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O-glycosylation and N-glycosylation in MUC-1 contribute to the formation of mucin. [14] MUC-1 is a transcriptional coactivator involved in the activity and stabilization of enzymes and transcription of metabolic functions. MUC-1 regulates tyrosine kinase signaling receptors, which promote synthesis of biosynthetic intermediates used in cell ...
Mucin genes encode mucin monomers that are synthesized as rod-shaped apomucin cores that are post-translationally modified by exceptionally abundant glycosylation. The dense "sugar coating" of mucins gives them considerable water-holding capacity and also makes them resistant to proteolysis , which may be important in maintaining mucosal barriers.
In this test, acetic acid is added to the synovial fluid specimen. In a normal specimen, this should lead to a congealing of the hyaluronic acid, forming a 'mucin clot.' If inflammation is present, a mucin clot is not formed (the hyaluronic acid is degraded). [21] Lactate is elevated in septic arthritis, usually above 250 mg/dL.
MUC1 is a member of the mucin family and encodes a membrane bound, glycosylated phosphoprotein. MUC1 has a core protein mass of 120-225 kDa which increases to 250-500 kDa with glycosylation. It extends 200-500 nm beyond the surface of the cell. [7] The protein is anchored to the apical surface of many epithelia by a transmembrane domain. Beyond ...
Mucin-1 kidney disease (MKD) is due to a mutation within the MUC1 gene, which is located on chromosome 1. [12] The mucin-1 protein is involved in the creation of a mucus-like substance that coats the surface of different small tubules in the body, it is expressed on distal tubular cells in the kidney. Mucin-1 kidney disease (MKD) is caused by a ...
Pseudomyxoma peritonei (PMP) is a clinical condition caused by cancerous cells (mucinous adenocarcinoma) that produce abundant mucin or gelatinous ascites. [1] The tumors cause fibrosis of tissues and impede digestion or organ function, and if left untreated, the tumors and mucin they produce will fill the abdominal cavity.
[1] Another use is in surgical pathology where it can identify mucin. This is helpful, for example, in determining if the cancer is a type that produces mucin. Example would be to distinguish between high grade Mucoepidermoid Carcinoma of the parotid, which stains positive vs Squamous Cell Carcinoma of the parotid which does not.
Mucin 16 is a membrane associated mucin that possesses a single transmembrane domain. [9] A unique property of MUC16 is its large size. MUC16 is more than twice as long as MUC1 and MUC4 and contains about 22,000 amino acids, making it the largest membrane-associated mucin. [10] MUC16 is composed of three different domains: [11] An N-terminal domain