Hepassocin, also known as hepatocyte-derived fibrinogen-related protein 1 (HFREP-1), is a liver-specific secreted protein belonging to the fibronogen superfamily, whose members share a fibrinogen domain at their C-termini. It is secreted by the liver and functions as a mitogen for hepatocytes. Hepassocin may play a role in the development of hepatocellular carcinomas. Hepassocin is a disulfide-linked homodimeric protein with a C-terminal fibrinogen domain. It is reported that it is a major immune inhibitory ligand of LAG-3.
Hepassocin; also known as hepatocyte-derived fibrinogen-related protein 1 (HFREP-1); is a liver-specific secreted protein belonging to the fibronogen superfamily; whose members share a fibrinogen domain at their C-termini. It is secreted by the liver and functions as a mitogen for hepatocytes. Hepassocin may play a role in the development of hepatocellular carcinomas. Hepassocin is a disulfide-linked homodimeric protein with a C-terminal fibrinogen domain. It is reported that it is a major immune inhibitory ligand of LAG-3 .
Acidic Fibroblast Growth Factor Intracellular-Binding Protein (FIBP) is highly expressed in the heart, skeletal muscle, and pancreas. Acidic Fibroblast Growth Factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FIBP is an intracellular protein that binds selectively to acidic fibroblast growth factor (aFGF). It is postulated that FIBP may be involved in the mitogenic action of aFGF.
Asprosin is a protein hormone that is produced by white adipose tissue in mammals (and potentially by other tissues), which is then transported to the liver and stimulates it to release glucose into the blood stream. In the liver asprosin activates rapid glucose release by a cAMP-dependent pathway. The glucose release by the liver into the blood stream is vital for brain function and survival during fasting. People with neonatal progeroid syndrome lack asprosin, while people with insulin resistance have it in abundance. In animal tests asprosin showed potential for treating type 2 diabetes. When antibodies targeting asprosin were injected into diabetic mice, blood glucose and insulin levels improved.
Seprase, also known as 17 KD melanoma membrane-bound gelatinase , Fibroblast activation protein alpha, Integral membrane serine protease and FAP, is a single-pass type II membrane protein which belongs to thepeptidase S9B family. Seprase / FAP is found in cell surface lamellipodia, invadopodia and on shed vesicles. Seprase / FAP appears to act as a proteolytically active 17-KD dimer, consisting of two 97-KD subunits. It is a member of the group type II integral serine proteases, which includes dipeptidyl peptidase IV ( DPPIV / CD26 ) and related type II transmembrane prolyl serine peptidases, which exert their mechanisms of action on the cell surface. Seprase / FAP colocalized with DPP4 in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Seprase / FAP colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. DPP4 and seprase exhibit multiple functions due to their abilities to form complexes with each other and to interact with other membrane-associated molecules. In association with DPP4, Seprase / FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. Seprase / FAP has a dual function in tumour progression. The proteolytic activity of Seprase has been shown to promote cell invasiveness towards the ECM and also to support tumour growth and proliferation. Seprase / FAP may have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.
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