang et al.) and regulating anti-inflammatory signaling pathways through toll-like receptor 4 (TLR4) (Jang et al., 2017). A member of the resistin-like molecule (RELM) family, resistin is produced by adipocytes in mice, and has been implicated in insulin resistance, reducing glucose tolerance, and insulin sensitivity in vivo (Li et al.). In humans, resistin is expressed predominantly in leukocytes, modulating inflammation in numerous diseases (Jamaluddin et al.; Jang et al., 2015; Mantula et al.). Studies also show that resistin facilitates vascular endothelial growth factor (VEGF)-A-dependent angiogenesis in human chondrosarcoma cells, highlighting it as a promising target for chondrosarcoma angiogenesis (Chen et al.). For consistency and reproducibility across your applications, resistin from STEMCELL comes lyophilised with ≥95% purity, and endotoxin levels are verified to be ≤1,0 EU/μg protein.

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Interleukin 9 (IL-9) has pleiotropic functions in the immune system and signals through its specific IL-9 receptor (IL-9R) (Renauld et al.). IL-9/IL-9R signaling pathway mainly targets the downstream activation of JAK/STAT (janus kinase/signal transducer and activator of transcription) and subsequent phosphorylation cascades initiated by multiple kinases including IRS–PI3K–PKB (insulin receptor substrate, phosphatidyl-inositol 3-kinases, protein kinase-B) and ERK (Knoops and Renauld; Fontaine et al.). IL-9 has been shown to have a role in Th1/Th17-mediated inflammation and in regulatory T cell responses (Singh et al.; Goswami and Kaplan). IL-9/IL-9R signaling pathway represents a novel endogenous anti-apoptotic mechanism for cortical neurons (Fontaine et al.). IL-9 secreting T cells, termed Th9 cells, contribute to both effective immunity and immunopathological disease, and have been shown to have a role in the treatment of allergic and autoimmune disease (Kaplan et al.).

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R-Spondin-1 (RSPO1) is the prototype member of the R-Spondin (RSPO) protein subfamily of a superfamily of thrombospondin type 1 repeat (TSR-1)-containing proteins (Chen et al.; Kamata et al.; Kazanskaya et al.; Kim et al.). Although unable to initialize signaling, RSPO family members are potent enhancers of WNT signaling (Cruciat and Niehrs; de Lau et al.; Kamata et al.; Kazanskaya et al.). They are characterized by a TSR-1 domain, a carboxy-terminal region with positively charged amino acids, and two N-terminal furin-like cysteine-rich repeats (Glinka et al.; Kazanskaya et al.). R­-Spondin-1 activates β­-catenin signaling via the WNT signaling cascade and by indirectly increasing low-density lipoprotein receptor-related protein 6 (LRP6) on the cell surface. It does this by binding leucine-rich repeat-containing G-protein-coupled receptor 5 (LGR5), and competing with WNT antagonist DKK­1 for binding to the WNT co­receptors, Kremen and LRP­6, which reduces DKK­1-­mediated internalization of LRP6 (Binnerts et al.). RSPO1 is involved in a wide range of pleiotropic roles during embryogenesis, it is required for the specification of hematopoietic stem cells, and it has been shown to be important in the growth, survival, and migration of ovarian cancer cells (Cruciat and Niehrs; de Lau et al.; Genthe and Clements; Liu et al.).

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RANTES (regulated upon activation, normal T cell expressed and secreted), also known as CCL5, is a member of the CC family of chemokines and is able to recruit leukocytes to sites of inflammation (Schall et al.). RANTES is secreted by T lymphocytes, macrophages, platelets, synovial fibroblasts, tubular epithelium, and certain types of tumor cells (Aldinucci and Colombatti; Soria and Ben-Baruch). This chemokine exerts its effect by interacting with the chemokine receptors CCR1, CCR3, CCR4, and CCR5. RANTES plays an active role in recruiting a variety of leukocytes into inflammatory sites, including T cells, macrophages, eosinophils, and basophils. In collaboration with certain cytokines that are released by T cells such as IL-2 and IFN-γ, RANTES also induces the activation and proliferation of NK cells to generate CC chemokine-activated killer cells, which are highly cytolytic (Lv et al.; Maghazachi et al.). It has been shown that RANTES produced by CD8+ T cells inhibits HIV infection of primary human peripheral blood mononuclear cells (Appay and Rowland-Jones; Cocchi et al.).

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Interleukin 13 (IL-13) is a cytokine important in type 2 immune responses and is expressed by T helper type 2 (Th2) cells and group 2 innate lymphoid cells (ILC2s) (Pulendran and Artis). IL-13 binds a receptor composed of IL-4Ra and IL-13Ra1 or IL-13Ra2 (Wynn 2003). IL-13 receptor is expressed on B cells and promotes B cell proliferation, induces class switching to IgG4 and IgE, and functions in the recruitment and activation of IgE-producing B cells (Hershey). The receptor is also expressed on basophils, eosinophils, mast cells, endothelial cells, fibroblasts, monocytes, macrophages, respiratory epithelial cells, and smooth muscle cells (Hershey). Signaling through the IL-13 receptor activates the JAK/STAT and IRS-1/IRS-2 pathways. in vivo, IL-13 has a role in resistance to extracellular helminth parasites by regulating gastrointestinal parasite expulsion, as well as in airway hyperresponsiveness, allergic inflammation, tissue remodeling, tumor cell growth, and fibrosis (Wynn 2015). Secreted IL-13 is a protein consisting of 112 amino acids with a molecular mass of 10 kDa (Hershey). Human IL-13 is not species-specific but has greater activity on human cells compared to mouse cells (Hershey).

