Calcium-independent lectin displaying mannose-binding specificity and able to maintain carbohydrate recognition activity in an acidic environment. May be involved in inflammatory and metaplastic responses of the gastrointestinal epithelium.
Regenerating islet-derived protein 4, also known as REG-like protein, REG4, GISP and RELP, a member of the regenerating gene family belonging to the calcium (C-type) dependent lectin superfamily, has been found to be involved in malignancy in several different organs including the stomach, colorectum, pancreas and prostate. It is highly expressed in the gastrointestinal tract and markedly up-regulated in colon adenocarcinoma, pancreatic cancer, gastric adenocarcinoma, and inflammatory bowel disease. Expression of the Reg4 in different cell types has been associated with regeneration, cell growth and cell survival, cell adhesion and resistance to apoptosis. REG4 protein overexpression is associated with an unfavorable response to preoperative chemoradiotherapy and may be used as a predictive biomarker clinically. REG4 may play an important role in the development and progression of colorectal cancer, as well as in intestinal morphogenesis and epithelium restitution.
Renin-1, also known as Ren-1, Angiotensinogenase and Kidney renin, is a member of thepeptidase A1 family. Renin-1 is synthesized by the juxtaglomerular cells of the kidney in response to decreased blood pressure and sodium concentration. androgen and thyroid hormones influence levels of Renin-1 in mouse submandibular gland (SMG) primarily by regulating the amount of Renin-1 mRNA available for translation. Renin-1 is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. It is expressed at relatively low levels in mouse SMG and kidney. Ren-2 is expressed at high levels in the mouse SMG and at very low levels, if at all, in the kidney. Ren-1 and Ren-2 are closely linked on mouse chromosome 1, show extensive homology in coding and noncoding regions and provide a model for studying the regulation of gene expression.
Mouse Renin, also known as Renin-1,is a member of the peptidase A1 amily. Renin is synthesized by the juxtaglomerular cells of the kidney in response to decreased blood pressure and sodium concentration. It cleaves angiotensinogen to generate angiotensin I, which can be further converted by angiotensin converting enzyme (ACE) to angiotensin II. Angiotensin II is the active molecule of the reninangiotensin system that acts by binding to angiotensin receptors type 1 and 2 (AT1 and AT2),and has direct pathophysiological effects on the heart and peripheral vasculature. After secretion, inactive prorenin can be proteolytically activated by trypsin, cathepsin B, or other proteinases.
RCN3 belongs to the CREC family which contains multiple EF-hand Ca2+-binding proteins localized to the secretory pathway. RCN3 sequence is characterized by the presence of five Arg-Xaa-Xaa-Arg motifs, which represents the target sequence of subtilisin-like proprotein convertases(SPCs). SPCs are a family of seven structurally related serine endoproteases that are involved in the proteolytic activation of proproteins.RCN3 is transiently associated with proPACE4, but not with mature PACE4. Inhibition of PACE4 maturation by a Ca2+ ionophore resulted in accumulation of the proPACE4-RCN-3 complex in cells. It has been proposed that elective and transient association of RCN3 with the precursor of PACE4 plays an important role in the biosynthesis of PACE4.
Resistin, also known as adipocyte-specific secretory factor (ADSF) and found in inflammatory zone 3 (FIZZ3), is a member of a family of secreted cysteine-rich peptide hormones that also includes Resistin-like molecules RELM alpha, beta, and gamma. These molecules play important roles in inflammation, glucose metabolism, and insulin resistance. Mature Mouse Resistin is a 12 kDa protein with an N-terminal alpha-helical domain and a C-terminal beta-sandwich domain that is stabilized by multiple intrachain disulfide bonds. Resistin circulates as noncovalent trimers and disulfide-linked hexamers, with an the trimeric form showing greater bioactivity. Resistin can also form multimers with an RELM beta. Mature Mouse Resistin shares 56% and 72% amino acid (aa) sequence identity with an Human and rat Resistin, respectively. It shares 34%-42% aa sequence identity with an Mouse RELM alpha, beta, and gamma. In rodents, Resistin is expressed by adipocytes and in the pituitary and arcuate nucleus of the hypothalamus. It is upregulated during adipogenesis, in obesity, and by insulin or a high carbohydrate diet. This is in contrast to Human Resistin which is produced by macrophages and monocytes but not by adipocytes. Mouse Resistin induces proinflammatory molecule production in adipocytes and promotes hepatic gluconeogenesis and insulin resistance. Human Resistin promotes lipolysis by Human and Mouse adipocytes, but Mouse Resistin does not promote lipolysis by adipocytes of either species. Both Mouse and Human Resistin promote vascular endothelial cell sprouting in vitro and inflammatory reactions in vivo.
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