Cryptic (CFC1) is a member of the epidermal growth factor (EGF)- Cripto, Frl-1, and Cryptic (CFC) family. It contains an EGF-like domain, and is glycosylated on its N-terminal during post-translational modification. Cryptic is identified as a NODAL coreceptor involved in the correct establishment of the left-right axis. It may play a role in mesoderm and/or neural patterning during gastrulation. The unnormal expression of this gene may causes a series of diseases such as HTX2, Transposition of the great arteries dextro-looped 2, and Conotruncal heart malformations.
SIGLEC5 contains 2 Ig-like C2-type (immunoglobulin-like) domains and 1 Ig-like V-type (immunoglobulin-like) domain. It belongs to the immunoglobulin superfamily and SIGLEC (sialic acid binding Ig-like lectin) family. SIGLEC5 is expressed by monocytic/myeloid lineage cells. It is found at high levels in peripheral blood leukocytes, spleen, bone marrow and at lower levels in lymph node, lung, appendix, placenta, pancreas and thymus. It is also expressed by monocytes and neutrophils but absent from leukemic cell lines representing early stages of myelomonocytic differentiation. SIGLEC5 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
M-CSFR encoded by the proto-oncogene c-fms is the receptor for colony stimulating factor 1 (CSF1R), a cytokine involved in the proliferation, differentiation, and activation of macrophages. This cell surface glycoprotein is consisted by an extracellular ligand-binding domain, a single membrane-spanning segment, and an intracellular tyrosine kinase domain. Binding of CSF1 activates the receptor kinase, leading to "autophosphorylation" of receptor subunits and the concomitant phosphorylation of a series of cellular proteins on tyrosine residues. CSF1R is a tyrosine kinase receptor that is absolutely required for macrophage differentiation and thus occupies a central role in hematopoiesis. CSF1 and its receptor (CSF1R, product of c-fms proto-oncogene) were initially implicated as essential for normal monocyte development as well as for trophoblastic implantation. This apparent role for CSF1/CSF1R in normal mammary gland development is very intriguing because this receptor/ligand pair has also been found to be important in the biology of breast cancer in which abnormal expression of CSF1 and its receptor correlates with tumor cell invasiveness and adverse clinical prognosis. Tumor cell expression of CSF1R is under the control of several steroid hormones (glucocorticoids and progestins) and the binding of several bHLH transcription factors, while tumor cell expression of CSF-1 appears to be regulated by other hormones, some of which are involved in normal lactogenic differentiation.
Macrophage colony-stimulating factor 1 receptor (CSF1R) is a member of the type III subfamily of receptor tyrosine kinases that also includes receptors for SCF and PDGF. These receptors each contain five immunoglobulin-like domains in their extracellular domain (ECD) and a split kinase domain in their intracellular region. CSF1R is expressed primarily on cells of the monocyte/macrophage lineage; dendritic cells; stem cells and in the developing placenta. CSF1 and its receptor (CSF1R; product of c-fms proto-oncogene) were initially implicated as essential for normal monocyte development as well as for trophoblastic implantation. It plays an important role in the regulation of osteoclast proliferation and differentiation; the regulation of bone resorption; and is required for normal bone and tooth development. It is required for normal male and female fertility; and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases; such as rheumatoid arthritis; glomerulonephritis; atherosclerosis; and allograft rejection.
Macrophage colony-stimulating factor 1 receptor (CSF1R) is a member of the type III subfamily of receptor tyrosine kinases that also includes receptors for SCF and PDGF. These receptors each contain five immunoglobulin-like domains in their extracellular domain (ECD) and a split kinase domain in their intracellular region. CSF1R is expressed primarily on cells of the monocyte/macrophage lineage, dendritic cells, stem cells and in the developing placenta. CSF1 and its receptor (CSF1R, product of c-fms proto-oncogene) were initially implicated as essential for normal monocyte development as well as for trophoblastic implantation. It plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. It is required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Aberrant expression of CSF1 or CSF1R may play a role in inflammatory diseases, such as rheumatoid arthritis, glomerulonephritis, atherosclerosis, and allograft rejection.
Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
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