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Leukemia inhibitory factor (LIF) is an interleukin 6 class cytokine that regulates a broad variety of developmental functions. After LIF binds to the LIF receptor (LIFR), LIFR associates with gp130 and activates JAK/STAT and MAPK signaling (Auernhammer and Melmed; Suman et al.). LIFR activation of STAT3 is essential for maintaining the mouse embryonic stem cell phenotype (Niwa et al.). Produced by the endometrium, LIF plays an important autocrine and paracrine role in implantation by regulating proliferation, invasion, and differentiation of trophoblasts following blastocyst attachment (Auernhammer and Melmed; Suman et al.). Human LIF can be used for the maintenance of mouse embryonic stem cells; however, mouse LIF cannot bind to the human receptor, thus rendering mouse LIF inactive (Dahéron et al.). LIF is produced by CD4+ and activated regulatory T cells, and promotes Foxp3 expression, while repressing Th17 lineage-specific genes (Metcalfe). LIF is also secreted by mesenchymal stromal cells, where it supports hematopoiesis and immune modulation (Nasef et al.).

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Stromal cell-derived factor 1 alpha (SDF-1α) is a member of the CXC group of chemokines that binds to the G-protein coupled receptor, CXCR4, to regulate migration, proliferation, differentiation, and survival of many cell types including hematopoietic stem cells, B cells, and T cells. It is produced by bone marrow stromal cells, osteoblasts, endothelial cells, and neuronal cells. SDF-1α was first identified as the pre-B-cell growth-stimulating factor (PBSF) in the mouse bone marrow-derived stromal cell line, PA6, in the growth of B cell precursors (Hayashi et al.). SDF-1α primarily regulates cell motility during development and adulthood, including the homing of hematopoietic stem cells and neutrophils to fetal bone marrow during ontogeny (Ara et al. 2003a) and the recruitment of endothelial progenitor cells from bone marrow during angiogenesis in adulthood (Zheng et al.). In addition to its role in hematopoiesis, the SDF-1α/CXCR4 signaling pathway is also essential for the homing of primordial germ cells to gonads (Ara et al. 2003b), the migration of granule cells in the cerebellum during neurogenesis (Zou et al.), and the migration of breast cancer cells to sites of metastasis (Muller et al.).

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Platelet-derived growth factor (PDGF) is a dimeric glycoprotein consisting of two disulfide bridge stabilized polypeptide chains, A and B, which are assembled as heterodimers (PDGF-AB) or homodimers (PDGF-AA and PDGF-BB) (Fretto et al.; Westermark and Heldin). PDGF signals through the receptor tyrosine kinases PDGFRalpha and PDGFRbeta. It has been shown that PDGF-induced migration involves signaling pathways involving MEK/ERK, EGFR, Src and PI3K/AKT (Kim et al.). PDGF is a potent mitogen for cells of mesenchymal origin- like fibroblasts, glial cells, and vascular smooth muscle cells. PDGF has been implicated in pathogenesis of atherosclerosis, glomerulonephritis, cancer, and in the contraction of vascular smooth muscle cells of rat aortic tissues (Fretto et al.; Sachinidis et al.). PDGF-BB is secreted by osteoblasts to induce mesenchymal stem cell migration and angiogenesis. It has also been shown that PDGF-BB is secreted by preosteoclasts during bone modeling and remodeling to induce angiogenesis and thus proper osteogenesis (Xie et al.).

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Betacellulin is a member of the epidermal growth factor (EGF) family, and signals through EGF receptor and ERBB4. It activates ERK and AKT pathways, which induces neural stem cell proliferation and prevents spontaneous differentiation in culture. Betacellulin stimulates the expansion of neural stem cells, transit-amplifying cells, and neuroblasts derived from subventricular zone and dentate gyrus (Gómez-Gaviro et al.). It is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. Betacellulin down-regulates E-cadherin expression in ovarian cancer cell lines via MEK/ERK1/2 and PI3K/AKT signaling pathways, thus increasing cell migration (Zhao et al.). It is a modulator of interferon (IFN) response and enhances anti-viral effects of IFN (Al-Yahya et al.). Betacellulin is expressed in pancreatic α cells, β cells, and duct cells. It induces the proliferation of pancreatic cancer cell lines, inhibits apoptosis, promotes the neogenesis of β cells, and converts non-β cells into insulin-producing cells (Kawaguchi et al.; Miyagawa al.; Saito et al.).

