Disease relevance of Pros1

• The coronavirus spike protein S is responsible for important biological activities including virus neutralization by antibody, cell attachment, and cell fusion [1].
• Coronavirus-induced encephalomyelitis: balance between protection and immune pathology depends on the immunization schedule with spike protein S [2].
• The findings in this study are the first to indicate a new biological activity of Gas6 and protein S as a direct regulator of osteoclastic function; they give an insight into the role of these vitamin K-dependent ligands in bone resorption in vivo [3].

High impact information on Pros1

• In contrast to the other vitamin K-dependent plasma proteins, the carboxyl-terminal part of protein S is not homologous to the serine proteases [4].
• Protein S consists of 634 amino acids in a single polypeptide chain and has one asparagine-linked carbohydrate side chain [4].
• However, the surface protein S of both viruses was retained in the endoplasmic reticulum at the nonpermissive temperature [5].
• More specifically, considerable amounts of PS mRNA and antigen were expressed in a cultured mouse cardiomyocyte cell line, and again, treatment with IL-1 decreased the PS expression in these cells [6].
• We further investigated the effects of lipopolysaccharide (LPS), tumor necrosis factor-alpha (TNF-alpha), and interleukin-1 (IL-1) on the PS mRNA expression in murine tissues in vivo [6].

Biological context of Pros1

• The amino acid sequence of mouse protein S is about 80% identical to that of other species [7].
• A cDNA clone encoding the vitamin K-dependent protein S was isolated from a murine liver cDNA library [8].
• We report here that recombinant rat PS is able to stimulate OS phagocytosis, and similar to Gas6, it does so through a Mer-dependent mechanism [9].
• Protein S (PS) is a vitamin K-dependent serum protein with a high degree of structural similarity to Gas6, and a well characterized role in blood coagulation [9].
• TNF as a mediator of cardiac transplant rejection, including effects on the intragraft protein C/protein S/thrombomodulin pathway [10].

Anatomical context of Pros1

• Cross-linking of protein S bound to lymphocytes promotes aggregation and inhibits proliferation [11].
• Here, using a flow cytometric assay, we demonstrate that protein S binds to the surface of B and T lymphocytes [11].
• Gas6 and protein S directly enhanced the bone resorbing activity of mature osteoclasts [3].

Associations of Pros1 with chemical compounds

• The mouse protein S contains two potential N-glycosylation sites at positions #458 and 468 and is lacking the putative glycosylation site at #490 found in human protein S [7].
• Gas6 and protein S are dependent on vitamin K, a cofactor for the enzyme responsible for carboxylation of glutamic acid residues [3].

Analytical, diagnostic and therapeutic context of Pros1

• Structure of mouse protein S as determined by PCR amplification and DNA sequencing of cDNA [7].

References