Protein Delta Homolog 1 (DLK-1) is a transmembrane protein which contains a signal peptide, an extracellular domain with six tandem epidermai growth factor (EGF)-like domains, a single pass transmembrane domain, and a short cytoplasmic tail. It is found within the stromal cells in close contact to the vascular structure of placental villi, yolk sac, fetal liver, adrenal cortex and pancreas and in the beta cells of the islets of Langerhans in the adult pancreas. In addition, it is detected in some forms of neuroendocrine lung tumor tissue. DLK-1 may have a improtant role in neuroendocrine differentiation.
Proteoglycan 3, also known as Eosinophil major basic protein homolog, Prepro-major basic protein homolog, PRG3 and MBPH, contains one C-type lectin domain. Proteoglycans are a major component of the animal extracellular matrix. PRG3 localizes to the eosinophil secondary granule and is expressed in bone marrow, not detected in placenta. PRG3 has similar cytotoxic and cytostimulatory activities to PRG2/MBP. In vitro, PRG3 can stimulate neutrophil superoxide production and IL8 release, histamine and leukotriene C4 release from basophils.
Protocadherin-10 (PCDH10) is a single-pass type I membrane protein that contains six extracellular cadherin domains; one transmembrane domain and one cytoplasmic tail differing from those of the classical cadherins. As a potential calcium-dependent cell-adhesion neuronal receptor; it may plays a role in the establishment and function of specific cell-cell connections in the brain. PCDH10 moderately expressed in all regions of the brain examined; as well as in testis and ovary; and low expression in all other tested tissues.
Protocadherin-1, also known as Cadherin-like protein 1, Protocadherin-42 and PCDH1, belongs to the protocadherin subfamily within the cadherin superfamily. PCDH1 contains seven cadherin-like domains, a transmembrane region and a C-terminal cytoplasmic region. PCDH1 can be detected as early as embryonic day 9.5. In early embryogenesis, expression is especially prominent in blood vessels. The tight spatial and temporal regulation of Pcdh1 expression suggests that this protocadherin plays multiple roles not only during development but also in mature tissues and organs. In addition, protocadherin-1 is involved in cell-cell interaction processes and in neural cell adhesion.
Ribose-Phosphate Pyrophosphokinase 2 (PRPS2) is a phosphoribosyl pyrophosphate synthetase that belongs to the ribose-phosphate pyrophosphokinase family. PRPS2 is a homodimer. The active form is probably an hexamer composed of three homodimers. PRPS2 catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. PRPS2 catalyzes the synthesis of 5-phosphoribosyl 1-pyrophosphate from ATP and D-ribose 5-phosphate. In addition, PRPS2 plays a central role in the synthesis of purines and pyrimidines.
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