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Brain-derived neurotrophic factor (BDNF), like nerve growth factor (NGF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4), is a member of the NGF family of neurotrophins, which are required for the differentiation and survival of specific neuronal subpopulations in both the central and the peripheral nervous systems (Minichiello and Klein; Minichiello et al.). BDNF binds with high affinity to the tropomyosin receptor kinase B (TrkB), and activates AKT and ERK pathways (Mattson et al.). It is expressed in the hippocampus, cortex, and synapses of the basal forebrain. BDNF acts as a survival factor for human embryonic stem cells when plated on either feeder cells or Corning® Matrigel® (Pyle et al.). BDNF regulates synaptic transmission and plasticity at adult synapses in the central nervous system, and contributes to adaptive neuronal responses including long-term potentiation, long-term depression, certain forms of short-term synaptic plasticity, and homeostatic regulation of neuronal excitability (Reichardt). It also has a role in neurogenesis by promoting survival and growth of dorsal root ganglion cells, and hippocampal and cortical neurons (Binder and Scharfman). BDNF, together with glial cell line-derived neurotrophic factor (GDNF) and other supplements, is commonly used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Brafman).

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Glial cell line-derived neurotrophic factor (GDNF) is a neurotrophic factor and a member of the tumor growth factor (TGF)-beta superfamily. The GDNF family of growth factors also includes neurturin, persephin, and artemin, which have seven conserved cysteine residues called cysteine-knots (Treanor et al.). GDNF family ligands signal through binding to specific GDNF-family receptor-α (GFRα) co-receptors and activate the RET receptor tyrosine kinase (Durbec et al.). Four different forms of GFRα co-receptors have been characterized (GFRα 1-4); GDNF binds specifically to GFRα1 prior to forming a complex with RET (Airaksinen and Saarma). GDNF is known to promote survival and morphological differentiation of midbrain dopaminergic neurons in both in vivo and in vitro studies and increases their high-affinity dopamine uptake (Granholm et al.; Lin et al.). GDNF has also been shown to have restorative effects on dying dopaminergic neurons in response to degenerative toxins (Aoi et al.). GDNF, together with Human Recombinant BDNF (brain-derived neurotrophic factor), BrainPhys™ Neuronal Medium, and other supplements, can be used to differentiate human pluripotent stem cell (hPSC)-derived neural progenitor cells into neurons (Bardy et al.).

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Macrophage colony-stimulating factor (M-CSF) is a homodimeric glycoprotein growth factor that regulates proliferation and differentiation of myeloid hematopoietic progenitor cells to mononuclear phagocytic cell lineages, including monocytes, macrophages, and osteoclasts. M-CSF is a crucial factor for the development of tissue-resident macrophages in most tissues (Ginhoux and Jung). It is required for the maturation and activation of monocytes and macrophages, and regulates inflammatory responses in conjunction with other stimuli such as IFN-γ, LPS, and IL-4 (Murray et al.). M-CSF is also required for bone resorption by osteoclasts, and is involved in the development and regulation of the placenta, mammary gland, and brain. M-CSF is produced by monocytes, fibroblasts, osteoclasts, stromal cells, endothelial cells, and tumor cells (Chockalingam and Ghosh). M-CSF exerts its biological effects by signaling through a receptor tyrosine kinase (CSF-1R or M-CSF-R) encoded by the c-fms proto-oncogene (Hamilton). CSF-1R shares similar structural features with other growth factor receptors, including the stem cell factor (SCF) receptor, platelet-derived growth factor receptor (PDGF-R), and Flt3/Flk-2 receptor tyrosine kinase. Stimulation of the CSF-1R upon binding to M-CSF activates MAPK, PI3K, and PLCγ signaling pathways (Chockalingam and Ghosh). Human and mouse M-CSF sequences are highly conserved both at nucleotide and amino acid levels (80% homology; DeLamarter et al.).

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Interleukin 17A (IL-17A) is the founding member of the family of cytokines that includes Interleukin 17B through Interleukin 17F. It is a potent proinflammatory cytokine that plays a key role in defense against pathogens. IL-17A and IL-17F signal as homodimers or heterodimers through the same receptor, and activate NF-kB, MAPK, and C/EBP pathways (Gaffen). IL-17A receptor is expressed on a variety of cell types, including hematopoietic cell compartments. IL-17A is produced by T helper 17 cells, CD8+ T cells, γδ T cells, natural killer T cells, B cells, neutrophils, innate lymphoid cells and mesenchymal stromal cells (MSCs; Zenobia and amp; Hajishengallis; Mojsilovic et al.). IL-17A receptor is expressed at particularly high levels on stromal cells, including MSCs. IL-17A increases the frequency and the average size of colony-forming units-fibroblast derived from bone marrow, as well as the proliferation of bone marrow-derived MSCs. IL-17A suppresses osteogenic differentiation and bone formation of bone marrow-derived MSCs. The action of IL-17A on hematopoiesis is deeply reliant on the microenvironment and the induction of other regulators. In healthy mouse bone marrow, IL-17A stimulates myeloid and early stage erythroid progenitor cells but inhibits late stage erythroid progenitor cells (Mojsilovic et al.).

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GPBB